Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linkedN-acetylgalactosamine
Autore:
Kang, HG; Evers, MR; Xia, GQ; Baenziger, U; Schachner, M;
Indirizzi:
Univ Hamburg, Zentrum Mol Neurobiol, D-20246 Hamburg, Germany Univ Hamburg Hamburg Germany D-20246 Neurobiol, D-20246 Hamburg, Germany Washington Univ, Sch Med, Dept Pathol, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 Dept Pathol, St Louis, MO 63110 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 14, volume: 276, anno: 2001,
pagine: 10861 - 10869
SICI:
0021-9258(20010406)276:14<10861:MCAEOA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ASPARAGINE-LINKED OLIGOSACCHARIDES; PITUITARY GLYCOPROTEIN HORMONES; MYELIN-ASSOCIATED GLYCOPROTEIN; HNK-1 CARBOHYDRATE EPITOPE; FIBROBLAST GROWTH-FACTOR; SIALYLATED OLIGOSACCHARIDES; CRYSTAL-STRUCTURE; HEPARAN-SULFATE; MONOCLONAL IGM; SULFOTRANSFERASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Schachner, M Univ Hamburg, Zentrum Mol Neurobiol, Martinistr 52, D-20246 Hamburg, Germany Univ Hamburg Martinistr 52 Hamburg Germany D-20246 , Germany
Citazione:
H.G. Kang et al., "Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linkedN-acetylgalactosamine", J BIOL CHEM, 276(14), 2001, pp. 10861-10869

Abstract

We have identified and characterized an N-acetyl-galaetosamine-4-O-sulfotransferase designated GalNAc-4-ST2 (GenBank(TM) accession number AF332472) based on its homology to HNK-1 sulfotransferase (HNK-1 ST). The cDNA predicts an open reading frame encoding a type II membrane protein of 443 amino acids with a 12-amino acid cytoplasmic domain, a 23-amino acid transmembrane domain, and a 408-amino acid luminal domain containing four potential N-linked glycosylation sites. GalNAc-4-ST2 displays a high degree of amino acid sequence identity with GalNAc-4-ST1 (46%), HNK-1 ST (23%), chondroitin 4-O-sulfotransferase-1 (C4ST-1) (27%), and chondroitin 4-O-sulfotransferase-2 (C4ST-2) (24%), GalNAc-4-ST2 transfers sulfate to the C-4 hydroxyl of terminal beta1,4-linked GalNAc in the sequence GalNAc beta1,4GlcNAc beta -R foundon N-linked oligosaccharides and nonterminal beta1,4-linked GalNAc in chondroitin and dermatan. The translated region of GalNAc-4-ST2 is encoded by five exons located on human chromosome 18q11.2, Northern blot analysis reveals a 2.1-kilobase transcript. GalNAc-4-ST2 message is most highly expressedin trachea and to a lesser extent in heart, liver, pancreas, salivary gland, and testis. The I.M.A.G.E. cDNA clone 49547 contains a putative GalNAc-4-ST2 splice form with an open reading frame encoding a protein of 358 aminoacids that lacks the transmembrane domain and the stem region. This form of GalNAc-4-ST2 is not retained by transfected cells and is active against chondroitin but not terminal beta1,4-linked GalNAc. Thus, as with GalNAc-4-ST1, sequences N-terminal to the catalytic domain contribute to the specificity of GalNAc-4-ST2 toward terminal beta1,4-linked GalNAc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 21:21:14