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词条 CHST7
释义

  1. Function

  2. References

  3. External links

  4. Further reading

{{Infobox_gene}}Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.[1][2]

Function

This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moieties during chondroitin sulfate biosynthesis. They create considerable structural diversity among chondroitin sulfates by transferring sulfate with remarkable specificity for the underlying oligosaccharide substrate. This gene product mainly transfers sulfate to N-acetylgalactosamine. The regulated expression of each member of this gene family may be an important determinant of sulfated GAGs expression and the associated function of chondroitin sulfates as regulators of many biologic processes. This gene is part of a gene cluster on chromosome Xp11.23.[2]

References

1. ^{{cite journal |vauthors=Kitagawa H, Fujita M, Ito N, Sugahara K | title = Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase | journal = J Biol Chem | volume = 275 | issue = 28 | pages = 21075–80 |date=Aug 2000 | pmid = 10781596 | pmc = | doi = 10.1074/jbc.M002101200 }}
2. ^{{cite web | title = Entrez Gene: CHST7 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56548| accessdate = }}

External links

  • {{UCSC gene info|CHST7}}

Further reading

{{refbegin | 2}}
  • {{cite journal | author=Liu T |title=Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070–80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 | pmc=1850943 |name-list-format=vanc| author2=Qian WJ | author3=Gritsenko MA | display-authors=3 | last4=Camp | first4=David G. | last5=Monroe | first5=Matthew E. | last6=Moore | first6=Ronald J. | last7=Smith | first7=Richard D. }}
  • {{cite journal | author=Ross MT |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 | pmc=2665286 |name-list-format=vanc| author2=Grafham DV | author3=Coffey AJ | display-authors=3 | last4=Scherer | first4=Steven | last5=McLay | first5=Kirsten | last6=Muzny | first6=Donna | last7=Platzer | first7=Matthias | last8=Howell | first8=Gareth R. | last9=Burrows | first9=Christine }}
  • {{cite journal | author=Gerhard DS |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 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
  • {{cite journal | author=Strausberg RL |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 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }}
  • {{cite journal | author=Thiselton DL |title=An integrated, functionally annotated gene map of the DXS8026-ELK1 interval on human Xp11.3-Xp11.23: potential hotspot for neurogenetic disorders |journal=Genomics |volume=79 |issue= 4 |pages= 560–72 |year= 2002 |pmid= 11944989 |doi= 10.1006/geno.2002.6733 |name-list-format=vanc| author2=McDowall J | author3=Brandau O | display-authors=3 | last4=Ramser | first4=Juliane | last5=d'Esposito | first5=Fabiana | last6=Bhattacharya | first6=Shomi S. | last7=Ross | first7=Mark T. | last8=Hardcastle | first8=Alison J. | last9=Meindl | first9=Alfons }}
  • {{cite journal | author=Bhakta S |title=Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5) |journal=J. Biol. Chem. |volume=275 |issue= 51 |pages= 40226–34 |year= 2001 |pmid= 10956661 |doi= 10.1074/jbc.M006414200 |name-list-format=vanc| author2=Bartes A | author3=Bowman KG | display-authors=3 | last4=Kao | first4=WM | last5=Polsky | first5=I | last6=Lee | first6=JK | last7=Cook | first7=BN | last8=Bruehl | first8=RE | last9=Rosen | first9=SD }}
  • {{cite journal | author=Uchimura K |title=Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities |journal=Biochem. Biophys. Res. Commun. |volume=274 |issue= 2 |pages= 291–6 |year= 2000 |pmid= 10913333 |doi= 10.1006/bbrc.2000.3141 |name-list-format=vanc| author2=Fasakhany F | author3=Kadomatsu K | display-authors=3 | last4=Matsukawa | first4=Tetsuya | last5=Yamakawa | first5=Taishi | last6=Kurosawa | first6=Nobuyuki | last7=Muramatsu | first7=Takashi }}
  • {{cite journal | author=Shilatifard A |title=Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine |journal=J. Virol. |volume=67 |issue= 2 |pages= 943–52 |year= 1993 |pmid= 8419650 |doi= | pmc=237448 |name-list-format=vanc| author2=Merkle RK | author3=Helland DE | display-authors=3 | last4=Welles | first4=JL | last5=Haseltine | first5=WA | last6=Cummings | first6=RD }}
  • {{cite journal |vauthors=Bernstein HB, Compans RW |title=Sulfation of the human immunodeficiency virus envelope glycoprotein |journal=J. Virol. |volume=66 |issue= 12 |pages= 6953–9 |year= 1992 |pmid= 1433500 |doi= | pmc=240329 }}
{{refend}}{{gene-X-stub}}
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