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Titolo:
In vivo glycosylation of mucin tandem repeats
Autore:
Silverman, HS; Parry, S; Sutton-Smith, M; Burdick, MD; McDermott, K; Reid, CJ; Batra, SK; Morris, HR; Hollingsworth, MA; Dell, A; Harris, A;
Indirizzi:
Univ Oxford, John Radcliffe Hosp, Inst Mol Med, Oxford OX3 9DS, England Univ Oxford Oxford England OX3 9DS Inst Mol Med, Oxford OX3 9DS, England Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AZ,England Univ London Imperial Coll Sci Technol & Med London England SW7 2AZ gland Univ Nebraska, Med Ctr, Eppley Inst, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 ed Ctr, Eppley Inst, Omaha, NE 68198 USA Univ Nebraska, Med Ctr, Dept Biochem, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 d Ctr, Dept Biochem, Omaha, NE 68198 USA
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 6, volume: 11, anno: 2001,
pagine: 459 - 471
SICI:
0959-6658(200106)11:6<459:IVGOMT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYPEPTIDE-N-ACETYLGALACTOSAMINYLTRANSFERASE; MURINE MONOCLONAL-ANTIBODIES; CYSTIC FIBROTIC SPUTUM; BREAST-CANCER CELLS; O-GLYCOSYLATION; GALNAC ALPHA-2,6-SIALYLTRANSFERASE; MICROSOMAL PREPARATIONS; MUCUS GLYCOPROTEINS; MOLECULAR-CLONING; IN-VIVO;
Keywords:
glycosylation; mucin; tandem repeat; in vivo;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Harris, A Univ Oxford, John Radcliffe Hosp, Inst Mol Med, Oxford OX3 9DS, England Univ Oxford Oxford England OX3 9DS ed, Oxford OX3 9DS, England
Citazione:
H.S. Silverman et al., "In vivo glycosylation of mucin tandem repeats", GLYCOBIOLOG, 11(6), 2001, pp. 459-471

Abstract

The biochemical and biophysical properties of mucins are largely determined by extensive O-glycosylation of serine- and threonine-rich tandem repeat (TR) domains. In a number of human diseases aberrant O-glycosylation is associated with variations in the properties of the cell surface-associated and secreted mucins, To evaluate in vivo the O-glycosylation of mucin TR domains, we generated recombinant chimeric mucins with TR sequences from MUC2, MUC4 MUC5AC, or MUC5B, which were substituted for the native TRs of epitope-tagged MUC1 protein (MUC1F), These hybrid mucins were extensively O-glycosylated and showed the expected association with the cell surface and release into culture media. The presence of different TR domains within the chimeric mucins appears to have limited influence on their posttranslational processing. Alterations in glycosylation were detailed by fast atom bombardment mass spectrometry and reactivity with antibodies against particular blood-group and tumor-associated carbohydrate antigens, Future applications of these chimeras will include investigations of mucin posttranslational modification in the context of disease.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:12:05