释义 |
- References
- Further reading
{{Infobox_gene}}CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA4 gene.[1][2]{{PBB_Summary | section_title = | summary_text = The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.[2] }}References1. ^{{cite journal |vauthors=Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M | title = Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain | journal = Proc Natl Acad Sci U S A | volume = 92 | issue = 15 | pages = 7031–5 |date=Aug 1995 | pmid = 7624364 | pmc = 41465 | doi =10.1073/pnas.92.15.7031 }} 2. ^1 {{cite web | title = Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7903| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Cohn JA, Noone PG, Jowell PS |title=Idiopathic pancreatitis related to CFTR: complex inheritance and identification of a modifier gene |journal=J. Investig. Med. |volume=50 |issue= 5 |pages= 247S–255S |year= 2002 |pmid= 12227654 |doi= }}
- {{cite journal | author=Eckhardt M |title=Molecular characterization of eukaryotic polysialyltransferase-1 |journal=Nature |volume=373 |issue= 6516 |pages= 715–8 |year= 1995 |pmid= 7854457 |doi= 10.1038/373715a0 |name-list-format=vanc| author2=Mühlenhoff M | author3=Bethe A | display-authors=3 | last4=Koopman | first4=Jaap | last5=Frosch | first5=Matthias | last6=Gerardy-Schahn | first6=Rita }}
- {{cite journal | author=Angata K |title=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 |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7182–90 |year= 1997 |pmid= 9054414 |doi=10.1074/jbc.272.11.7182 |name-list-format=vanc| author2=Nakayama J | author3=Fredette B | display-authors=3 | last4=Chong | first4=K | last5=Ranscht | first5=B | last6=Fukuda | first6=M }}
- {{cite journal |vauthors=Angata K, Suzuki M, Fukuda M |title=Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28524–32 |year= 1998 |pmid= 9774483 |doi=10.1074/jbc.273.43.28524 }}
- {{cite journal |vauthors=Close BE, Colley KJ |title=In vivo autopolysialylation and localization of the polysialyltransferases PST and STX |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34586–93 |year= 1999 |pmid= 9852130 |doi=10.1074/jbc.273.51.34586 }}
- {{cite journal |vauthors=Close BE, Tao K, Colley KJ |title=Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4484–91 |year= 2000 |pmid= 10660622 |doi=10.1074/jbc.275.6.4484 }}
- {{cite journal | author=Angata K |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 |name-list-format=vanc| author2=Suzuki M | author3=McAuliffe J | display-authors=3 | last4=Ding | first4=Y | last5=Hindsgaul | first5=O | last6=Fukuda | first6=M }}
- {{cite journal | author=Angata K |title=Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15369–77 |year= 2001 |pmid= 11279095 |doi= 10.1074/jbc.M100576200 |name-list-format=vanc| author2=Yen TY | author3=El-Battari A | display-authors=3 | last4=Macher | first4=BA | last5=Fukuda | first5=M }}
- {{cite journal | author=Close BE |title=The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule |journal=Glycobiology |volume=11 |issue= 11 |pages= 997–1008 |year= 2002 |pmid= 11744634 |doi=10.1093/glycob/11.11.997 |name-list-format=vanc| author2=Wilkinson JM | author3=Bohrer TJ | display-authors=3 | last4=Goodwin | first4=CP | last5=Broom | first5=LJ | last6=Colley | first6=KJ }}
- {{cite journal | author=Nałogowska-Głośnicka K |title=[Relationship between SA gene Pst1 polymorphism and predisposition to H-gestosis] |journal=Pol. Arch. Med. Wewn. |volume=107 |issue= 1 |pages= 7–11 |year= 2002 |pmid= 12046348 |doi= |name-list-format=vanc| author2=Łacka B | author3=Zychma M | display-authors=3 | last4=Grzeszczak | first4=W | last5=Zukowska-Szczechowska | first5=E | last6=Michalski | first6=B | last7=Poreba | first7=R | last8=Kniazewski | first8=B | last9=Rzempołuch | first9=J }}
- {{cite journal |vauthors=Angata K, Suzuki M, Fukuda M |title=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 |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36808–17 |year= 2002 |pmid= 12138100 |doi= 10.1074/jbc.M204632200 }}
- {{cite journal | author=Strausberg RL |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 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }}
- {{cite journal | author=Gerhard DS |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 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
- {{cite journal | author=Beecken WD |title=Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells |journal=Int. Immunopharmacol. |volume=5 |issue= 4 |pages= 757–69 |year= 2005 |pmid= 15710344 |doi= 10.1016/j.intimp.2004.12.009 |name-list-format=vanc| author2=Engl T | author3=Ogbomo H | display-authors=3 | last4=Relja | first4=B | last5=Cinatl | first5=J | last6=Bereiterhahn | first6=J | last7=Oppermann | first7=E | last8=Jonas | first8=D | last9=Blaheta | first9=R }}
- {{cite journal |vauthors=Mendiratta SS, Sekulic N, Lavie A, Colley KJ |title=Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST |journal=J. Biol. Chem. |volume=280 |issue= 37 |pages= 32340–8 |year= 2005 |pmid= 16027151 |doi= 10.1074/jbc.M506217200 }}
- {{cite journal |vauthors=Wang B, Hu H, Yu B |title=Molecular characterization of pig ST8Sia IV--a critical gene for the formation of neural cell adhesion molecule and its response to sialic acid supplement in piglets |journal=Nutritional neuroscience |volume=9 |issue= 3–4 |pages= 147–54 |year= 2007 |pmid= 17176637 |doi=10.1080/10284150600903594 }}
- {{cite journal |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |pages= 210-270 |year= 2017 |doi= 10.1002/med.21407 }}
{{refend}}{{Glycosyltransferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{2.4-enzyme-stub}}{{gene-5-stub}} 1 : EC 2.4.99 |