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词条 MTAP
释义

  1. References

  2. Further reading

{{Underlinked|date=March 2014}}{{Infobox_gene}}S-methyl-5'-thioadenosine phosphorylase is an enzyme that in humans is encoded by the MTAP gene.[1][2]

This gene encodes an enzyme that plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine. The encoded enzyme is deficient in many cancers because this gene and the tumor suppressor p16 gene are co-deleted. Multiple alternatively spliced transcript variants have been described for this gene, but their full-length natures remain unknown.[2]

References

1. ^{{cite journal |vauthors=Schmid M, Sen M, Rosenbach MD, Carrera CJ, Friedman H, Carson DA | title = A methylthioadenosine phosphorylase (MTAP) fusion transcript identifies a new gene on chromosome 9p21 that is frequently deleted in cancer | journal = Oncogene | volume = 19 | issue = 50 | pages = 5747–54 |date=Dec 2000 | pmid = 11126361 | pmc = | doi = 10.1038/sj.onc.1203942 }}
2. ^1 {{cite web | title = Entrez Gene: MTAP methylthioadenosine phosphorylase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4507| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Carrera CJ, Eddy RL, Shows TB, Carson DA |title=Assignment of the gene for methylthioadenosine phosphorylase to human chromosome 9 by mouse-human somatic cell hybridization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 9 |pages= 2665–8 |year= 1984 |pmid= 6425836 |doi=10.1073/pnas.81.9.2665 | pmc=345130 }}
  • {{cite journal |vauthors=Olopade OI, Pomykala HM, Hagos F, etal |title=Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 14 |pages= 6489–93 |year= 1995 |pmid= 7604019 |doi=10.1073/pnas.92.14.6489 | pmc=41543 }}
  • {{cite journal |vauthors=Nobori T, Takabayashi K, Tran P, etal |title=Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 12 |pages= 6203–8 |year= 1996 |pmid= 8650244 |doi=10.1073/pnas.93.12.6203 | pmc=39214 }}
  • {{cite journal |vauthors=Della Ragione F, Takabayashi K, Mastropietro S, etal |title=Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=223 |issue= 3 |pages= 514–9 |year= 1996 |pmid= 8687427 |doi= 10.1006/bbrc.1996.0926 }}
  • {{cite journal |vauthors=Appleby TC, Erion MD, Ealick SE |title=The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. |journal=Structure |volume=7 |issue= 6 |pages= 629–41 |year= 1999 |pmid= 10404592 |doi=10.1016/S0969-2126(99)80084-7 }}
  • {{cite journal |vauthors=Gursky S, Olopade OI, Rowley JD |title=Identification of a 1.2 Kb cDNA fragment from a region on 9p21 commonly deleted in multiple tumor types. |journal=Cancer Genet. Cytogenet. |volume=129 |issue= 2 |pages= 93–101 |year= 2001 |pmid= 11566337 |doi=10.1016/S0165-4608(01)00444-7 }}
  • {{cite journal |vauthors=Christopher SA, Diegelman P, Porter CW, Kruger WD |title=Methylthioadenosine phosphorylase, a gene frequently codeleted with p16(cdkN2a/ARF), acts as a tumor suppressor in a breast cancer cell line. |journal=Cancer Res. |volume=62 |issue= 22 |pages= 6639–44 |year= 2002 |pmid= 12438261 |doi= }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
  • {{cite journal |vauthors=Bornhauser BC, Olsson PA, Lindholm D |title=MSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35412–20 |year= 2003 |pmid= 12826659 |doi= 10.1074/jbc.M306271200 }}
  • {{cite journal |vauthors=Behrmann I, Wallner S, Komyod W, etal |title=Characterization of methylthioadenosin phosphorylase (MTAP) expression in malignant melanoma. |journal=Am. J. Pathol. |volume=163 |issue= 2 |pages= 683–90 |year= 2003 |pmid= 12875987 |doi= 10.1016/S0002-9440(10)63695-4| pmc=1868213 }}
  • {{cite journal |vauthors=Subhi AL, Diegelman P, Porter CW, etal |title=Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 49868–73 |year= 2004 |pmid= 14506228 |doi= 10.1074/jbc.M308451200 }}
  • {{cite journal |vauthors=Beausoleil SA, Jedrychowski M, Schwartz D, etal |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Bataille F, Rogler G, Modes K, etal |title=Strong expression of methylthioadenosine phosphorylase (MTAP) in human colon carcinoma cells is regulated by TCF1/[beta]-catenin. |journal=Lab. Invest. |volume=85 |issue= 1 |pages= 124–36 |year= 2005 |pmid= 15492751 |doi= 10.1038/labinvest.3700192 }}
  • {{cite journal |vauthors=Berasain C, Hevia H, Fernández-Irigoyen J, etal |title=Methylthioadenosine phosphorylase gene expression is impaired in human liver cirrhosis and hepatocarcinoma. |journal=Biochim. Biophys. Acta |volume=1690 |issue= 3 |pages= 276–84 |year= 2004 |pmid= 15511635 |doi= 10.1016/j.bbadis.2004.08.002 }}
  • {{cite journal |vauthors=Subhi AL, Tang B, Balsara BR, etal |title=Loss of methylthioadenosine phosphorylase and elevated ornithine decarboxylase is common in pancreatic cancer. |journal=Clin. Cancer Res. |volume=10 |issue= 21 |pages= 7290–6 |year= 2005 |pmid= 15534104 |doi= 10.1158/1078-0432.CCR-04-0972 }}
  • {{cite journal |vauthors=Hustinx SR, Hruban RH, Leoni LM, etal |title=Homozygous deletion of the MTAP gene in invasive adenocarcinoma of the pancreas and in periampullary cancer: a potential new target for therapy. |journal=Cancer Biol. Ther. |volume=4 |issue= 1 |pages= 83–6 |year= 2005 |pmid= 15662124 |doi=10.4161/cbt.4.1.1380 }}
  • {{cite journal |vauthors=Hustinx SR, Leoni LM, Yeo CJ, etal |title=Concordant loss of MTAP and p16/CDKN2A expression in pancreatic intraepithelial neoplasia: evidence of homozygous deletion in a noninvasive precursor lesion. |journal=Mod. Pathol. |volume=18 |issue= 7 |pages= 959–63 |year= 2005 |pmid= 15832197 |doi= 10.1038/modpathol.3800377 }}
  • {{cite journal |vauthors=Hellerbrand C, Mühlbauer M, Wallner S, etal |title=Promoter-hypermethylation is causing functional relevant downregulation of methylthioadenosine phosphorylase (MTAP) expression in hepatocellular carcinoma. |journal=Carcinogenesis |volume=27 |issue= 1 |pages= 64–72 |year= 2007 |pmid= 16081515 |doi= 10.1093/carcin/bgi201 }}
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