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Titolo:
O-glycosylation of the mucin type
Autore:
Hanisch, FA;
Indirizzi:
Univ Cologne, Fac Med, Inst Biochem, D-50931 Cologne, Germany Univ Cologne Cologne Germany D-50931 t Biochem, D-50931 Cologne, Germany
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 382, anno: 2001,
pagine: 143 - 149
SICI:
1431-6730(200102)382:2<143:OOTMT>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE; RESPIRATORY-MUCUS GLYCOPROTEINS; 500-MHZ H-1-NMR SPECTROSCOPY; QUANTITATIVE SUGAR ANALYSIS; BREAST-CANCER CELLS; HUMAN COLONIC MUCIN; SKIM MILK MUCINS; TANDEM REPEAT; UDP-GALNAC; NEUTRAL OLIGOSACCHARIDES;
Keywords:
glycoproteins; mucins; O-glycosylation; O-linked oligosaccharides;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Hanisch, FA Univ Cologne, Fac Med, Inst Biochem, Joseph-Stelzmann-Str 52, D-50931 Cologne, Germany Univ Cologne Joseph-Stelzmann-Str 52 Cologne Germany D-50931
Citazione:
F.A. Hanisch, "O-glycosylation of the mucin type", BIOL CHEM, 382(2), 2001, pp. 143-149

Abstract

While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteinsare glycoproteins. Mucin-type O-glycosylation is a widespread post-translational modification of proteins found in the entire animal kingdom, but also in higher plants, The structural complexity of the chains initiated by O-linked GalNAc exceeds that of N-linked chains by far, The process during which serine and threonine residues of proteins become modified is confined to the cis to trans Golgi compartments. The initiation of this process by peptidyl GalNAc-transferases is ruled by the sequence context of putative O-glycosylation sites, but also by epigenetic regulatory mechanisms, which canbe mediated by enzyme competition. The cellular repertoir of glycosyltransferases with their distinct donor sugar and acceptor sugar specificities, their sequential action at highly-ordered surfaces, and their localizations in subcompartments of the Golgi finally determine the cell-specific O-glycosylation profile. Dramatic alterations of the glycosylation machinery are observed in cancer cells, resulting in aberrantly O-glycosylated proteins that expose previously masked peptide motifs and new antigenic targets, The functional aspects of O-linked glycans, which comprise among many others their potential role in sorting and secretion of glycoproteins, their influence on protein conformation, and their multifarious involvement in cell adhesion and immunological processes, appear as complex as their structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 23:40:32