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ST8SIA1

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{{Short description|Protein-coding gene in the species Homo sapiens}}

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Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA1 gene.{{cite journal | vauthors = Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M | title = Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection | journal = J Biol Chem | volume = 268 | issue = 30 | pages = 22782–7 |date=Dec 1993 | doi = 10.1016/S0021-9258(18)41595-5 | pmid = 7901202 | doi-access = free }}{{cite web | title = Entrez Gene: ST8SIA1 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6489}}

Gangliosides are membrane-bound glycosphingolipids containing sialic acid. Ganglioside GD3 is known to be important for cell adhesion and growth of cultured malignant cells. The protein encoded by ST8SIA1 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to GM3 to produce gangliosides GD3 and GT3. The encoded protein may be found in the Golgi apparatus and is a member of glycosyltransferase family 29.

In melanocytic cells, ST8SIA1 gene expression may be regulated by MITF.{{cite journal |vauthors=Hoek KS, Schlegel NC, Eichhoff OM, etal | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell Melanoma Res. | volume = 21 | issue = 6 | pages = 665–76 | year = 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x | s2cid = 24698373 | doi-access = free }}

References

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Further reading

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  • {{cite journal |vauthors=Haraguchi M, Yamashiro S, Yamamoto A, etal |title=Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2,8-sialyltransferase cDNA using anti-GD2 monoclonal antibody. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 22 |pages= 10455–9 |year= 1994 |pmid= 7937974 |doi=10.1073/pnas.91.22.10455 | pmc=45039 |bibcode=1994PNAS...9110455H |doi-access=free }}
  • {{cite journal |vauthors=Nara K, Watanabe Y, Maruyama K, etal |title=Expression cloning of a CMP-NeuAc:NeuAc alpha 2-3Gal beta 1-4Glc beta 1-1'Cer alpha 2,8-sialyltransferase (GD3 synthase) from human melanoma cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 17 |pages= 7952–6 |year= 1994 |pmid= 8058740 |doi=10.1073/pnas.91.17.7952 | pmc=44522 |bibcode=1994PNAS...91.7952N |doi-access=free }}
  • {{cite journal |vauthors=Sasaki K, Kurata K, Kojima N, etal |title=Expression cloning of a GM3-specific alpha-2,8-sialyltransferase (GD3 synthase). |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15950–6 |year= 1994 |doi=10.1016/S0021-9258(17)40773-3 |pmid= 8195250 |doi-access=free }}
  • {{cite journal |vauthors=Nakayama J, Fukuda MN, Hirabayashi Y, etal |title=Expression cloning of a human GT3 synthase. GD3 AND GT3 are synthesized by a single enzyme. |journal=J. Biol. Chem. |volume=271 |issue= 7 |pages= 3684–91 |year= 1996 |pmid= 8631981 |doi= 10.1074/jbc.271.7.3684|doi-access=free }}
  • {{cite journal |vauthors=Matsuda Y, Nara K, Watanabe Y, etal |title=Chromosome mapping of the GD3 synthase gene (SIAT8) in human and mouse. |journal=Genomics |volume=32 |issue= 1 |pages= 137–9 |year= 1996 |pmid= 8786103 |doi= 10.1006/geno.1996.0090 }}
  • {{cite journal |vauthors=De Maria R, Lenti L, Malisan F, etal |title=Requirement for GD3 ganglioside in CD95- and ceramide-induced apoptosis. |journal=Science |volume=277 |issue= 5332 |pages= 1652–5 |year= 1997 |pmid= 9287216 |doi=10.1126/science.277.5332.1652 |hdl=11566/37451 }}
  • {{cite journal |vauthors=Angata K, Suzuki M, McAuliffe J, etal |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18594–601 |year= 2000 |pmid= 10766765 |doi= 10.1074/jbc.M910204199 |doi-access= free }}
  • {{cite journal |vauthors=Zeng G, Gao L, Suetake K, etal |title=Variations in gene expression patterns correlated with phenotype of F-11 tumor cells whose expression of GD3-synthase is suppressed. |journal=Cancer Lett. |volume=178 |issue= 1 |pages= 91–8 |year= 2002 |pmid= 11849746 |doi=10.1016/S0304-3835(01)00817-5 }}
  • {{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 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Furukawa K, Horie M, Okutomi K, etal |title=Isolation and functional analysis of the melanoma specific promoter region of human GD3 synthase gene. |journal=Biochim. Biophys. Acta |volume=1627 |issue= 2–3 |pages= 71–8 |year= 2003 |pmid= 12818424 |doi= 10.1016/s0167-4781(03)00076-9}}
  • {{cite journal | vauthors=Moon SK, Kim HM, Lee YC, Kim CH |title=Disialoganglioside (GD3) synthase gene expression suppresses vascular smooth muscle cell responses via the inhibition of ERK1/2 phosphorylation, cell cycle progression, and matrix metalloproteinase-9 expression. |journal=J. Biol. Chem. |volume=279 |issue= 32 |pages= 33063–70 |year= 2004 |pmid= 15175338 |doi= 10.1074/jbc.M313462200 |doi-access= free }}
  • {{cite journal | vauthors=Ha KT, Lee YC, Kim CH |title=Overexpression of GD3 synthase induces apoptosis of vascular endothelial ECV304 cells through downregulation of Bcl-2. |journal=FEBS Lett. |volume=568 |issue= 1–3 |pages= 183–7 |year= 2004 |pmid= 15196944 |doi= 10.1016/j.febslet.2004.05.020 |s2cid=34782656 |doi-access=free }}
  • {{cite journal |vauthors=Tomassini B, Malisan F, Franchi L, etal |title=Calnexin suppresses GD3 synthase-induced apoptosis. |journal=FASEB J. |volume=18 |issue= 13 |pages= 1553–5 |year= 2005 |pmid= 15319364 |doi= 10.1096/fj.04-1675fje |doi-access=free |s2cid=44936219 }}
  • {{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 }}
  • {{cite journal |vauthors=Teintenier-Lelièvre M, Julien S, Juliant S, etal |title=Molecular cloning and expression of a human hST8Sia VI (alpha2,8-sialyltransferase) responsible for the synthesis of the diSia motif on O-glycosylproteins. |journal=Biochem. J. |volume=392 |issue= Pt 3 |pages= 665–74 |year= 2006 |pmid= 16120058 |doi= 10.1042/BJ20051120 | pmc=1316308 }}
  • {{cite journal |vauthors=Kang NY, Kang Y, Kang SK, etal |title=Transcriptional regulation of the human GD3 synthase gene expression in Fas-induced Jurkat T cells: a critical role of transcription factor NF-kappaB in regulated expression. |journal=Glycobiology |volume=16 |issue= 5 |pages= 375–89 |year= 2006 |pmid= 16481330 |doi= 10.1093/glycob/cwj087 |doi-access= }}
  • {{cite journal |vauthors=Ko K, Furukawa K, Takahashi T, etal |title=Fundamental study of small interfering RNAs for ganglioside GD3 synthase gene as a therapeutic target of lung cancers. |journal=Oncogene |volume=25 |issue= 52 |pages= 6924–35 |year= 2006 |pmid= 16862187 |doi= 10.1038/sj.onc.1209683 |s2cid=30102036 |doi-access= }}
  • {{cite journal |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |issue=2 |pages= 210–270 |year= 2017 |doi= 10.1002/med.21407 |pmid=27678392 |s2cid=26280291 |url=http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5226&context=smhpapers }}

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