Biology:ST8SIA2
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 Generic protein structure example |
Alpha-2,8-sialyltransferase 8B is an enzyme that in humans is encoded by the ST8SIA2 gene.[1][2]
Function
The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.[2]
References
- ↑ "A human STX cDNA confers polysialic acid expression in mammalian cells". The Journal of Biological Chemistry 270 (39): 22685–8. September 1995. doi:10.1074/jbc.270.39.22685. PMID 7559389.
- ↑ 2.0 2.1 "Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8128.
Further reading
- "An investigation of the role of transmembrane domains in Golgi protein retention". The EMBO Journal 14 (19): 4695–704. October 1995. doi:10.1002/j.1460-2075.1995.tb00151.x. PMID 7588599.
- "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry 269 (27): 17872–8. July 1994. doi:10.1016/S0021-9258(17)32390-6. PMID 8027041.
- "Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation". The Journal of Biological Chemistry 271 (32): 19457–63. August 1996. doi:10.1074/jbc.271.32.19457. PMID 8702635.
- "Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST". The Journal of Biological Chemistry 272 (11): 7182–90. March 1997. doi:10.1074/jbc.272.11.7182. PMID 9054414.
- "In vivo autopolysialylation and localization of the polysialyltransferases PST and STX". The Journal of Biological Chemistry 273 (51): 34586–93. December 1998. doi:10.1074/jbc.273.51.34586. PMID 9852130.
- "Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III". The Journal of Biological Chemistry 275 (24): 18594–601. June 2000. doi:10.1074/jbc.M910204199. PMID 10766765.
- "The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule". Glycobiology 11 (11): 997–1008. November 2001. doi:10.1093/glycob/11.11.997. PMID 11744634.
- "ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes". The Journal of Biological Chemistry 277 (39): 36808–17. September 2002. doi:10.1074/jbc.M204632200. PMID 12138100.
- "SV2B regulates synaptotagmin 1 by direct interaction". The Journal of Biological Chemistry 279 (50): 52124–31. December 2004. doi:10.1074/jbc.M407502200. PMID 15466855.
- "Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells". International Immunopharmacology 5 (4): 757–69. April 2005. doi:10.1016/j.intimp.2004.12.009. PMID 15710344.
- "Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia". Biological Psychiatry 59 (7): 652–9. April 2006. doi:10.1016/j.biopsych.2005.08.016. PMID 16229822.
- "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities.". Med. Res. Rev. 37 (2): 210–270. 2017. doi:10.1002/med.21407. PMID 27678392. http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5226&context=smhpapers.
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