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madl@bjmu.edu.cn ¼° dlma@263.net

References

1. Cai Y, Gao Y, Sheng Q et al. Characterization and potential function of a novel testis-specific nucleoporin BS-63. Mol Reprod Dev. 2002;61:126-134.£¨Ò½¿ÆÔº»ù´¡Ëù£©

Abstract: A 1933 bp cDNA fragment, coding a truncated testis-specific novel nucleoporin, was isolated from a human testis lambdaZAPII cDNA library, designated as BS-63 and assigned GenBank accession number: U64675. By applying the methods of rapid amplification of cDNA ends (5' RACE) and PCR, a full-length BS-63 cDNA composed of 5475 bp was obtained. BS-63 cDNA contained an open reading frame consisting of 1765 codons and XFXFG or GLFG repetitive sequence motifs. These repetitive motifs are structural characteristic of nucleoporins. BS-63 cDNA has high homology with Nup358/Ran BP2. A 1599 bp fragment, corresponding to the C- terminus of BS-63 cDNA, was prepared and expressed in E. coli BL21(DE3). The recombinant product was purified by affinity chromatography and SDS-PAGE and polyclonal antibodies raised. In rat testis section, the BS-63 protein was localized at the sites of nuclear pores in spermatids by immuno-gold transmission electron microscopy and on the nuclear membrane of Triton X-treated sperm by colloidal silver immuno-gold scanning electron microscopy. The recombinant BS-63 protein can be phosphorylated in vitro with PKC and p34(cdc2). A yeast two- hybrid system was used to screen a mouse testis cDNA library to identify proteins capable of interacting with BS-63. Using the 1.6 kb cDNA fragment as bait, the following interacting proteins were identified: Ran, transportin (karyopherin beta2), two proteins related to the nucleocytoplasmic transporter and aF10 protein. The latter protein is a putative transcriptor containing a cysteine-rich N- terminus, a LAP/PHD finger, a leucine zipper domain and a glutamine- rich C-terminus. Also it is highly expressed in murine testis and is located in the cell nucleus and cytoplasm. The interaction of BS-63 with aF10 (696-1001aa) was validated by surface plasmon resonance and by affinity precipitation combined with Western blot. aF10 (696-1001aa) interacted in vitro with BS-63 extracted from rat testis germ cells. It is hypothesized that BS-63 is a testis-specific nucleoporin and possibly acts as a docking site and a cotransporter of Ran and transportin. The complex performs the task of a carrier system in transporting aF10 into the nucleus of germ cells during spermiogenesis

2. Cao J, Zheng S, Zheng L et al. A novel serine protease SNC19 associated with human colorectal cancer. Chin Med J (Engl ). 2001;114:726-730.£¨Õã½­´óѧ£©

Abstract: OBJECTIVE: To study the structure and function of a novel serine protease gene associated with human colorectal cancer SNC19. METHODS: The cDNA sequence was determined by both manual and automatic sequencing techniques. The full length cDNA sequence was obtained by the 5'-Rapid Amplification of cDNA Ends technique and web-based analysis. Open reading frame analysis and protein function prediction were also performed. Northern blot was used to detect the expression of SNC19 in various human normal tissues and tumor cell lines. Fluorescent in situ hybridization combined with fluorescent R-banding technique was employed to map the SNC19 gene on human chromosome. RESULTS: Full length SNC19 cDNA, size 3152 bp, encodes a protein highly homologous to a mouse serine protease epithin. In normal human tissues, high SNC19 expression levels were observed in the kidney, pancreas, prostate, small intestine and colon; moderate SNC19 expression levels were observed in the placenta, lung, liver, spleen thymus, testis and peripheral blood lymphocytes; and extremely low expression levels were observed in the heart, brain, skeletal muscle and ovary. In tumor cell lines, colorectal cancer cells SW480, SW620, SW1116 and Colo205, breast cancer cell Bcap37 and gastric cancer cells MKN28 and SGC7901 showed high levels of SNC19 expression; cervical cancer cell HeLa-S3, lung cancer PAA, oral epithelial cancer cell KB and lymphoma cell Raji showed moderate levels of SNC19 expression; and tongue squamous cancer cell Tca8113, leukemia cells HL-60, K562, MOLT-4, lung cancer cell A549 and melanoma cell G361 showed very low levels of SNC19 expression. SNC19 was mapped to human chromosome 11q24-25. CONCLUSION: SNC19 encodes a novel human serine protease with 855 amino acid residues. As a novel serine protease associated with human colorectal cancer, the expression of SNC19 in various tissues and cell lines may have very important impact on their phenotypes and biological behaviors

3. Cao X, Zhang W, Wan T et al. Molecular cloning and characterization of a novel CXC chemokine macrophage inflammatory protein-2 gamma chemoattractant for human neutrophils and dendritic cells. J Immunol. 2000;165:2588-2595.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: Chemokines play important roles in leukocyte trafficking as well as function regulation. In this study, we described the identification and characterization of a novel CXC chemokine from a human dendritic cell (DC) cDNA library, the full-length cDNA of which contains an open reading frame encoding 111 aa with a putative signal peptide of 34 aa. This CXC chemokine shares greatest homology with macrophage inflammatory protein (MIP)-2alphabeta, hence is designated as MIP- 2gamma. Mouse MIP-2gamma was identified by electrocloning and is highly homologous to human MIP-2gamma. Northern blotting revealed that MIP- 2gamma was constitutively and widely expressed in most normal tissues with the greatest expression in kidney, but undetectable in most tumor cell lines except THP-1 cells. In situ hybridization analysis demonstrated that MIP-2gamma was mainly expressed by the epithelium of tubules in the kidney and hepatocytes in the liver. Although no detectable expression was observed in freshly isolated or PMA-treated monocytes, RT-PCR analysis revealed MIP-2gamma expression by monocyte- derived DC. Recombinant MIP-2gamma from 293 cells is about 9.5 kDa in size and specifically detectable by its polyclonal Ab developed by the immunization with its 6His-tagged fusion protein. The eukaryotically expressed MIP-2gamma is a potent chemoattractant for neutrophils, and weaker for DC, but inactive to monocytes, NK cells, and T and B lymphocytes. Receptor binding assays showed that MIP-2gamma does not bind to CXCR2. This implies that DC might contribute to the innate immunity through the production of neutrophil-attracting chemokines and extends the knowledge about the regulation of DC migration

4. Chang MS, Huang CJ, Chen ML et al. Cloning and characterization of hMAP126, a new member of mitotic spindle-associated proteins. Biochem Biophys Res Commun. 2001;287:116-121.£¨Ì¨ÍåMackay Memorial Hospital£©

Abstract: One novel gene product, hMAP126, was demonstrated to interact with p29 in the yeast two-hybrid assay. The full-length cDNA of hMAP126 has been obtained and encodes a protein of 1120 amino acids. Multiple tissue Northern blot analysis showed that hMAP126 was abundantly expressed in the testis. Polyclonal antiserum against hMAP126 was raised and affinity-purification of anti-hMAP126 antibodies was performed. The subcellular distribution of hMAP126 was localized to the mitotic spindle. Furthermore, hMAP126 was identified to be post-translationally modified and phosphorylated by p34(cdc2) kinase in vitro. Taken together, we have isolated a novel protein, hMAP126, which may be involved in the functional and dynamic regulation of mitotic spindles

5. Chang NC, Hung SI, Hwa KY et al. A macrophage protein, Ym1, transiently expressed during inflammation is a novel mammalian lectin. J Biol Chem. 2001;276:17497-17506.£¨Ì¨ÍåÑôÃ÷´óѧ£©

Abstract: Oral infections of mice with Trichinella spiralis induce activation of peritoneal exudate cells to transiently express and secrete a crystallizable protein Ym1. Purification of Ym1 to homogeneity was achieved. It is a single chain polypeptide (45 kDa) with a strong tendency to crystallize at its isoelectric point (pI 5.7). Co- expression of Ym1 with Mac-1 and scavenger receptor pinpoints macrophages as its main producer. Protein microsequencing data provide information required for full-length cDNA cloning from libraries constructed from activated peritoneal exudate cells. A single open reading frame of 398 amino acids with a leader peptide (21 residues) typical of secretory protein was deduced and later deposited in GenBank (accession number M94584) in 1992. By means of surface plasmon resonance analyses, Ym1 has been shown to exhibit binding specificity to saccharides with a free amine group, such as GlcN, GalN, or GlcN polymers, but it failed to bind to other saccharides. The interaction is pH-dependent but Ca2+ and Mg2+ ion-independent. The binding avidity of Ym1 to GlcN oligosaccharides was enhanced by more than 1000-fold due to the clustering effect. Specific binding of Ym1 to heparin suggests that heparin/heparan sulfate may be its physiological ligand in vivo during inflammation and/or tissue remodeling. Although it shares approximately 30% homology with microbial chitinases, no chitinase activity was found associated with Ym1. Genomic Southern blot analyses suggest that Ym1 may represent a member of a novel lectin gene family

6. Chen D, Shou C. Molecular cloning of a tumor-associated antigen recognized by monoclonal antibody 3H11. Biochem Biophys Res Commun. 2001;280:99-103.£¨±±¾©Ö×ÁöËù£©

Abstract: Monoclonal antibody (MAb) 3H11 can bind specifically to different cancer cells from different tissues. MAb 3H11 labeled with radioactive isotopes has been used clinically to detect primary cancer and metastatic cancer. Molecular cloning of the antigen recognized by MAb 3H11 is important in studying tumor occurrence and in developing new biotherapy for cancer. Using MAb 3H11, we screened cDNA library made from the human gastric cancer cell line MGC 803, which reacts with MAb 3H11, and isolated one positive clone specifically recognized by the antibody. The insert cDNA fragment was 0.5 kb. After recombining with glutathione-S-transferase expression vector pGEX-4T, the cDNA fragment could be expressed into a fusion protein that specifically reacted with MAb 3H11. Moreover, the fusion protein could competitively inhibit MAb 3H11 binding to MGC 803 cells. Based on the nucleotide sequence of the cDNA fragment, the full length of the cDNA (2156 bp) was obtained by Rapid-Amplification-cDNA-End (RACE) and nested PCR. Its reading frame was 1767 bp encoding a protein of 589 amino acids. Sequence analysis indicated that there is no highly homologous gene in the GenBank. Northern blot and RT-PCR showed that the mRNA of MAb 3H11 antigen was extensively distributed in embryonic tissue and in different cancerous tissues, but not in corresponding normal tissues. Moreover, in producing antibodies to the antigen expressed prokaryotically, we found that the immunogenicity of the antigen was low in mammalian. Thus we believe that this novel antigen acts as an expression regulator in embryo cells and regains expression in tumor cells. In addition, this antigen is characterized by low differentiation and high proliferation. Molecular function of the antigen needs to be investigated

7. Chen J, Liu B, Liu Y et al. A novel gene IC53 stimulates ECV304 cell proliferation and is upregulated in failing heart. Biochem Biophys Res Commun. 2002;294:161-166.£¨Ò½¿ÆÔº¸·ÍâÒ½Ôº£©

Abstract: C53, cloned from rat brain cDNA library, can bind to p35, the precursor of activator of Cdk5. A novel gene with 84% homolog to C53, named IC53, was cloned from our 5300 EST database of human aorta cDNA library (GenBank Accession No. AF110322). Computational analysis showed that IC53 cDNA is 2538 bp long, encoding 419 amino acids, mapped to chromosome 17q21.31 with 12 exons, ubiquitously expressed in 12 tested normal tissues and 8 tumor cell lines from MTN membranes and vascular endothelial cells by Northern blot and in situ hybridization, and upregulated in the rat models of subacute heart failure and chronic ischemic heart failure by left coronary ligation. Stable transfection of IC53 stimulates ECV304 cell proliferation by 2.1-fold compared to cells with empty vector (P<0.05). The results support that IC53 is a novel gene, mainly expressed in vascular endothelial cells and mediates cell proliferation

8. Chen J, Yu L, Li D et al. Human CRYL1, a novel enzyme-crystallin overexpressed in liver and kidney and downregulated in 58% of liver cancer tissues from 60 Chinese patients, and four new homologs from other mammalians. Gene. 2003;302:103-113.£¨¸´µ©´óѧ£©

Abstract: Lambda-crystallin is a composition of lens in rabbit and hare. It contains the putative NAD- or FAD-binding domain, which is named as HCDH domain in 3-hydroxyacyl-CoA dehydrogenase. In our attempt to search for genes differentially expressed between liver cancer tissues and normal tissues, human CRYL1 (crystallin, lambda 1) was identified. It was downregulated in 58% of 60 Chinese HCC tissue samples. The putative protein encoded by CRYL1 shares 83% identity with rabbit lambda-crystallin and contains two HCDH domains. Interestingly, CRYL1 mRNA level is remarkably high in liver and kidney, while it is extremely low in peripheral blood leukocyte and thymus. The CRYL1mRNA levels in liver and kidney are about 1.6 and 1.2 times the total amount of that in other 14 tissues, respectively. Both the special expression pattern and the putative HCDH structure of CRYL1 suggested that the protein may be of the similar function of 3-hydroxyacyl-CoA dehydrogenase. To further understand the lambda-crystallin protein family, we cloned four novel mammalian homologs from mouse, rat, bovine and pig. The unrooted phylogenetic tree of this protein family including human and other 26 species was drawn to analyse their evolutionary relationship. In addition, human CRYL1 was mapped to chromosome 13q12.11 and mouse Cryl1 to chromosome 14 between marker D14Mit83 and D14Mit260

9. Chen J, Ji C, Gu S et al. Isolation and identification of a novel cDNA that encodes human yrdC protein. J Hum Genet. 2003;48:164-169.£¨¸´µ©´óѧ£©

Abstract: In the course of detecting the interaction protein of RBBP10 by yeast two-hybridization, we isolated a novel cDNA that encodes a putative human protein with yrdC domain. It is named human yrdC protein. Because the cDNA contains an open reading fragment (ORF) without a 5' in- frame stop codon, 5' RACE and 3' RACE were proceeded to produce the full- length cDNA. An 1825 bp cDNA was isolated from human placenta, which encodes a putative protein of 279 amino acids. The protein contains a sua5-yciO-yrdC domain. Blast analysis against the human genome database of Genbank revealed that the gene contains five exons, and assigned the gene to human chromosome 1p34.2. A transcript about 2.5 kb is ubiquitously expressed in human tissues. The gene is highly conserved during evolution

10. Chen J, Huang Y, Wu H et al. Molecular cloning and characterization of a novel human J-domain protein gene (HDJ3) from the fetal brain. J Hum Genet. 2003;48:217-221.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: The J-domain is believed to be part of a chaperone involved in protein folding. From a fetal brain cDNA library, we isolated a cDNA of 3249 bp encoding a novel human J-domain protein, which was named as HDJ3. The expression pattern of HDJ3 was examined by reverse transcription/polymerase chain reaction, which suggested that the transcripts were highly expressed in human pancreas and selectively expressed in human brain, lung, liver, skeletal muscle and kidney. The results also showed that a probable splice variant of HDJ3 gene might exist. The HDJ3 gene was located on human chromosome 12q13.1-12q13.2 and consisted of seven exons spanning 8593 bp of the human genome. PSORT analysis indicated that the HDJ3 gene contained a transmembrane domain. The putative protein of the HDJ3 gene was highly homologous to rat dopamine-receptor-interacting protein, suggesting that it was a novel member of the molecular chaperone family and functionally related to dopamine signal transduction

11. Chen JZ, Wang S, Tang R et al. Cloning and identification of a cDNA that encodes a novel human protein with thrombospondin type I repeat domain, hPWTSR. Mol Biol Rep. 2002;29:287-292.£¨¸´µ©´óѧ£©

Abstract: A cDNA was isolated from the fetal brain cDNA library by high throughput cDNA sequencing. The 2390 bp cDNA with an open reading fragment (ORF) of 816 bp encodes a 272 amino acids putative protein with a thrombospondin type I repeat (TSR) domain and a cysteine-rich region at the N-terminus, so it is named hPWTSR. We used Northern blot detected two bands with length of about 3 kb and 4 kb respectively, which expressed in human adult tissues with different intensities. The expression pattern was verified by RT-PCR, revealing that the transcripts were expressed ubiquitously in fetal tissues and human tumor tissues too. However, the transcript was detected neither in ovarian carcinoma GI-102 nor in lung carcinoma LX-1. Blast analysis against NCBI database revealed that the new gene contained at least 5 exons and located in human chromosome 6q22.33. Our results demonstrate that the gene is a novel member of TSR supergene family

12. Chen JZ, Yang QS, Wang S et al. Cloning and expression of a novel retinoblastoma binding protein cDNA, RBBP10. Biochem Genet. 2002;40:273-282.£¨¸´µ©´óѧ£©

Abstract: A 2860-bp cDNA was isolated from a human fetal brain cDNA library by high throughput cDNA sequencing, which encodes a putative protein with 186 amino acids. The putative protein shares 90.7% identity with rat pBOG (3403163) and shares 93.4% identity with human RBBP9 (NP_006597.1). A conserved RB binding domain, L x C x E, located between residue 63 and 68 was recognized. Therefore, it was named RBBP10. Mapviewer analysis locates it on human chromosome 20q11.22. RBBP10 spans about 9.6 kb of the genome and consists of six exons and five introns. RT-PCR revealed that the gene was expressed widely in various human tissues, and the expression level is somewhat higher in tumor tissues than in normal tissues. But subsequent sequencing analysis did notfound any mutation of this in tumor tissues. The COS 7 cell transfected with the ORF of RBBP10 showed that the protein was distributed both in the cytoplasm and in the nucleus. Our results suggest that RBBP10 is the orthologue of the rat BOG gene (AF025819) and a paralogue of human RBBP9 (AF039564)

13. Chen T, Han Y, Yang M et al. Rab39, a novel Golgi-associated Rab GTPase from human dendritic cells involved in cellular endocytosis. Biochem Biophys Res Commun. 2003;303:1114-1120.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: Rab GTPases are Ras-like small molecular weight GTP binding proteins that are involved in various steps along the exocytic and endocytic pathways. Here we report that Rab39, a novel Rab protein, is a Golgi- associated protein involved in endocytosis of HeLa cells. Full-length cDNA of Rab39 contains 1251bp with an open reading frame (ORF) of 636bp, which is predicted to encode a 211 aa protein. By blast analysis of Rab39 cDNA and protein sequence with homologues, we find that Rab39 may be a short variant of Rab34. Rab39 contains conserved motifs involved in phosphate/guanosine binding and a microbody C-terminal targeting signal. RT-PCR analysis indicates that Rab39 is mainly detected in epithelial cell lines, and Northern blot analysis shows that Rab39 is expressed ubiquitously in human tissues. By using FITC- BSA as an endocytic tracer, we show that Rab39 can facilitate endocytosis in HeLa cells when expressed either transiently or stably. Confocal microscopy examination of Rab39 subcellular localization suggests that Rab39 is associated with Golgi-associated organelles. Our findings demonstrate that Rab39 is a novel Rab GTPase involved in cellular endocytosis

14. Cheng C, Xu J, Ye X et al. Cloning, expression and characterization of a novel human VMP gene. Mol Biol Rep. 2002;29:281-286.£¨¸´µ©´óѧ£©

Abstract: We report here cloning and characterization of a novel human gene, termed VMP, which is a vesicular membrane protein. RT-PCR analysis shows that VMP is expressed exclusively in brain of the 16 tissues examined, suggesting that it is a neuron-specific membrane protein. The cDNA encodes 195 amino acid with a putative molecular weight of about 24 KDa. VMP contains two putative membrane spanning domains and a hydrophilic tail homologous to the microtubule-binding domain of MAPs. So it is speculated that VMP may associated with microtubules through its C-terminal and plays an important role in vesicular organelles transport and nerve signals

15. Cheng H, Ma Y, Ni X et al. cDNA cloning and expression analysis of a novel human F-box only protein. Mol Cells . 2002;14:56-59.£¨¸´µ©´óѧ£©

Abstract: F-box proteins are an expanding family of eukaryotic proteins that are characterized by an approximately 40 amino acid motif. Some F-box proteins are critical for the controlled degradation of cellular regulatory proteins. During a large-scale sequencing analysis of a human fetal brain cDNA library, we isolated a cDNA clone that encodes a novel F-box protein. It showed a 90.0% identity with the previously isolated mouse F-box protein16 at the amino acid level. Northern blot analysis showed no detectable expression, while reverse transcription- polymerase chain reaction analysis indicated that FBXO16 was expressed in the heart, spleen, and colon. By mapping, we localized the FBXO16 gene to the human chromosome 8p12. The FBXO16 gene consisted of 9 exons that spanned 67,816 bp of human genomic DNA

16. Cheng H, Ma Y, Ni X et al. Isolation and characterization of a human novel RAB (RAB39B) gene. Cytogenet Genome Res. 2002;97:72-75.£¨¸´µ©´óѧ£©

Abstract: Rab proteins are small-molecular-weight GTPases that control vesicular trafficking in eukaryotic cells. During the large-scale sequencing analysis of a human fetal brain cDNA library, we isolated a cDNA clone encoding a novel Rab protein, which showed 74.2% identity with previously isolated Rab39A at the amino acid level. RAB39B was expressed in a variety of human tissues and located in human chromosome Xq28. It consisted of two exons spanning 3764 bp of human genomic DNA

17. Cheng H, Ma Y, Ni X et al. Cloning, mapping, and characterization of the human Rab3C gene. Biochem Genet. 2002;40:263-272.£¨¸´µ©´óѧ£©

Abstract: Rab proteins are small molecular weight GTPases that control vesicular traffic in eukaryotic cells. A subset of Rab proteins, the Rab3 proteins are thought to play an important role in regulated exocytosis of vesicles. During the large-scale sequencing analysis of a human fetal brain cDNA library, we isolated a cDNA clone encoding a novel Rab protein, which showed 99% identity with previously isolated bovine Rab3C at the amino acid level It contained four conserved motifs characteristic of the Rab3 family. RT-PCR analysis indicated that human Rab3C was expressed in the human brain, placenta, and lung. By mapping, we localized the Rab3Cgene to human chromosome 5q13. The Rab3C gene consisted of 6 exons spanning more than 310 kb of human genomic DNA. Rab3A, Rab3B, and Rab3D have been mapped to three different chromosomes, suggesting that they are not transcripts of the same gene

18. Cheng H, Gao Q, Jiang M et al. Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3. Int J Biochem Cell Biol. 2003;35:226-234.£¨¸´µ©´óѧ£©

Abstract: Reversible phosphorylation is recognized to be a major mechanism for the control of intracellular events in eukaryotic cells. From a human fetal brain cDNA library, we isolated a cDNA clone encoding a novel dual specificity protein phosphatase, which showed 88% identity with previously reported mouse LMW-DSP3 at the amino acid level. The deduced protein had a single dual-specificity phosphatase catalytic domain, and lacked a cdc25 homology domain. LMW-DSP3 was expressed in the heart, lung, liver, and pancreas, and the expression level in the pancreas was highest. The LMW-DSP3 gene was located in human chromosome 2q32, and consisted of five exons spanning 21kb of human genomic DNA. LMW-DSP3 fused to GST showed phosphatase activity towards p-nitrophenyl phosphate which was optimal at pH 7.0 and 40 degrees C, and the activity was enhanced by Ca(2+) and Mn(2+). The phosphatase activity of LMW-DSP3 was inhibited by orthovanate. LMW-DSP3 showed phosphatase activity toward oligopeptides containing pSer/Thr and pTyr, indicating that LMW-DSP3 is a protein phosphatase with dual substrate specificity

19. Cheng LJ, Li JM, Chen J et al. NYD-SP16, a novel gene associated with spermatogenesis of human testis. Biol Reprod. 2003;68:190-198.£¨ÄϾ©Ò½¿Æ´óѧ£©

Abstract: By hybridizing human adult testis cDNA microarrays with human adult and embryo testis cDNA probes, a novel human testis gene NYD-SP16 was identified. NYD-SP16 expression was 6.44-fold higher in adult testis than in fetal testis. NYD-SP16 contains 1595 base pairs (bp) and a 762- bp open reading frame encoding a 254-amino acid protein with 73% amino acid sequence identity with the mouse testis homologous protein. The NYD-SP16 gene was localized to human chromosome 5q14. The deduced structure of the NYD-SP16 protein contains one transmembrane domain, which was confirmed by GFP/NYD-SP16 fusion protein expression in the cytomembrane of the transfected human choriocarcinoma JAR cells, suggesting that it is a transmembrane protein. Multiple tissue distribution indicated that NYD-SP16 mRNA is highly expressed in the testes and pancreas, with little or no expression elsewhere. Further analysis of abnormal expression in infertile male patients revealed complete absence of NYD-SP16 in the testes of patients with Sertoli- cell-only syndrome and variable expression in patients with spermatogenic arrest. Homologous gene expression in mouse testis was confirmed in spermatogenic cells by in situ hybridization. The results of cDNA microarray, in situ hybridization, and semiquantitative polymerase chain reaction in mouse testis of different stages indicated that NYD-SP16 expression is developmentally regulated. These results suggest that the putative NYD-SP16 protein may play an important role in testicular development/spermatogenesis and may be an important factor in male infertility

20. Cui W, Yu L, He H et al. Cloning of human myeloid-associated differentiation marker (MYADM) gene whose expression was up-regulated in NB4 cells induced by all-trans retinoic acid. Mol Biol Rep. 2001;28:123-138.£¨¸´µ©´óѧ£©

Abstract: A full-length cDNA of 3192 bp isolated from human bone marrow cDNA library was predicted an ORF encoding 298 amino acids. The deduced protein, containing seven putative transmembrane segments and sharing 75.8% amino acid identity with mouse Myadm protein, was named as human MYADM. The results of Northern blot analysis showed that MYADM was ubiquitously expressed in 15 of 16 adult tissues tested, except thymus. To determine whether the novel human gene was involved in hematopoietic differentiation process as mouse Myadm did, we examined the mRNA expressive abundance of this gene between normal bone marrow cells and peripheral blood leukocytes, and detected the expression change in NB4 cells induced by all-trans retinoic acid at different induce time by the semi-quantitative RT-PCR. The results showed that the expression of the novel gene was not only significantly higher in peripheral blood leukocytes than in bone marrow cells, but also significantly up- regulated when the NB4 cells(derived from a patient with acute promyelocytic leukemia) were induced by all-trans retinoic acid (ATRA) for 48hr. It is suggested that human MYADM was also associated with the differentiation of hematopoietic cells or acute promyelocytic leukemia cells. In addition, MYADM was mapped to human chromosome 19q 13.33-q 13.4 by Radiation Hybrid mapping, and it consists of 3 exons and 2 introns and spans a 7.1-Kb genomic region

21. Cui Y, Yu L, Gong R et al. Cloning and tissue expressional characterization of a full-length cDNA encoding human neuronal protein P17.3. Biochem Genet. 1999;37:175-185.£¨¸´µ©´óѧ£©

Abstract: A full-length cDNA of 595 bp was isolated from a human fetal brain cDNA library. It contains an open reading frame encoding 153 amino acids, with an 18-bp 5'UTR and a 118-bp 3'UTR in which there is an atypical polyadenylation signal (ATTAAA). The calculated molecular weight of the deduced protein is 17.3 kU. The predicted isoelectric point is 4.89. On account of its high homology to mouse neuronal protein NP15.6 (81.2% identity), the deduced protein was named neuronal protein 17.3 (NP17.3). When its secondary structure was examined by the GGBSM program of PCGENE software, it was found that 32.6 and 15.0% of its amino acids are involved in forming alpha-helices and beta-sheets, respectively. Examined with the PESTFIND program, a typical PEST region found in rapidly degraded proteins was found between residue 48 and residue 68

22. Cui Y, Wang J, Zhang X et al. ECRG2, a novel candidate of tumor suppressor gene in the esophageal carcinoma, interacts directly with metallothionein 2A and links to apoptosis. Biochem Biophys Res Commun. 2003;302:904-915.£¨Ò½¿ÆÔºÖ×ÁöËù£©

Abstract: Esophageal cancer related gene 2 (ECRG2) is a novel candidate of the tumor suppressor gene identified from human esophagus. To study the biological role of the ECRG2 gene, we performed a GAL4-based yeast two- hybrid screening of a human fetal liver cDNA library. Using the ECRG2 cDNA as bait, we identified nine putative clones as associated proteins. The interaction of ECRG2 and metallothionein 2A (MT2A) was confirmed by glutathione S-transferase pull-down assays in vitro and co- immunoprecipitation experiments in vivo. ECRG2 co-localized with MT2A mostly to nuclei and slightly to cytoplasm, as shown by confocal microscopy. Transfection of ECRG2 gene inhibited cell proliferation and induced apoptosis in esophageal cancer cells. In the co-transfection of ECRG2 and MT2A assays, cell proliferation was inhibited and apoptosis was slightly induced compared with control groups. When we used antisense MT2A to interdict the effect of MT2A, the inhibition of cell proliferation and induction of apoptosis were significantly enhanced. When we used antisense ECRG2 to interdict the effect of ECRG2 in the group of Bel7402 cells co-transfected with ECRG2 and MT2A, the inhibition of cell proliferation and induction of apoptosis disappeared. The results provide evidence for ECRG2 in esophageal cancer cells acting as a bifunctional protein associated with the regulation of cell proliferation and induction of apoptosis. ECRG2 might reduce the function of MT2A on the regulation of cell proliferation and induction of apoptosis. The physical interaction of ECRG2 and MT2A may play an important role in the carcinogenesis of esophageal cancer

23. Deng Y, Wang Z, Gu S et al. Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002;13:301-306.£¨¸´µ©´óѧ£©

Abstract: There are three types of NAD(P)(+)-dependent alcohol dehydrogenase: "medium-chain" zinc-containing enzymes, "short-chain" zinc-lacking enzymes and iron-activated enzymes. Although the medium-chain family and the short-chain family have been characterized in human, the iron- activated alcohol dehydrogenase family seems to exist only in microbial organisms. We have now cloned and characterized an iron-activated alcohol dehydrogenase gene, Fe-containing alcohol dehydrogenase 1 (ADHFe1) in human. The cDNA was isolated from the human fetal brain cDNA library. It contains a long open reading frame, which is not homologous with the other alcohol dehydrogenases isoenzymes characterized in human. The hypothetical alcohol dehydrogenase does, however, show strong homology to the iron-activated alcohol dehydrogenases from microbial organisms. Northern blotting analysis only detected expression in adult liver tissue. At least two different splicing variants were screened by PCR using the multiple tissue cDNA panels as templates

24. Di Y, Li J, Fang J et al. Cloning and characterization of a novel gene which encodes a protein interacting with the mitosis-associated kinase-like protein NTKL. J Hum Genet. 2003.£¨¸´µ©´óѧ£©

Abstract: NTKL is an evolutionarily conserved kinase-like protein. The cell-cycle- dependent centrosomal localization of NTKL suggested that it was involved in centrosome-related cellular function. The mouse NTKL protein is highly homologous with human NTKL. A novel mouse protein was identified as an NTKL-binding protein (NTKL-BP1) by yeast two-hybrid screening, and the full-length cDNA was amplified based on the result of a sequence data analysis cloning strategy. The full-length cDNA sequence of the NTKL-BP1 gene consists of 2,537 bp, which encode 368 amino acids. A database search revealed that homologues of NTKL-BP1 exist in different organisms, including Arabidopsis thaliana, Drosophila melanogaster, Plasmodium falciparum, Geobacter metallireducens, Anopheles gambiae and human. It suggests that NTKL-BP1 is an evolutionarily conserved protein. The expression of NTKL-BP1 was observed in multiple normal mouse tissues. The interaction of the two proteins was confirmed by co-immunoprecipitation. Moreover, immunofluorescent staining indicated that NTKL and NTKL-BP1 were all localized in the cytoplasm

25. Fan Y, Yu L, Tu Q et al. Molecular cloning, genomic organization, and mapping of beta 4GalT-VIb, a brain abundant member of beta 4-galactosyltransferase gene family, to human chromosome 18q12.1. DNA Seq. 2002;13:1-8.£¨¸´µ©´óѧ£©

Abstract: In the present study, a brain abundant member of beta 4- galactosyltransferase gene family with an open reading frame encoding 343 amino acids was cloned and identified from a human leukemia cell cDNA library. The putative protein sequence is about 94.8 and 94.2% identical to the 382-amino-acid mouse and rat beta 4- galactosyltransferase respectively and also contains cysteine residues previously shown to be important for the function of the gene family members. This cDNA (tentatively termed beta 4GalT-VIb) is identical to a recently reported cDNA (tentatively termed beta 4GalT-VIa) of human beta 4-galactosyltransferase except lacking one exon, suggesting that these two cDNAs are two different alternative transcripts of the same gene. Northern hybridization showed that the new alternative transcript, beta 4GalT-VIb, is expressed in all 16 human tissues tested with highest level in brain and rich level in testis, thymus and pancreas, whereas weak expression was detected in lung. The beta 4GalT- VIb gene was located to human chromosome 18q12.1 between markers WI- 9180 and SGC35630 by radiation hybrid mapping. The genomic organization and adjacent gene content of beta 4GalT-VIb were identified by comparing its cDNA sequence with three genomic sequences AC017100, AP002474 and AP001336, which showed that beta 4GalT-VIb spans an approximately 58 kb region and is composed of 8 exons. In addition, the most conserved motif composed of 41 residues, LXYX3FGGVSXL(T/S)X2 QFX2INGFPNX(Y/F)WGWGGEDDDX2NR, was defined according to 17 sequences of beta 4GalTs from seven different organisms for the first time

26. Fu Q, Yu L, Liu Q et al. Molecular cloning, expression characterization, and mapping of a novel putative inhibitor of rho GTPase activity, RTKN, to D2S145-D2S286. Genomics. 2000;66:328-332.£¨¸´µ©´óѧ£©

Abstract: The Rho proteins are a class of small molecular GTPases that regulate multiple fundamental cellular processes by mediating the G-protein- coupled receptor signaling pathway. Rhotekin, which is one of the downstream target molecules of Rho with a Rho binding motif class I domain, can inhibit endogenous or RhoGAP-stimulating Rho GTPase activity to regulate the signaling pathway. Here, a novel human cDNA containing an intact open reading frame that encodes 544 amino acids has been identified. As this putative protein shares 84. 6% amino acid identity with mouse Rhotekin, and has a tandem Rho binding domain class 1 and Pleckstrin homology domain, it was regarded as a human homologue of the mouse Rhotekin and assigned a symbol of RTKN. With the human Rhotekin cDNA as a probe, Northern hybridization revealed that a 4.0-kb transcript was expressed at a high level in prostate and at a middle level in 13 of 16 tissues examined, but it cannot be detected in liver and lung tissues. Meanwhile, a 2.4-kb transcript was expressed at a middle level in prostate and another 3.0-kb transcript in kidney. In addition, the RTKN gene was localized to chromosome 2p13 between markers D2S145 at 6.94 cR (LOD > 12) and D2S286 at 8.12 cR (LOD > 9.7) by radiation hybrid panel mapping. Compared with BAC clone AC005041 sequence, there were 12 exons for the RTKN gene and it spanned a 16.5- kb genomic region

27. Gao J, Yu L, Zhang P et al. Cloning and characterization of human and mouse mitochondrial elongation factor G, GFM and Gfm, and mapping of GFM to human chromosome 3q25.1-q26.2. Genomics. 2001;74:109-114.£¨¸´µ©´óѧ£©

Abstract: Similar to the translational system in the cell cytoplasm, the initiation, elongation, and termination of protein synthesis in the mitochondria of eukaryotes are catalyzed by several protein factors. These factors, from the viewpoint of evolution, are more closely related to the corresponding prokaryotic factors than to those in the eukaryotic cytoplasm. In this paper, we isolated two cDNAs coding for human and mouse mitochondrial elongation factor G (GFM and Gfm, respectively). The GFM cDNA, which is 3481 bp in length, predicts a protein of 751 amino acids sharing 84 and 42% identity and 88 and 62% similarity to rat EF-G(mt) and Escherichia coli EF-G, respectively, and 24% identity and 39% similarity to human EF-2, the equivalent of EF-G in the cytoplasm. The mouse Gfm cDNA is 2564 bp and contains an intact open reading frame that encodes 751 amino acids showing 89% sequence identity and 94% similarity to human GFM. Northern blot analysis of human GFM revealed three transcripts of 3.8, 3.4, and 2.9 kb. The first two were expressed at high levels in heart, skeletal muscle, and testis, at moderate levels in liver and kidney, and at low levels in other tissues including brain, placenta, and lung, while the last transcript was expressed only in testis. The relative abundance of GFM was consistent with the observations for human EF-Tu(mt) and EF-Ts(mt), the other two mitochondrial elongation factors, indicating that the three factors were expressed at corresponding levels. The expression pattern of mouse Gfm was also determined, which showed that Gfm was expressed as a 3.0-kb transcript, abundantly in heart, skeletal muscle, kidney, and testis. In addition, GFM was assigned to human chromosome 3q25.1-q26.2 by the radiation hybrid mapping method. The genomic organization of GFM was also analyzed by comparing this cDNA with a genomic DNA sequence (Accession No. AC010936), which showed that GFM contained 18 exons and spanned at least 40 kb

28. Gou DM, Sun Y, Gao L et al. Cloning and characterization of a novel Kruppel-like zinc finger gene, ZNF268, expressed in early human embryo. Biochim Biophys Acta. 2001;1518:306-310.£¨Î人´óѧ£©

Abstract: With the aim of identifying genes involved in early human embryonic development, we have isolated a cDNA clone representing a novel human zinc finger gene ZNF268 from 3 week old human embryo cDNA library using a differential hybridization strategy. The complete cDNA sequence of ZNF268 contained an open reading frame of 2841 nucleotides that encodes a 947 amino acid protein with an N-terminal Kruppel-associated box (KRAB) domain and 24 C-terminal zinc fingers. Northern blot analysis showed that ZNF268 mRNA is mainly expressed in 3-5 week old human embryos suggesting it could play certain roles in the embryogenesis. The gene consists of six exons spanning about 22 kb of genomic DNA. According to the genomic sequence from the HTGS database, the ZNF268 gene is assigned to human chromosome 5

29. Guo L, Jiang M, Ma Y et al. Molecular cloning, mapping and characterization of a human CK1gamma1 gene. Int J Mol Med. 2002;10:227-230.£¨¸´µ©´óѧ£©

Abstract: We isolated and sequenced a cDNA clone coding a human protein kinase CK1 (casein kinase 1) by screening a human fetal brain cDNA library. This new cDNA clone of 1756 bp contained an open reading frame, encoding a protein of 438 amino acids with a molecular weight of 50,272 Da and an isoelectric point of 9.37. The entire amino acid sequence of the novel human CK1 was 94% homologous to that of rat CK1gamma1. Northern blot analysis indicated that the human CK1gamma1 was highly expressed in the liver, skeletal muscle, heart and kidney. Furthermore, the human CK1gamma1 gene was mapped to chromosome 15q22 between STS marker D15S159 and D15S125 by polymerase chain reaction analysis of human/rodent hybrid cell panels

30. Han W, Lou Y, Tang J et al. Molecular cloning and characterization of chemokine-like factor 1 (CKLF1), a novel human cytokine with unique structure and potential chemotactic activity. Biochem J. 2001;357:127-135.£¨±±¾©´óѧҽѧ²¿£©

Abstract: Cytokines are small proteins that have an essential role in the immune and inflammatory responses. The repertoire of cytokines is becoming diverse and expanding. Here we report the identification and characterization of a novel cytokine designated as chemokine-like factor 1 (CKLF1). The full-length cDNA of CKLF1 is 530 bp long and a single open reading frame encoding 99 amino acid residues. CKLF1 bears no significant similarity to any other known cytokine in its amino acid sequence. Expression of CKLF1 can be partly inhibited by interleukin 10 in PHA-stimulated U937 cells. Recombinant CKLF1 is a potent chemoattractant for neutrophils, monocytes and lymphocytes; moreover, it can stimulate the proliferation of murine skeletal muscle cells. These results suggest that CKLF1 might have important roles in inflammation and in the regeneration of skeletal muscle

31. Han W, Ding P, Xu M et al. Identification of eight genes encoding chemokine-like factor superfamily members 1-8 (CKLFSF1-8) by in silico cloning and experimental validation. Genomics. 2003;81:609-617.£¨±±¾©´óѧҽѧ²¿£©

Abstract: TM4SF11 is only 102 kb from the chemokine gene cluster composed of SCYA22, SCYD1, and SCYA17 on chromosome 16q13. CKLF maps on chromosome 16q22. CKLFs have some characteristics associated with the CCL22/MDC, CX3CL1/fractalkine, CCL17/TARC, and TM4SF proteins. Bioinformatics based on CKLF2 cDNA and protein sequences in combination with experimental validation identified eight novel genes designated chemokine-like factor superfamily members 1-8 (CKLFSF1-8). CKLFSF1-8 form gene clusters; the sequence identities between CKLF2 and CKLFSF1-8 are from 12.5 to 39.7%. Most of the CKLFSFs have alternative RNA splicing forms. CKLFSF1 has a CC motif and higher sequence similarity with chemokines than with any of the other CKLFSFs. CKLFSF8 shares 39.3% amino acid identity with TM4SF11. CKLFSF1 links the CKLFSF family with chemokines, and CKLFSF8 links it with TM4SF. The characteristics of CKLFSF2-7 are intermediate between CKLFSF1 and CKLFSF8. This indicates that CKLFSF represents a novel gene family between the SCY and the TM4SF gene families

32. Han ZG, Zhang QH, Ye M et al. Molecular cloning of six novel Kruppel-like zinc finger genes from hematopoietic cells and identification of a novel transregulatory domain KRNB. J Biol Chem. 1999;274:35741-35748.£¨¹ú¼ÒÈËÀà»ùÒò×éÄÏ·½ÖÐÐÄ£©

Abstract: To clone zinc finger genes expressed in hematopoietic system, we designed primers based on conserved Cys(2)/His(2) zinc finger sequences to amplify corresponding domains from mRNA of normal bone marrow and leukemia cell line NB4. DNA fragments of novel zinc finger genes were chosen and used as probe pool to screen cDNA libraries or subject to rapid amplification of cDNA ends in order to obtain full-length cDNA. Six cDNAs including whole open reading frame of zinc finger proteins, named as ZNF191, ZNF253 (BMZF-1), ZNF255 (BMZF-2), ZNF256 (BMZF-3), ZNF257 (BMZF-4), and ZNF254 (BMZF-5) were obtained. All six belong to the Kruppel-like zinc finger gene family, and typical transcriptional regulatory motifs exist in the N-terminal moiety, such as the SCAN box in ZNF191, and the KRAB domains in ZNF253, ZNF254, ZNF256, and ZNF257. A previously undefined sequence nominated as Kruppel-related novel box, which may represent a new transregulatory motif, was revealed at the N terminus of ZNF255. The transregulatory function of non-zinc finger regions of ZNF191, ZNF253, and ZNF255 were addressed in yeast and mammalian cells. The results indicated that ZNF255 might be a conditional transactivator, whereas ZNF253 and ZNF191 displayed a suppressive effect on the transcription in yeast and/or mammalian systems

33. He X, Di Y, Li J et al. Molecular cloning and characterization of CT120, a novel membrane- associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002;297:528-536.£¨ÉϺ£Ö×ÁöËù£©

Abstract: Within the minimum LOH region on chromosome 17p13.3 deleted in hepatocellular carcinoma, a novel human plasma membrane-associated gene, named CT120, was isolated from a human kidney cDNA library using electronical cloning and RACE. The novel gene CT120 consists of 2145bp and encodes a protein with 257 amino acids. Database search revealed that homologs of CT120 exist in different organisms from plant to animal kingdoms, which suggests that CT120 is a highly conserved gene during biological evolution. Different expression patterns of CT120 were observed in many different human normal tissues and in various human tumor cell lines. Transcript of CT120 was not detectable in normal lung tissue, but was abundant in SPC-A-1 (human epithelial-like lung adenocarcinoma) cell line, suggesting that CT120 may be involved in lung cancer development. Subcellular localization analysis showed that CT120 is a novel membrane-associated protein. CT120 can interact with SLC3A2 (member 2 of solute carrier family 3) and GGTL3B (isoform of gamma-glutamyltranspeptidase-like 3) in eukaryotic cells by yeast two-hybrid screen and co-immunoprecipitation assay, which suggested that CT120 may assume very essential physiological functions involved in amino acid transport and glutathione metabolism

34. Hu P, Yu L, Zhang M et al. Molecular cloning and mapping of the brain-abundant B1gamma subunit of protein phosphatase 2A, PPP2R2C, to human chromosome 4p16. Genomics. 2000;67:83-86.£¨¸´µ©´óѧ£©

Abstract: Protein phosphatase 2A (PP2A) is one kind of serine/ threonine protein phosphatase regulating mainly cell growth and division. It comprises three subunits, A, B, and C. The B-subunit is involved in enzyme activity and substrate specificity. The B-subunit family is of great diversity and is divided into three classes, the B1, B2, and B3 subfamilies. Until now, two members of the B1 subfamily, B1alpha and B1beta, have been identified in human. In this report, the third member of the sub-family, B1gamma, was identified, and its cDNA was isolated from a human brain cDNA library. This novel cDNA is 4,120 bp in length and contains an open reading frame (nt 55-1,398) encoding 447 amino acid residues. The putative protein shares 81 and 85% identity with B1alpha (PPP2R2A) and B1beta (PPP2R2B), respectively, and was named PPP2R2C for its high level of homology to the other two isoforms. One remarkable characteristic of this novel gene is that it is highly expressed in brain with a 4.7-kb transcript while it is nearly undetectable in other tissues. In addition, the PPP2R2C gene was localized to human chromosome 4p16 between markers D4S2925 and D4S3007 with 5.45 cR (LOD > 14) and 2.63 cR (LOD > 15) RH distance, respectively, by radiation hybrid panel mapping

35. Huang X, Yuan Z, Chen G et al. Cloning and characterization of a novel ITIM containing lectin-like immunoreceptor LLIR and its two transmembrane region deletion variants. Biochem Biophys Res Commun. 2001;281:131-140.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: A novel full-length cDNA was cloned from human dendritic cells (DC) by subtractive cloning and RACE. The deduced protein is a type II lectin- like membrane protein that contains an ITIM proximal to N terminal and is designated as lectin-like immunoreceptor (LLIR). The gene of LLIR is located in a region of chromosomal 12p13 and shows highest homologous with ASGPR. Two alternatively spliced transmembraneless variants of LLIR were identified by RT-PCR and named as LLIRv1 and LLIRv2. RT-PCR and immunoblotting analysis revealed that LLIR was expressed with much higher level in immature DC than in mature DC. The ITIM in LLIR was demonstrated to bind SHP-1 in HL-60 cell after the tyrosine had been phosphorylated. In addition, the mRNA expression level of LLIRv2 was raised when leukemia cells were induced to differentiate by PMA

36. Huang Y, Tang R, Dai J et al. A novel human hydroxysteroid dehydrogenase like 1 gene (HSDL1) is highly expressed in reproductive tissues. Mol Biol Rep. 2001;28:185-191.£¨¸´µ©´óѧ£©

Abstract: We report the cloning and characterization of a novel human hydroxysteroid dehydrogenase like gene (HSDL1) located on human chromosome 16q24.2. The HSDL1 cDNA is 3407 base pair in length, encoding a 309 amino acid polypeptide related to human 17beta-HSD3. Northern blot reveals that the HSDL1 is highly expressed in testis and ovary. In situ hybridization indicates that the expression of HSDL1 is predominantly increased in the prostate cancer tissue compared with the normal prostate tissue, which suggests that the gene expression is important to the arising of prostate cancer

37. Huang Y, Ying K, Xie Y et al. Cloning and characterization of a novel human leptin receptor overlapping transcript-like 1 gene (LEPROTL1). Biochim Biophys Acta. 2001;1517:327-331.£¨¸´µ©´óѧ£©

Abstract: A new full-length cDNA encoding a novel protein was isolated from our human fetal brain cDNA library. The cDNA consists of 2701 bp and has a putative open reading frame encoding 131 amino acids which possesses a JAK binding site (Pro(46)-Ile-Pro(48) which is preceded by a cluster of hydrophobic residues) and is highly homologous to the leptin receptor gene-related protein (OB-RGRP). Northern blot analysis showed that this new gene is widely expressed in human tissues and radiation hybrid mapping placed the gene to human chromosome 8p21.1-8p21.2

38. Ji CN, Chen JZ, Xie Y et al. A novel cDNA encodes a putative hRALY-like protein, hRALYL. Mol Biol Rep. 2003;30:61-67.£¨¸´µ©´óѧ£©

Abstract: High throughput cDNA sequencing and 5'-rapid amplification of cDNA ends (5'RACE) isolated two cDNAs that shared the same open reading fragment (ORF). Northern blot analysis with the fetal brain mRNA blots detected two transcripts with the length of 3.2 kb and 2.2 kb respectively. The ORF encodes a 291 residues putative protein that shares great homology with hRALY and hnRNPC. So it was named hRALY like protein, hRALYL. Expression pattern was detected by multiple-issue cDNA (MTC) panel based RT-PCR. It revealed that the transcripts of hRALYL were expressed ubiquitously in human tissues with different intensities. The transcript is highest in brain. Blast analysis found the cDNA corresponding to a contig NT_008292, which revealed the gene containing at least 9 exons and located the gene on human chromosome 8q21.13- 8q21.2. hRALYL might be a member of hnRNPC subfamily

39. Jiang C, Yu L, Zhao Y et al. Cloning and characterization of CIS 1b (cytokine inducible SH2- containing protein 1b), an alternative splicing form of CIS 1 gene. DNA Seq. 2000;11:149-154.£¨¸´µ©´óѧ£©

Abstract: JAK-STAT pathway is essential in relaying cytokine signals and plays a vital role in cellular responses such as proliferation, differentiation and immunity. Some members of a recently found cytokine-inducible SH2 protein (CIS, =SOCS or SSI) family have proved to have negative effects on modulating JAK-STAT signaling pathway. In the present study, a novel human cDNA (CIS1b) which proved to be a variant of CIS1 gene was isolated by screen human placenta lambda gt11 cDNA library and 5'-rapid amplification of cDNA ends (RACE). Furthermore, the gene structure of CIS1 was determined by comparing the cDNA sequences of CIS1 and CIS1b to the genomic sequence in human chromosome 3p21.3. The expression patterns of CIS1b as well as CIS1 were analysed by Northern blot

40. Jiang M, Ma Y, Cheng H et al. Molecular cloning and characterization of a novel human gene (HSPBAP1) from human fetal brain. Cytogenet Cell Genet. 2001;95:48-51.£¨¸´µ©´óѧ£©

Abstract: Rat PASS1 is a novel protein binding specifically to hsp27 and thus plays a role in regulating stress response in the living cell. Here we report on a human homologue of PASS1, encoded by the gene HSPBAP1. The gene was cloned and identified during a large-scale sequencing analysis of a human fetal brain cDNA library. The human protein shared 80% amino acid identity with rat PASS1. According to bioinformatics analysis, the HSPBAP1 gene is located on chromosome 3q21. RT-PCR analysis indicated that HSPBAP1 was abundant in thymus and pancreas but had a ubiquitously low expression pattern in other human adult tissues except for brain where it was absent

41. Jiang M, Ma Y, Ni X et al. Molecular cloning and characterization of a novel human gene (ANP32E alias LANPL) from human fetal brain. Cytogenet Genome Res. 2002;97:68-71.£¨¸´µ©´óѧ£©

Abstract: Leucine-rich acidic nuclear protein (LANP) is a member of the leucine- rich repeats (LRRs) superfamily. Here we report on a human homologue of LANP, encoded by the gene ANP32E (alias LANPL). The gene was cloned and identified during large-scale sequencing analysis of a human fetal brain cDNA library. The human protein shared 70% amino acid identity with rat LANP. According to bioinformatics analysis, ANP32E is located on chromosome 1q22. RT-PCR analysis indicates that ANP32E was expressed in human peripheral blood leukocytes, colon, small intestine, prostate, thymus, spleen, skeletal muscle, liver and kidney

42. Jiang Y, Wan T, Chen G et al. DC-CLM, a cadherin-like molecule cloned from human dendritic cells, inhibits growth of breast cancer cells. J Cancer Res Clin Oncol. 2003;129:57-64.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: PURPOSE: To identify the characteristics and function of a cadherin- like molecule, cloned from a human dendritic cell (DC) cDNA library and designated DC-derived cadherin-like molecule (DC-CLM). METHODS: The mRNA expression of DC-CLM in tissues and cells was analyzed by Northern blot and RT-PCR, respectively. In order to express DC-CLM in target cells, we constructed a pcDNA3.1/DC-CLM expression vector and transfected it into MCF-7 human breast cancer cells. Tumor growth was demonstrated by cell proliferation and colony formation. RESULTS: DC- CLM cDNA encoded a protein of 260 amino acids and the gene was localized to chromosome 5q31. The predicted protein possessed a definitive cadherin-specific sequence motif and shared homology with classical cadherin. However, no transmembrane segment was observed in DC-CLM. Northern blot revealed the ubiquitous nature of DC-CLM transcripts in human tissues, with high expression in heart, brain, prostate, testis and ovary. RT-PCR demonstrated that DC-CLM was widely expressed in hematopoietic and epithelial tumor cell lines, but was not expressed in MCF-7. Interestingly, DC-CLM expression was upregulated in DC activated by lipopolysaccharides. DC-CLM expression in the stable transfectant (MCF-7/DC-CLM) was confirmed by RT-PCR and Western blot. DC-CLM protein was found to be secreted by MCF-7/DC-CLM but not expressed on the membrane of MCF-7/DC-CLM. DC-CLM transfection resulted in significant inhibition of in vitro growth and colony formation of MCF-7 cells. CONCLUSIONS: A cadherin-like molecule DC-CLM was cloned from human DC and it may be a soluble cadherin-like molecule for tumor suppression. DC-CLM was upregulated in activated DC and may be involved in the effector function of activated DC

43. Lang T, Yu L, Tu Q et al. Molecular cloning, genomic organization, and mapping of PRKAG2, a heart abundant gamma2 subunit of 5'-AMP-activated protein kinase, to human chromosome 7q36. Genomics. 2000;70:258-263.£¨¸´µ©´óѧ£©

Abstract: 5'-AMP-activated protein kinase (AMPK) acts as a major regulator of cellular ATP levels and protects cells against stresses that cause ATP depletion. AMPK is a protein heterotrimer composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. In the present study, a homologue of the AMPK gamma1-subunit cDNA with an open reading frame encoding 328 amino acids was identified. The putative protein sequence is about 76% identical to the 331-amino-acid gamma1 subunit and also has four consecutive cystathionine-beta-synthase (CBS) domains, a characteristic structure of AMPK gamma subunits from various species. This cDNA (tentatively termed PRKAG2-b) is identical to a recently reported cDNA (tentatively termed PRKAG2-a) of human AMPK gamma subunits except in their 5'-end regions, suggesting that these two cDNAs are two different transcripts of the same gene. To determine the expression pattern of the gene, two probes, one from the 3'-UTR of PRKAG2-b and the other from the 5'- unique region of PRKAG2-a, were used to hybridize MTN membranes. Three transcripts (3.8, 3.0, and 2.4 kb) were observed when the first probe was used, whereas only 3.8- and 3.0-kb transcripts were seen when the second probe was used. Thus, the PRKAG2-b corresponded to the 2.4-kb transcript, which is ubiquitously expressed except in liver and thymus. The highest level was detected in heart, while abundant expression also existed in placenta and testis. The expression pattern of PRKAG2-b is completely different from those of PRKAG2-a and PRKAG1, whose expression patterns were also determined in the current study. The PRKAG2 gene was located to human chromosome 7q36 between markers D7S2439 and D7S2462 by radiation hybrid mapping. The genomic organization of PRKAG2-b was identified by comparing its cDNA sequence with two genomic sequences AC006358 and AC006966, which showed that PRKAG2-b spanned an approximately 80-kb region and was composed of 12 exons

44. Li B, Wang ZZ, Ma FR et al. Cloning, expression and characterization of a cDNA (6A8) encoding a novel human alpha-mannosidase. Eur J Biochem. 2000;267:7176-7183.£¨Ò½¿ÆÔº»ù´¡Ëù£©

Abstract: A 3300-bp cDNA (6A8) has been isolated from a human tonsil cell lambdagt11 cDNA library (GenBank accession number: AF044414). The 6A8 gene is localized on human chromosome 13q31-32. Its cDNA has an open reading frame from position 57 bp to 3243 bp, encoding a 1062 amino- acid polypeptide. The sequence of the polypeptide has 89% identity to rat liver ER alpha-mannosidase. Homogenates of COS-7 cells transfected with 6A8 cDNA showed an enhanced enzymatic activity with p-nitro-phenyl- alpha-D-mannopyranoside, which was not inhibited by swainsonine. These data suggest that 6A8 alpha-mannosidase belongs to the class II alpha- mannosidase. Western blot analysis showed a band for 6A8 cDNA encoded protein of approximately 120 kDa. Northern blot analysis revealed two 6A8 mRNA transcripts with different tissue distribution. Enhanced concanavalin A (ConA) binding to CNE-2L2 cells transfected with a reverse 6A8 DNA was observed, indicating that the 6A8 protein is an important cellular alpha-mannosidase

45. Li N, Huang X, Zhao Z et al. Identification and characterization of a novel gene KE04 differentially expressed by activated human dendritic cells. Biochem Biophys Res Commun. 2000;279:487-493.£¨µÚ¶þ¾üÒ½´óѧ£©
Abstract: To better understand the molecular mechanisms of dendritic cells (DC) function, we isolated differentially expressed genes in Ag-activated DC by a PCR-based subtractive hybridization technique. A novel full-length cDNA, KE04, was thus isolated from KLH-activated human PBMC-derived DC. KE04 cDNA encoded a 346-aa protein devoid of functionally indicative motifs. KE04 protein showed 64% identity with a Caenorhabditis elegans protein and 83% identity with a human putative protein. Distant relationship was also found with other prokaryotic and eukaryotic proteins. Differential expression of KE04 in activated DC other than nonactivated DC was confirmed at both mRNA and protein levels. KE04 mRNA expression was detectable in various human tissues and cell lines by Northern blot and RT-PCR. Western blot and confocal microscopy analysis indicated that its cytolocalization was intracellular. Our data suggest the potential involvement of KE04 in DC activation and will facilitate the research of molecular mechanism of DC function

46. Li N, Zhang W, Wan T et al. Cloning and characterization of Siglec-10, a novel sialic acid binding member of the Ig superfamily, from human dendritic cells. J Biol Chem. 2001;276:28106-28112.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: The Siglecs (sialic acid-binding Ig-like lectins) are a subfamily of I- type lectins, which specifically recognize sialic acids. Nine members of the family have been identified thus far. We have obtained a novel cDNA clone from a human dendritic cell cDNA library encoding a protein with sequence and structural features of the Siglec family, hence designated as Siglec-10. The full-length Siglec-10 cDNA encodes a type 1 transmembrane protein containing four extracellular immunoglobulin- like domains, a transmembrane region, and a cytoplasmic tail with two classical immunoreceptor tyrosine-based inhibitory motifs. The N- terminal V-set Ig domain has most of the amino acid residues typical of the Siglecs. Siglec-10 shows the closest homology to Siglec-5 and Siglec-3/CD33. Various cells and cell lines including monocytes and dendritic cells express Siglec-10. High levels of mRNA expression were seen in peripheral blood leukocytes, spleen, and liver. When expressed on COS-7 cells, Siglec-10 was able to bind human red blood cells and soluble sialoglycoconjugates in a sialic acid-dependent manner. The identification of Siglec-10 as a new Siglec family member and its expression profile, together with its sialic acid-dependent binding capacity, suggest that it may be involved in cell-cell recognition by interacting with sialylated ligands expressed on specific cell populations

47. Li Z, Yao K, Cao Y. Molecular cloning of a novel tissue-specific gene from human nasopharyngeal epithelium. Gene. 1999;237:235-240.£¨ºþÄÏÒ½¿Æ´óѧ£©

Abstract: A novel cDNA of human nasopharyngeal epithelium was cloned. The cDNA fragment of the gene, termed NESG1, was originally isolated by mRNA differential display, and was not homologous to any of the known genes in the database. The complete sequence of NESG1 cDNA, 1850 bp, contains an open reading frame of 1575 nucleotides, and encodes a soluble basic protein of 386 amino acids containing multiple protein kinase phosphorylation sites. The deduced protein has no homology to any of the known proteins in the database. A homologous STS localized NESG1 to the chromosomal region of 1q22-24. Messenger RNA of this gene was expressed only in nasopharynx and trachea. These results suggest that the human NESG1 gene may be a specific gene of columnar ciliated epithelium

48. Liang X, Zhang H, Zhou A et al. AngRem104, an Angiotensin II-Induced Novel Upregulated Gene in Human Mesangial Cells, Is Potentially Involved in the Regulation of Fibronectin Expression. J Am Soc Nephrol. 2003;14:1443-1451.£¨±±¾©´óѧµÚÒ»Ò½Ôº£©

Abstract: ABSTRACT. Accumulation of extracellular matrix (ECM) in the glomerular mesangium is a common feature of many progressive renal diseases. Angiotensin II (AngII) plays important roles in the proliferation of glomerular mesangial cells (MC) as well as the synthesis of ECM such as fibronectin (FN) and collagens. However, the precise molecular signals responsible for these effects are unknown. To explore possible molecule mechanism of ECM accumulation related to AngII, suppression subtractive hybridization (SSH) was performed to screen and identify upregulated genes induced by AngII in cultured human MC. A novel gene, AngRem104 (GenBank accession number, AF367870), was isolated. The full-length cDNA of AngRem104 is 1690 bp, and it contains a 1041-bp open reading frame (ORF) encoding 347 amino acid residues with a predicted molecular mass of 37.2 kD. AngRem104 widely expressed in human heart, placenta, liver, muscle, kidney, and pancreas. Moreover, AngRem104 was found in human glomeruli and tubule by in situ hybridization. In human MC, the upregulation of AngRem104 induced by AngII was time-dependent, and it was dose-dependently blocked by AngII type 1 receptor antagonist (AT1RA), Losartan. The subcellular localization detected by AngRem104- pEGFP fusion protein revealed that AngRem104 was a nuclear protein. Interestingly, when AngRem104 was overexpressed by transfection of its sense construct, cDNA Microarray showed that two of the ECM-related genes, i.e., human mRNA for FN and integrin-beta-1 (FN receptor), dramatically upregulated their expressions. Furthermore, AngRem104 could regulate the expression of FN induced by AngII, which were detected by RT-PCR and quantitative real-time PCR, when AngRem104 was overexpressed. It is concluded that AngRem104 is a novel human gene potentially involved in the regulation of FN induced by AngII in human MC. These findings may provide new insights into mechanisms of glomerular sclerosis associated with AngII. E-mail: hongzh@bjmu.edu.cn

49. Lin L, Wu Y, Li C et al. Cloning, tissue expression pattern, and chromosome location of a novel human gene BRI3BP. Biochem Genet. 2001;39:369-377.£¨¸´µ©´óѧ£©

Abstract: A novel cDNA fragment was identified from a human fetal brain cDNA library by using the coding sequence of human BRI3 gene (Accession No. NM015379) as bait in a yeast two-hybrid screening. Then by 5'-RACE (rapid amplification of cDNA end) and electronic hybridization, we obtained a 1.9 kb contig which consists of a novel gene. It was designated as BRI3BP by the HUGO Nomenclature Committee. It contains an open reading frame encoding 251 amino acids. The calculated molecular weight of the deduced protein is 27.8 kU. The predicted isoelectric point is 9.48. Northern hybridization showed its mRNA was highly expressed in brain, kidney, and liver. By RH mapping, the BRI3BP gene was mapped to human chromosome 12q24.2-qter

50. Lin S, McLennan AG, Ying K et al. Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001;276:18695-18701.£¨¸´µ©´óѧ£©

Abstract: ITP and dITP exist in all cells. dITP is potentially mutagenic, and the levels of these nucleotides are controlled by inosine triphosphate pyrophosphatase (EC ). Here we report the cloning, expression, and characterization of a 21.5-kDa human inosine triphosphate pyrophosphatase (hITPase), an enzyme whose activity has been reported in many animal tissues and studied in populations but whose protein sequence has not been determined before. At the optimal pH of 10.0, recombinant hITPase hydrolyzed ITP, dITP, and xanthosine 5'- triphosphate to their respective monophosphates whereas activity with other nucleoside triphosphates was low. K(m) values for ITP, dITP, and xanthosine 5'-triphosphate were 0.51, 0.31, and 0.57 mm, respectively, and k(cat) values were 580, 360, and 640 s(-1), respectively. A divalent cation was absolutely required for activity. The gene encoding the hITPase cDNA sequence was localized by radiation hybrid mapping to chromosome 20p in the interval D20S113-D20S97, the same interval in which the ITPA inosine triphosphatase gene was previously localized. A BLAST search revealed the existence of many similar sequences in organisms ranging from bacteria to mammals. The function of this ubiquitous protein family is proposed to be the elimination of minor potentially mutagenic or clastogenic purine nucleoside triphosphates from the cell

51. Lin W, Zhou X, Zhang M et al. Expression and function of the HSD-3.8 gene encoding a testis-specific protein. Mol Hum Reprod. 2001;7:811-818.£¨Ò½¿ÆÔº»ù´¡Ëù£©

Abstract: The nucleotide sequence of the full length HSD-3.8 cDNA (accession number AF311312), encoding a human sperm component, was determined to consist of 3818 bp with a reading frame of 2778 bp encoding a deduced polypeptide composed of 926 amino acids. A 0.7 kb fragment containing three immunological epitopes of HSD-3.8 cDNA was prepared and used to construct recombinant expression vectors. The constructs were transformed into E.coli BL-21, and the fusion proteins were expressed, isolated and purified. Using the polyclonal antibodies raised against the purified expressed fusion proteins, positive immunostaining occurred over the surface of the postacrosomal zone of human spermatozoa and of germ cells within the seminiferous epithelium of human testis. Intense staining of large pachytene primary spermatocytes occurred. The capacity of the recombinant protein to reduce fertility as an immunogen in adult female rats was assessed. Immunized animals were infertile or exhibited marked reduction in their fertility. Analysis of the deduced HSD-3.8 polypeptide revealed the presence of a tetratricopeptide repeat (TPR) motif, a P-loop sequence that acts as a binding site for ATP/GTP and phosphorylation sites for PKC, CK2 and cAMP/cGMP-dependent protein kinases. A blot overlay assay with [alpha- (32)P]GTP showed that the polypeptide encoded by the 0.7 kb fragment of HSD-3.8 is a GTP binding protein. It was also shown to possess GTPase activity and to be phosphorylated by PKC in vitro. In conclusion, HSD- 3.8 is a GTP binding protein and its activity may be regulated by phosphorylation

52. Liu B, Liu Y, Chen J et al. CARP is a novel caspase recruitment domain containing pro-apoptotic protein. Biochem Biophys Res Commun. 2002;293:1396-1404.£¨Ò½¿ÆÔº¸·ÍâÒ½Ôº£©

Abstract: Many CARD-containing caspase mediators interact with CARD-containing caspases and participate in activation or suppression of caspases. We cloned a novel CARD-containing protein from our EST database, named CARP. Computational characterization revealed that CARP encoded 445 amino acids with predicted MW 49.7 kDa, localized at chromosome 10p13 with 15 exons, and four putative function domains, one CARD domain (aa 160-243), one nuclear receptor-binding motif, two EF-hand motifs, and 42% alpha-helix content. Stable transfection of CARP into lung carcinoma A549 and HEK293S cells leads to 23% of the cells undergoing apoptosis, but only 3% in the cells transfected with empty control vector. The cell proliferation was significantly inhibited by 1.2-5 folds (P<0.02) in seven CARP-transfected tumor cell lines-lung carcinoma A549 and PG, melanoma WM451, prostate cancer PC-3 and PC-3M, liver cancer H7402, and bladder cancer BIU87. Our results suggest that CARP is a novel CARD-containing pro-apoptotic protein

53. Liu H, Wang Y, Zhang Y et al. TFAR19, a novel apoptosis-related gene cloned from human leukemia cell line TF-1, could enhance apoptosis of some tumor cells induced by growth factor withdrawal. Biochem Biophys Res Commun. 1999;254:203-210.£¨±±´óҽѧ²¿£©

Abstract: Using the cDNA-representative differences analysis (cDNA-RDA) approach, we identified a novel gene, TFAR19 (TF-1 cell apoptosis related gene- 19), from TF-1 cells undergoing apoptosis. The human TFAR19 encodes a protein which shares significant homology to the corresponding proteins of species ranging from yeast to mice. TFAR19 exhibits a ubiquitous expression pattern and its expression is upregulated in the tumor cells undergoing apoptosis. Overexpression of TFAR19 in tumor cells enhances apoptosis triggered by growth factor or serum deprivation. We propose that TFAR19 may play a general role in the apoptotic process

54. Liu J, Zhou R, Zhang N et al. Biological function of a novel gene overexpressed in human hepatocellular carcinoma. Chin Med J (Engl ). 2000;113:881-885.£¨±±´óҽѧ²¿£©

Abstract: OBJECTIVE: To clone the full-length of a differentially expressed cDNA fragment, LC27, and study its biological function tentatively. METHODS: Northern blot was used to analyze the expression pattern of LC27 in hepatocellular carcinoma, matched nontumor liver tissues, fetal liver and normal adult liver tissues, as well as BEL-7402 hepatocellular carcinoma cell line ESTs splicing and 5' rapid amplification of cDNA ends (5' RACE) were used to clone the full-length of LC27 cDNA. An antisense oligodeoxynucleotide approach was used to investigate the biological role of the gene in the proliferation of BEL-7402 cells. RESULTS: A 2186 bp novel cDNA with an open reading frame encoding a 283 amino acid protein was cloned. Analysis of the deduced amino acid sequence indicated that it is 38% (88/229) identical to human Golgi 4- transmembrane spanning transporter MTP. The gene and the encoded protein was termed hepatocellular carcinoma overexpressed transmembrane protein (hotp) and HOTP, respectively. Hotp mRNA was almost undetectable in normal adult liver and fetal liver tissues. However, it was significantly up-regulated in hepatocellular carcinoma and some matched nontumor liver tissues, as well as BEL-7402 cells. The proliferation of BEL-7402 cells was suppressed by an antisense oligodeoxynucleotide against hotp mRNA at a concentration of 50 micrograms/ml. CONCLUSION: HOTP may be an integral membrane transporter protein. The overexpression of the gene in hepatocellular carcinoma may play an important role in hepatocarcinogenesis and disease progression

55. Liu J, Liu H, Zhang X et al. Identification and characterization of P15RS, a novel P15(INK4b) related gene on G1/S progression. Biochem Biophys Res Commun. 2002;299:880-885.£¨±±¾©Ê¦·¶´óѧ£©

Abstract: To screen genes involved in P15(INK4b) regulation during cell cycle, differential display method was applied to compare mRNAs from G(1) synchronized cells of MLIK6, which overexpressed P15(INK4b) gene, and its control MLC2. By using this approach, 15 cDNA fragments that were preferentially expressed in MLIK6 cells, but not in MLC2 cells, were screened out. A novel gene named P15RS was identified with further analysis. Combining the sequence from DD-PCR, homology analysis against EST database and RACE, a 4,404 bp complete cDNA sequence of P15RS was generated. Sequence analysis revealed that P15RS cDNA encoded a 312- amino-acid peptide containing a RAR domain that is involved in regulation of nuclear pre-mRNA, which suggests that P15RS may be a nuclear regulation protein. Genomic sequence analysis demonstrated that human P15RS gene was localized on chromosome 18q12 with seven exons and six introns. Expressing antisense P15RS in MLIK6 cells can up-regulate the expression of cyclinD1 and cyclinE. These data indicate that P15RS may act as a negative regulator in G(1) phase

56. Liu Q, Yu L, Gao J et al. Cloning, tissue expression pattern and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor. Mol Biol Rep. 2000;27:241-246.£¨¸´µ©´óѧ£©

Abstract: Latexin, a carboxypeptidase A inhibitor, is expressed in a cell type- specific manner in both central and peripheral nervous systems in the rat. It is used as a molecular marker for the regional specification of the neocortex. In this study, a cDNA was isolated from a human fetal brain cDNA library. The cDNA (LXN) contains an open reading frame encoding 222 amino acids. The comparison between the deduced amino acid sequences of LXN and latexins of rat and mouse revealed high sequence identity (84.2 and 84.7%, respectively). Northern blot analysis showed that LXN was expressed as a transcript of 1.3 kb in 15 out of 16 tissues examined, except in peripheral blood leukocyte. The expression levels were high in heart, prostate, ovary, kidney, pancreas, and colon, moderate or low in other tissues including brain. It is noteworthy that the tissue distribution of human LXN differs greatly to that of its homologue in the model animal, rat latexin. In addition, the LXN gene contains at least 6 exons and spans 5.9 kb according to the genomic sequence of the clone RP11-79M21 and the gap sequence cloned in this paper. LXN was assigned to 3q25-q26.2 according to the position of the marker SHGC-35682 found adjacent to LXN gene

57. Liu S, Yu Y, An H et al. Cloning and identification of a novel ubiquitin-like protein, BMSC-UbP, from human bone marrow stromal cells. Immunol Lett. 2003;86:169-175.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: Ubiquitin is one of phylogenetically well-conserved proteins in all eukaryotes. Ubiquitin-dependent modification of protein contributes to fine regulation of cellular biological processes. Using large-scale screening of human bone marrow stromal cell (BMSC) cDNA library, we isolated a full-length cDNA of 1352 bp encoding 380 amino acids with a ubiquitin domain (UBQ), which was designed as bone marrow stromal cell- derived ubiquitin-like protein (BMSC-UbP). In addition to UBQ domain at its N-terminus, BMSC-UbP also possesses a ubiquitin-associated domain at its C-terminus, sharing moderate homology to some ubiquitin-like proteins such as UBIN, Chap1, and ubiquilin. BMSC-UbP localizes at chromosome 15q22.3-q23 as confirmed by blast search in human genome. BMSC-UbP mRNA is widely expressed in human multiple tissues and various tumor cell lines. Moreover, BMSC-UbP mRNA decreased in BMSC stimulated with PMA and increased in HL60 cells stimulated with LPS, suggesting that BMSC-UbP might play roles in regulation of BMSC function or cell differentiation through an evocator- and cell-specific pattern

58. Liu S, An H, Li N et al. Cloning and identification of a novel human ubiquitin-like protein, DC- UbP, from dendritic cells. Biochem Biophys Res Commun. 2003;300:800-805.£¨µÚ¶þ¾üÒ½´óѧ£©

Abstract: Several ubiquitin-like proteins recently discovered have been confirmed to modify proteins akin to ubiquitinization for fine-regulation of intracellular proteins. In the present study, we report a novel ubiquitin-like protein from human dendritic cells (DC), named as dendritic cell-derived ubiquitin-like protein (DC-UbP). The full-length of DC-UbP cDNA is 565bp and encodes 106 amino acids. Ubiquitin domain (UBQ) in DC-UbP shares 28.6% identity and 55% similarity to ubiquitin, but does not possess the conserved C-terminus Gly-Gly of ubiquitin required for ubiquitinization. DC-UbP localized in cytoplasm, especially in mitochondrion, indicating that it may play a role in mitochondrial biology. DC-UbP mRNA was expressed in various tumor cells, but not in adult human normal tissues, suggesting that DC-UbP might be related to tumor genesis. In addition, DC-UbP mRNA expression decreased in the HL60 cells undergoing apoptosis after being stimulated with TRAIL and in the differentiated HL60 cells induced by ARTA. Taken together, DC-UbP might be downregulated during cellular differentiation and apoptosis

59. Liu X, Zhang C, Xing G et al. Functional characterization of novel human ARFGAP3. FEBS Lett. 2001;490:79-83.£¨¾üÊÂҽѧ¿ÆѧԺ·ÅÉäËù£©

Abstract: ADP ribosylation factors (ARFs) are critical in the vesicular trafficking pathway. ARF activity is controlled by GTPase-activating proteins (GAPs). We have identified recently a novel tentative ARF GAP derived from human fetal liver, ARFGAP3 (originally named as ARFGAP1). In the present study, we demonstrated that ARFGAP3 had GAP activity in vitro and remarked that the GAP activity of ARFGAP3 was regulated by phospholipids, i.e. phosphatidylinositol 4,5-diphosphate as agonist and phosphatidylcholine as antagonist. ARFGAP3 is a predominantly cytosolic protein, and concentrated in the perinuclear region. Its transient ectopic overexpression in cultured mammalian cells reduced the constitutive secretion of secreted alkaline phosphatase, indicating that ectopic overexpression of ARFGAP3 inhibits the early secretory pathway of proteins in vivo. These results demonstrated that ARFGAP3 is a novel GAP for ARF1 and might be involved in intracellular traffic of proteins and vesicular transport as predicted

60. Liu Y, Fan M, Yu S et al. cDNA cloning, chromosomal localization and expression pattern analysis of human LIM-homeobox gene LHX4. Brain Res. 2002;928:147-155.£¨¾üÊÂҽѧ¿ÆѧԺ£©

Abstract: LHX4 gene is a member of the LIM-homeobox gene family and plays a critical role in the development of motor neurons. We have isolated a cDNA of human LHX4 from a library of the adult human spinal cord. Its sequence is 92% homologous to that of the mouse Lhx4. The genomic structure of the LHX4 gene and its chromosomal localization were determined. The gene was mapped on human chromosome 1q 24.1-1q 24.3 and composed of six exons. The homeodomain was encoded by two exons, exons 4 and 5. The first LIM domain was coded by exon 2, and the second by exon 3. Human MTE Array was used to study the expression profile of LHX4 in 72 human tissues. The expression was specific in the CNS including the fetal brain, the spinal cord, and the cerebral cortex. In situ hybridization of the adult rodent CNS showed the abundant expression of LHX4 in the cerebral cortex and motor neurons of the spinal cord. Our results suggest that LHX4 may play a role in the CNS, especially the neocortex and the spinal cord, and provide a basis to investigate potential involvement of the LHX4 gene in human diseases

61. Liu Y, Li J, Zhang F et al. Molecular cloning and characterization of the human ASB-8 gene encoding a novel member of ankyrin repeat and SOCS box containing protein family. Biochem Biophys Res Commun. 2003;300:972-979.£¨ÉϺ£Ö×ÁöËù£©

Abstract: We have cloned a new member of human ankyrin repeat and SOCS box containing protein family (ASB), designed as hASB-8, from a human placental cDNA library and further extended by 5(') and 3(')-RACE. The full-length cDNA was 2545bp in length, with a predicted open reading frame encoding a protein of 288 amino acids, which was 96% identical to mouse ASB-8 protein. Computer analysis revealed that the deduced amino acid sequence of the human ASB-8 contained four Ankyrin repeats and one SOCS box. The gene had four exons separated by three introns and was mapped to human chromosome 12q13. Human ASB-8 mRNA was expressed at the highest level of expression in skeletal muscle and at a varied level of expression in heart, brain, placenta, liver, kidney, and pancreas. The transcript of hASB-8 was not detected in adult normal lung tissue, but found in lung carcinoma cell lines SPC-A1, A549, and NCI-H446. Subcellular localization analysis showed that the EGFP-tagged hASB-8 protein was localized at cytoplasm in human hepatocellular carcinoma cell line BEL-7402. We also provided evidence that hASB-8 could interact with Elongin B-C complex in vitro. Furthermore, transfection with the truncated mutant of hASB-8 cDNA lacking SOCS box could suppress cell growth of lung adenocarcinoma SPC-A1 cells in vitro, which suggests that this gene might be related to the development of lung cancer

62. Lo PK, Wang FF. Cloning and characterization of human and mouse DDA3 genes. Biochim Biophys Acta. 2002;1579:214-218.£¨Ì¨ÍåÑôÃ÷´óѧ£©

Abstract: We have previously reported the identification of the mouse DDA3 as a p53- and p73-inducible gene that encodes a protein capable of suppressing cell growth when ectopically expressed. We now report the cloning of the DDA3 cDNA of human as well as the genomic DDA3 DNA of human and mouse. Human DDA3 contains a 1002-bp open reading frame encoding a protein of 333 amino acids that shares 68.2% identity in amino acid sequence to the mouse protein. Expression of the human DDA3 transcript was detectable in various adult and fetal tissues examined, and was most abundantly expressed in the adult brain and fetal thymus. The DDA3 genes for human (7.7 kb) and mouse (6.7 kb) were sequenced; both contained eight exons, the genomic organization and the exon- intron junction sequences were highly conserved. The human DDA3 is located on chromosome 1p13.1, and the mouse gene is mapped to a syntenic region of chromosome 3. Analysis of a 300-kb genomic regions surrounding the mouse and human DDA3 genes revealed that the composition and orders for flanking genes were identical. Together, these results indicate that the newly cloned human gene is an orthologue of the mouse DDA3

63. Lu J, Hu G, Wang X et al. Cloning and characterization of a novel gene EC97 associated with human esophageal squamous cell carcinoma. Int J Mol Med. 2003;11:243-247.£¨Ò½¿ÆÔºÖ×ÁöËù£©

Abstract: We report on the cloning and characterization of a novel gene EC97 which is associated with human esophageal squamous cell carcinoma (ESCC). A fragment of expressed sequence tag (EST) (aa700351) was overexpressed in ESCC tissues compared with the normal tissues in cDNA microarray data. Based on the sequence of aa700351, the full-length cDNA was acquired by polymerase chain reaction (PCR) amplification and named EC97. EC97 was 3353 bp long and its encoding protein contained 813 amino acid residues. Northern blot and reverse transcription polymerase chain reaction (RT-PCR) analysis revealed that EC97 had a transcript of 3.4 kb in most human normal tissues we checked and its expression level was increased in 60% (12/20) of tested ESCC tissues versus the normal counterparts. EC97 was mapped to human chromosome 16p12-16p13.1 using radiation hybridization (RH) and predicted to include 25 exons and disseminated over 100 kb of genomic DNA

64. Luan Z, Zhang Y, Liu A et al. A novel GTP-binding protein hGBP3 interacts with NIK/HGK. FEBS Lett. 2002;530:233-238.£¨ÖпÆÔºÉϺ£ÉúÎﻯѧÓëϸ°ûÉúÎïѧÑо¿Ëù£©

Abstract: A novel human guanylate-binding protein (GBP) hGBP3 was identified and characterized. Similar as the two human guanylate-binding proteins hGBP1 and hGBP2, hGBP3 has the first two motifs of the three classical guanylate-binding motifs, GXXXXGKS (T) and DXXG, but lacks the N (T) KXD motif. Escherichia coli-expressed hGBP3 protein specifically binds to guanosine triphosphate (GTP). Using a yeast two-hybrid system, it was revealed that the N-terminal region of hGBP3 binds to the C- terminal regulatory domain of NIK/HGK, a member of the group I GCK (germinal center kinase) family. This interaction was confirmed by in vitro glutathione-S-transferase (GST) pull-down and co- immunoprecipitation assays

65. Luo K, Zhang W, Sui L et al. DIgR1, a novel membrane receptor of the immunoglobulin gene superfamily, is preferentially expressed by antigen-presenting cells. Biochem Biophys Res Commun. 2001;287:35-41.£¨Õã½­´óѧ£©

Abstract: A novel membrane receptor of immunoglobulin gene superfamily (IgSF) has been identified from mouse dendritic cells (DC) and designated as DC- derived Ig-like receptor 1 (DIgR1). It encodes a 228-amino-acid (aa) residue polypeptide with a 21-aa signal peptide, a 20-aa transmembrane region, a 189-aa extracellular region, and a 19 aa intracellular region. Its extracellular region contains a single V domain of Ig. So it is a novel type I transmembrane glycoprotein of IgSF. DIgR1 shows significant homologies to human CMRF-35 antigens and polymeric immunoglobulin receptors (pIgR). The mRNA expression of DIgR1 was highly abundant in mouse spleen. The preferential expression of DIgR1 mRNA is observed in the known antigen-presenting cells (APC) including DC, monocytes/macrophages, and B lymphocytes. A 40 kDa of protein in NIH/3T3 cells transfected with the DIgR1 cDNA was detected by Western blot analysis using anti-DIgR1 polyclonal antibodies. The expression of DIgR1 protein on DC is not regulated by LPS stimulation. Further study should be conducted to investigate what were biological functions of DIgR1 in the immunobiology of APC

66. Luo K, Yuan W, Zhu C et al. Expression of a novel Krupple-like zinc-finger gene, ZNF382, in human heart. Biochem Biophys Res Commun. 2002;299:606-612.£¨ºþÄÏʦ·¶´óѧ£©

Abstract: With the aim of identifying genes involved in human heart development and disease, we have isolated a novel KRAB-related zinc-finger gene named ZNF382 from heart cDNA library. The ZNF382 gene has a predicted 548-amino acid open reading frame, encoding a putative 64kDa zinc- finger protein. The N-terminus of the ZNF382 coding region has a well- conserved Krupple-associated box domain that consists of KRAB boxes A and B, whereas the C-terminus contains a Krupple-type zinc-finger domain possessing nine C(2)H(2) zinc-finger motifs in tandem arrays. The ZNF382 gene is mapped to chromosome 19q13.13. Northern blot analysis indicates that a 2.9-kb transcript specific for ZNF382 is expressed at very early embryonic stage of human (at least earlier than gestation 34 day) and widely in human embryo tissues. At the adult stage, ZNF382 expression is restricted largely to heart tissue suggesting a potential role in heart development and function

67. Ma Y, Zhang S, Xia Q et al. Molecular characterization of the TCP11 gene which is the human homologue of the mouse gene encoding the receptor of fertilization promoting peptide. Mol Hum Reprod. 2002;8:24-31.£¨ËÄ´¨´óѧ£©

Abstract: A human testis-specific gene was isolated by subtractive hybridization between the cDNA pools of adult and fetal testes, followed by rapid amplification of cDNA ends (RACE). This gene sequence is highly homologous to a large portion of the mouse Tcp11 gene which is important in sperm function because it encodes the receptor for fertilization-promoting peptide (FPP). The gene was mapped to human chromosome band 6p21 by fluorescence in-situ hybridization. The 9 exon gene spans a 22.8 kp genomic DNA sequence. The mature processed message encodes a 441 amino acid protein that is highly homologous to the mouse 566 amino acid protein after the first 142 amino acids. Results of Northern blot and RT-PCR analyses of RNA extracted from human tissues revealed that the gene is only expressed in fertile adult testes, but not in azoospermic testes, fetal testes nor in other human tissues. Taken together, our results along with the mouse Tcp11 function suggest that TCP11 gene is important in sperm function and fertility

68. Meng X, Zhang C, Chen J et al. Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 21. Biochem Genet. 2003;41:99-106.£¨¸´µ©´óѧ£©

Abstract: Thioredoxin plays an important role in various cellular processes through redox regulation. Here we report the molecular cloning and characterization of one member of the thioredoxin superfamily, designated as TMX2. The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail. Northern blot analysis shows it is widely expressed in human tissues

69. Ni X, Ma Y, Cheng H et al. Molecular cloning and characterization of a novel human Rab ( Rab2B) gene. J Hum Genet. 2002;47:548-551.£¨¸´µ©´óѧ£©

Abstract: Rab proteins are small-molecular-weight guanosine triphosphatases (GTPases) that control vesicular traffic in eukaryotic cells. The small GTPase Rab2 is a resident of pre-Golgi intermediates and is required for protein transport from the endoplasmic reticulum to the Golgi complex. We identified a novel human Rab (Rab2B) gene that was 2312 bp in length and encoded a protein of 216 amino acid residues. The protein shared high homology with mouse Rab2 (identity 83%, similarity 91%). The expression pattern of the human Rab2B gene showed that there is a transcript in kidney, prostate, lung, liver, thymus, colon, pancreas, and skeletal muscle, and low levels in placenta, whereas specific bands of the transcript could not be detected in heart, brain, spleen, testis, ovary, small intestine, and leukocyte. Overexpression has been observed in colon adenocarcinoma CX-1. The Rab2B gene consists of nine exons and eight introns and is mapped to chromosome 14q11.1-14q11.2 by bioinformatics analysis

70. Ni X, Gu S, Dai J et al. Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48:96-100.£¨¸´µ©´óѧ£©

Abstract: The NM23 gene is a conspicuous metastasis-suppressor gene. Eight human genes of the NM23/nucleoside diphosphate kinase family have been discovered. From our large cDNA cloning and sequencing project, we cloned a different transcript ( NM23-H1B) of human NM23-H1 from 18-week- old human fetal brain. The 987-bp cDNA encodes a protein of 177 amino acid residues. Compared with NM23H1, the cDNA contained an additional NH(2)-terminal region (25 amino acid residues). It was mapped to chromosome 17q21.3 using bioinformatics analysis, which shows that the second exon does not exist in NM23-H1. The expression pattern of NM23- H1B showed that it was ubiquitously expressed in normal tissues (15 tissues except colon) at different levels. Our data also indicated that the expression of the transcript in tumors related to tumor differentiation: in poorly differentiated breast carcinoma GI-101, pancreatic adenocarcinoma GI-103, and undifferentiated ovarian carcinoma GI-102, there was no expression. In poorly differentiated lung carcinoma LX-1, lung carcinoma GI-117, the expression level was very low. The transcript band in well-differentiated colon adenocarcinoma CX-1 was significantly higher than that in poorly differentiated colon adenocarcinoma GI-112. A high transcription level was also found in grade IV prostatic adenocarcinoma PC3

71. Pi H, Li Y, Zhu C et al. A novel human SCAN/(Cys)2(His)2 zinc-finger transcription factor ZNF323 in early human embryonic development. Biochem Biophys Res Commun. 2002;296:206-213.£¨ºþÄÏʦ·¶´óѧ£©

Abstract: The C(2)H(2) zinc-finger motif found in many transcription factors is thought to be important for nucleic acid binding and/or dimerization. Here, we have identified and characterized a novel zinc-finger gene named ZNF323 using degenerate primers from an early human embryo heart cDNA library. The predicted protein contains six different C(2)H(2) type zinc fingers and a SCAN box. ZNF323 maps to chromosome 6p22.1- 22.3. The expression levels were different during different development stages of human embryo between 15 and 23 weeks. Northern blot analysis shows that a 3.2-kb transcript specific for ZNF323 was expressed at high levels in the lung, liver, and kidney, while weakly expressed in intestine, brain, muscle, cholecyst, heart, and pancreas. In adult tissues, ZNF323 is expressed at high levels in liver and kidney, weakly in lung, pancreas, brain, placenta, muscle, and heart. Taken together, these results indicate that ZNF323 is a member of the zinc-finger transcription factor family and may be involved in the development of multiple embryonic organs

72. Qi ZY, Li Y, Ying K et al. Isolation of novel differentially expressed genes related to human glioma using cDNA microarray and characterizations of two novel full- length genes. J Neurooncol . 2002;56:197-208.£¨ËÕÖÝ´óѧµÚÒ»¸½ÊôÒ½Ôº£©

Abstract: Identification of the genes that are differentially expressed between brain tumor and normal brain tissues is important for understanding the molecular basis of these nerve system tumors and for defining possible targets for therapeutic intervention. This investigation is intended to obtain differentially expressed genes related to human glioma using cDNA microarray. Total RNA was extracted from human glioma specimens and normal brain tissues, and mRNA was obtained by oligotex chromatography. The cDNA microarray contains 4366 novel cDNA clones. The results of hybridization were scanned using computer system. Two genes selected from the results of cDNA microarray hybridization were subsequently analyzed by bio-informatic approach, Northern blot, in situ hybridization and radiation hybridization. We demonstrated that at a differentially expressed ration of two to three times, 15 cDNA clones were considered differentially expressed. Two novel full-length genes were selected for further investigation, one named human PKIbeta gene (clone 436F11, GenBank with accession number: AF225513) was over- expressed in normal brain tissues and the other named human ribosomal protein L14.22 gene (clone 507E08, GenBank with accession number: AF329277) was over-expressed in gliomas. Furthermore, the 436F11 gene was located on 6q21-q23 between the D6S304 and D6S2156 markers, while the 507E08 gene was located between the D14S1066 and D14S265 markers. We realized that cDNA microarray technology can be successfully applied to identify differentially expressed genes in human glioma. This approach is superior to routine representational difference analysis, suppression subtractive hybridization and Northern blot for detection and isolation of differentially expressed genes in different tissues. At present, we have discovered two novel full-length genes related to human glioma and their characterizations have been partially clarified

73. Qin WX, Wan F, Sun FY et al. Cloning and characterization of a novel gene (C17orf25) from the deletion region on chromosome 17p13.3 in hepatocelular carcinoma. Cell Res. 2001;11:209-216.£¨ÉϺ£Ö×ÁöËù£©

Abstract: Using a combination of hybridization of PAC to a cDNA library and RACE technique, we isolated a novel cDNA, designated as C17orf25 (Chromosome 17 open reading frame 25, previously named it HC71A), from the deletion region on chromosome 17p13.3. The cDNA encodes a protein of 313 amino acids with a calculated molecular mass of 34.8 kDa. C17orf25 is divided into 10 exons and 9 introns, spanning 23 kb of genomic DNA. Northern blot analysis showed that the mRNA expression of C17orf25 was decreased in hepatocellular carcinoma samples as compared to adjacent noncancerous liver tissues from the same patients. The transfection of C17orf25 into the hepatocellular carcinoma cell SMMC7721 and overexpression could inhibit the cell growth. The above results indicate that C17orf25 is a novel human gene, and the cloning and preliminary characterization of C17orf25 is a prerequisite for further functional analysis of this novel gene in human hepatocellular carcinoma

74. Qu X, Zhang C, Zhai Y et al. Characterization and tissue expression of a novel human gene npdc1. Gene. 2001;264:37-44.£¨¾ü¿ÆÔº·ÅÉäҽѧÑо¿Ëù£©

Abstract: We report the molecular characterization of a novel human homologue of mouse npdc1 (neural proliferation, differentiation and control, 1) gene, designated human npdc1 (hnpdc1). hnpdc1 was identified by large- scale sequencing of fetal liver cDNA libraries and the full-length cDNA was obtained by PCR amplification. The hnpdc1 gene, which contains nine exons, was mapped to human chromosome 15. It encodes a polypeptide of 325 amino acids, which shows high homology (77% identity) to the mouse NPDC1. Sequence analysis has shown that hNPDC1 protein contains a putative signal peptide of 34 amino acids, a transmembrane segment, and a typical bipartite nuclear localization signal. Northern blot and dot blot hybridization indicates that, just like mnpdc1, hnpdc1 mRNA is strongly expressed in adult brain (especially in hippocampus, frontal lobe and temporal lobe) and about 1.82-fold higher in adult brain than that in fetal brain. Unlike mnpdc1, however, hnpdc1 contains two transcripts instead of only one (1.5 kb), and has high expression levels in prostate, pituitary gland, and mammary glands. These results support that hNPDC1 plays a role in the control of neural cell proliferation and differentiation, and suggest that it may be involved in the development of several secretion glands

75. Qu X, Wei H, Zhai Y et al. Identification, characterization, and functional study of the two novel human members of the semaphorin gene family. J Biol Chem. 2002;277:35574-35585.£¨¾ü¿ÆÔº·ÅÉäҽѧÑо¿Ëù£©

Abstract: We cloned two novel human transmembrane semaphorins, (HSA)SEMA6C and (HSA)SEMA6D, that belong to the class VI subgroup of the semaphorin family. The genes for SEMA6C and SEMA6D are mapped on chromosome 1q1