HS3ST1
Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox 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
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- ^ Page Module:Citation/CS1/styles.css has no content.Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (February 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". The Journal of Biological Chemistry. 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1".
- ^ Page Module:Citation/CS1/styles.css has no content.Witoelar A, Rongve A, Almdahl IS, et al. (2018-12-27). "Meta-analysis of Alzheimer's disease on 9,751 samples from Norway and IGAP study identifies four risk loci". Scientific Reports. 8 (1): 18088. Bibcode:2018NatSR...818088W. doi:10.1038/s41598-018-36429-6. PMC 6308232. PMID 30591712.
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Razi N, Lindahl U (May 1995). "Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides". The Journal of Biological Chemistry. 270 (19): 11267–75. doi:10.1074/jbc.270.19.11267. PMID 7744762.
- Page Module:Citation/CS1/styles.css has no content.Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD (October 1996). "Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase". The Journal of Biological Chemistry. 271 (43): 27072–82. doi:10.1074/jbc.271.43.27072. PMID 8900198.
- Page Module:Citation/CS1/styles.css has no content.Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D, Rosenberg RD (October 1997). "Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase". The Journal of Biological Chemistry. 272 (44): 28008–19. doi:10.1074/jbc.272.44.28008. PMID 9346953.
- Page Module:Citation/CS1/styles.css has no content.Liu J, Shworak NW, Sinaÿ P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD (February 1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities". The Journal of Biological Chemistry. 274 (8): 5185–92. doi:10.1074/jbc.274.8.5185. PMID 9988768.
- Page Module:Citation/CS1/styles.css has no content.Hernaiz M, Liu J, Rosenberg RD, Linhardt RJ (September 2000). "Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III". Biochemical and Biophysical Research Communications. 276 (1): 292–7. doi:10.1006/bbrc.2000.3453. PMID 11006120.
- Page Module:Citation/CS1/styles.css has no content.Edavettal SC, Carrick K, Shah RR, Pedersen LC, Tropsha A, Pope RM, Liu J (April 2004). "A conformational change in heparan sulfate 3-O-sulfotransferase-1 is induced by binding to heparan sulfate". Biochemistry. 43 (16): 4680–8. doi:10.1021/bi0499112. PMID 15096036.
External links
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