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词条 HS3ST1
释义

  1. Function

  2. Clinical significance

  3. References

  4. Further reading

{{Infobox_gene}}Heparan sulfate glucosamine 3-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS3ST1 gene.[1][2]

Function

Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein.[2]

Clinical significance

Polymorphisms in HS3ST1 appear to be a risk factor for developing Alzheimer's disease.[3]

References

1. ^{{cite journal | vauthors = Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD | title = Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci | journal = The Journal of Biological Chemistry | volume = 274 | issue = 8 | pages = 5170–84 | date = February 1999 | pmid = 9988767 | pmc = | doi = 10.1074/jbc.274.8.5170 }}
2. ^{{cite web | title = Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9957| access-date = }}
3. ^{{cite journal |vauthors = Witoelar A, Rongve A, Almdahl IS, etal | title = Meta-analysis of Alzheimer’s disease on 9,751 samples from Norway and IGAP study identifies four risk loci | journal = Scientific Reports | volume = 8 | issue = 1 | pages = 18088 | date = 2018-12-27 | doi = 10.1038/s41598-018-36429-6}}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Razi N, Lindahl U | title = Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides | journal = The Journal of Biological Chemistry | volume = 270 | issue = 19 | pages = 11267–75 | date = May 1995 | pmid = 7744762 | doi = 10.1074/jbc.270.19.11267 }}
  • {{cite journal | vauthors = Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD | title = Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 43 | pages = 27072–82 | date = October 1996 | pmid = 8900198 | doi = 10.1074/jbc.271.43.27072 }}
  • {{cite journal | vauthors = Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D, Rosenberg RD | title = Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase | journal = The Journal of Biological Chemistry | volume = 272 | issue = 44 | pages = 28008–19 | date = October 1997 | pmid = 9346953 | doi = 10.1074/jbc.272.44.28008 }}
  • {{cite journal | vauthors = Liu J, Shworak NW, Sinaÿ P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD | title = Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities | journal = The Journal of Biological Chemistry | volume = 274 | issue = 8 | pages = 5185–92 | date = February 1999 | pmid = 9988768 | doi = 10.1074/jbc.274.8.5185 }}
  • {{cite journal | vauthors = Hernaiz M, Liu J, Rosenberg RD, Linhardt RJ | title = Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III | journal = Biochemical and Biophysical Research Communications | volume = 276 | issue = 1 | pages = 292–7 | date = September 2000 | pmid = 11006120 | doi = 10.1006/bbrc.2000.3453 }}
  • {{cite journal | vauthors = Edavettal SC, Carrick K, Shah RR, Pedersen LC, Tropsha A, Pope RM, Liu J | title = A conformational change in heparan sulfate 3-O-sulfotransferase-1 is induced by binding to heparan sulfate | journal = Biochemistry | volume = 43 | issue = 16 | pages = 4680–8 | date = April 2004 | pmid = 15096036 | doi = 10.1021/bi0499112 }}
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