ST8SIA1

Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA1 gene.^[5][6]

ST8SIA1
Identifiers
Aliases	ST8SIA1, GD3S, SIAT8, SIAT8-A, SIAT8A, ST8SiaI, ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1
External IDs	OMIM: 601123; MGI: 106011; HomoloGene: 2282; GeneCards: ST8SIA1; OMA:ST8SIA1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12p12.1 Start 22,063,773 bp[1] End 22,437,041 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 G3|6 74.78 cM Start 142,767,271 bp[2] End 142,910,178 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence Achilles tendon right hemisphere of cerebellum gonad muscle layer of sigmoid colon prefrontal cortex right adrenal cortex C1 segment testicle Top expressed in molar facial motor nucleus medial vestibular nucleus anterior horn of spinal cord deep cerebellar nuclei pontine nuclei dorsal tegmental nucleus substantia nigra proximal tubule habenula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity sialyltransferase activity glycosyltransferase activity alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Cellular component integral component of membrane Golgi membrane Golgi apparatus membrane Biological process glycosphingolipid biosynthetic process sialylation protein glycosylation cellular response to heat positive regulation of cell population proliferation sphingolipid metabolic process lipid metabolism carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6489 20449 Ensembl ENSG00000111728 ENSMUSG00000030283 UniProt Q92185 Q64687 RefSeq (mRNA) NM_001304450 NM_003034 NM_011374 RefSeq (protein) NP_001291379 NP_003025 NP_035504 Location (UCSC) Chr 12: 22.06 – 22.44 Mb Chr 6: 142.77 – 142.91 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[6]

In melanocytic cells, ST8SIA1 gene expression may be regulated by MITF.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000111728 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030283 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M (Dec 1993). "Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection". J Biol Chem. 268 (30): 22782–7. doi:10.1016/S0021-9258(18)41595-5. PMID 7901202.
6. "Entrez Gene: ST8SIA1 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1".
7. Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. S2CID 24698373.

Further reading

• Haraguchi M, Yamashiro S, Yamamoto A, et al. (1994). "Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2,8-sialyltransferase cDNA using anti-GD2 monoclonal antibody". Proc. Natl. Acad. Sci. U.S.A. 91 (22): 10455–9. Bibcode:1994PNAS...9110455H. doi:10.1073/pnas.91.22.10455. PMC 45039. PMID 7937974.
• Nara K, Watanabe Y, Maruyama K, et al. (1994). "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". Proc. Natl. Acad. Sci. U.S.A. 91 (17): 7952–6. Bibcode:1994PNAS...91.7952N. doi:10.1073/pnas.91.17.7952. PMC 44522. PMID 8058740.
• Sasaki K, Kurata K, Kojima N, et al. (1994). "Expression cloning of a GM3-specific alpha-2,8-sialyltransferase (GD3 synthase)". J. Biol. Chem. 269 (22): 15950–6. doi:10.1016/S0021-9258(17)40773-3. PMID 8195250.
• Nakayama J, Fukuda MN, Hirabayashi Y, et al. (1996). "Expression cloning of a human GT3 synthase. GD3 AND GT3 are synthesized by a single enzyme". J. Biol. Chem. 271 (7): 3684–91. doi:10.1074/jbc.271.7.3684. PMID 8631981.
• Matsuda Y, Nara K, Watanabe Y, et al. (1996). "Chromosome mapping of the GD3 synthase gene (SIAT8) in human and mouse". Genomics. 32 (1): 137–9. doi:10.1006/geno.1996.0090. PMID 8786103.
• De Maria R, Lenti L, Malisan F, et al. (1997). "Requirement for GD3 ganglioside in CD95- and ceramide-induced apoptosis". Science. 277 (5332): 1652–5. doi:10.1126/science.277.5332.1652. hdl:11566/37451. PMID 9287216.
• Angata K, Suzuki M, McAuliffe J, et al. (2000). "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". J. Biol. Chem. 275 (24): 18594–601. doi:10.1074/jbc.M910204199. PMID 10766765.
• Zeng G, Gao L, Suetake K, et al. (2002). "Variations in gene expression patterns correlated with phenotype of F-11 tumor cells whose expression of GD3-synthase is suppressed". Cancer Lett. 178 (1): 91–8. doi:10.1016/S0304-3835(01)00817-5. PMID 11849746.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Furukawa K, Horie M, Okutomi K, et al. (2003). "Isolation and functional analysis of the melanoma specific promoter region of human GD3 synthase gene". Biochim. Biophys. Acta. 1627 (2–3): 71–8. doi:10.1016/s0167-4781(03)00076-9. PMID 12818424.
• Moon SK, Kim HM, Lee YC, Kim CH (2004). "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". J. Biol. Chem. 279 (32): 33063–70. doi:10.1074/jbc.M313462200. PMID 15175338.
• Ha KT, Lee YC, Kim CH (2004). "Overexpression of GD3 synthase induces apoptosis of vascular endothelial ECV304 cells through downregulation of Bcl-2". FEBS Lett. 568 (1–3): 183–7. doi:10.1016/j.febslet.2004.05.020. PMID 15196944. S2CID 34782656.
• Tomassini B, Malisan F, Franchi L, et al. (2005). "Calnexin suppresses GD3 synthase-induced apoptosis". FASEB J. 18 (13): 1553–5. doi:10.1096/fj.04-1675fje. PMID 15319364. S2CID 44936219.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Teintenier-Lelièvre M, Julien S, Juliant S, et al. (2006). "Molecular cloning and expression of a human hST8Sia VI (alpha2,8-sialyltransferase) responsible for the synthesis of the diSia motif on O-glycosylproteins". Biochem. J. 392 (Pt 3): 665–74. doi:10.1042/BJ20051120. PMC 1316308. PMID 16120058.
• Kang NY, Kang Y, Kang SK, et al. (2006). "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". Glycobiology. 16 (5): 375–89. doi:10.1093/glycob/cwj087. PMID 16481330.
• Ko K, Furukawa K, Takahashi T, et al. (2006). "Fundamental study of small interfering RNAs for ganglioside GD3 synthase gene as a therapeutic target of lung cancers". Oncogene. 25 (52): 6924–35. doi:10.1038/sj.onc.1209683. PMID 16862187. S2CID 30102036.
• Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.