HS3ST1: Difference between revisions

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'''Heparan sulfate glucosamine 3-O-sulfotransferase 1''' is an [[enzyme]] that in humans is encoded by the ''HS3ST1'' [[gene]].<ref name="pmid9988767">{{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 = J Biol Chem | volume = 274 | issue = 8 | pages = 5170–84 |date=Mar 1999 | pmid = 9988767 | pmc =  | doi =10.1074/jbc.274.8.5170 }}</ref><ref name="entrez">{{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| accessdate = }}</ref>
'''Heparan sulfate glucosamine 3-O-sulfotransferase 1''' is an [[enzyme]] that in humans is encoded by the ''HS3ST1'' [[gene]].<ref name="pmid9988767">{{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 }}</ref><ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = 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.<ref name="entrez" />
}}


==References==
[[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.<ref name="entrez" />
 
== Clinical significance ==
 
[[Gene polymorphism|Polymorphism]]s in ''HS3ST1'' appear to be a risk factor for developing [[Alzheimer's disease]].<ref>{{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}}</ref>
 
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 }}
| citations =
* {{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=Razi N, Lindahl U |title=Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11267–75 |year= 1995 |pmid= 7744762 |doi=10.1074/jbc.270.19.11267 }}
* {{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, Fritze LM, etal |title=Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. |journal=J. Biol. Chem. |volume=271 |issue= 43 |pages= 27072–82 |year= 1996 |pmid= 8900198 |doi=10.1074/jbc.271.43.27072 }}
* {{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=Shworak NW, Liu J, Fritze LM, etal |title=Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 28008–19 |year= 1997 |pmid= 9346953 |doi=10.1074/jbc.272.44.28008 }}
* {{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=Liu J, Shworak NW, Sinaÿ P, etal |title=Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5185–92 |year= 1999 |pmid= 9988768 |doi=10.1074/jbc.274.8.5185 }}
* {{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 }}
*{{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=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 292–7 |year= 2000 |pmid= 11006120 |doi= 10.1006/bbrc.2000.3453 }}
*{{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=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Edavettal SC, Carrick K, Shah RR, etal |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 |year= 2004 |pmid= 15096036 |doi= 10.1021/bi0499112 }}
*{{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 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=9957}}
{{PDB Gallery|geneid=9957}}


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Revision as of 09:10, 29 December 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Wikidata
View/Edit Human

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. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1".
  3. ↑ 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. doi:10.1038/s41598-018-36429-6.

Further reading

  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.


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