HS3ST2

From Justapedia, unleashing the power of collective wisdom
Jump to navigation Jump to search

An Error has occurred retrieving Wikidata item for infobox Heparan sulfate glucosamine 3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the HS3ST2 gene.[1][2]

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 is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity. This gene is expressed predominantly in brain and may play a role in the nervous system.[2]

Role in breast cancer The HS3ST2 promoter is hypermethylated in breast cancer tissue compared to normal breast ducts, suggesting a potential involvement in the pathogenesis of the disease.[3] Functional analysis revealed that upregulation of HS3ST2 in human breast cancer cells resulted in altered invasiveness, which was due to changes in Mitogen-activated protein kinase signaling and matrix metalloproteinase expression.[4]

References

  1. ^ Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (Mar 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J Biol Chem. 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
  2. ^ a b "Entrez Gene: HS3ST2 heparan sulfate (glucosamine) 3-O-sulfotransferase 2".
  3. ^ Dietrich, Dimo (2009). "Analysis of DNA Methylation of Multiple Genes in Microdissected Cells From Formalin-fixed and Paraffin-embedded Tissues". Journal of Histochemistry and Cytochemistry. 57 (5): 477–489. doi:10.1369/jhc.2009.953026. PMC 2674771. PMID 19153192.
  4. ^ Vijaya Kumar, Archana (2014). "HS3ST2 modulates breast cancer cell invasiveness via MAP kinase- and Tcf4 (Tcf7l2)-dependent regulation of protease and cadherin expression". International Journal of Cancer. 135 (11): 2579–92. doi:10.1002/ijc.28921. PMID 24752740. S2CID 205950148.

Further reading