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Titolo:
Protein glycosylation and diseases: Blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring
Autore:
Durand, G; Seta, N;
Indirizzi:
Hop Bichat Claude Bernard APHP, Biochim Lab A, F-75877 Paris 18, France Hop Bichat Claude Bernard APHP Paris France 18 F-75877 Paris 18, France UFR Sci Pharmaceut & Biol Paris XI, Biochim Gen Lab, F-92260 Chatenay Malabry, France UFR Sci Pharmaceut & Biol Paris XI Chatenay Malabry France F-92260 rance Univ Paris 05, Fac Pharm, F-75270 Paris 06, France Univ Paris 05 Paris France 06 is 05, Fac Pharm, F-75270 Paris 06, France
Titolo Testata:
CLINICAL CHEMISTRY
fascicolo: 6, volume: 46, anno: 2000,
parte:, 1
pagine: 795 - 805
SICI:
0009-9147(200006)46:6<795:PGADBA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEFICIENT GLYCOPROTEIN-SYNDROME; WISKOTT-ALDRICH SYNDROME; WHEAT-GERM LECTIN; SYNDROME TYPE-II; CONCANAVALIN-A; ALPHA-FETOPROTEIN; PATHOLOGICAL CATABOLISM; ALKALINE-PHOSPHATASE; GLYCAN SYNTHESIS; SUGAR CHAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Seta, N Hop Bichat Claude Bernard APHP, Biochim Lab A, 46 Rue H Huchard, F-75877 Paris 18, France Hop Bichat Claude Bernard APHP 46 Rue H Huchard Paris France 18 e
Citazione:
G. Durand e N. Seta, "Protein glycosylation and diseases: Blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring", CLIN CHEM, 46(6), 2000, pp. 795-805

Abstract

Background:: N- and O-oligosaccharide variants on glycoproteins (glycoforms) can lead to alterations in protein activity or function that may manifest themselves as overt disease. Approach: This review summarizes those diseases that are known to be the result of an inherited or acquired glycoprotein oligosaccharide structural alteration and that are diagnosed in blood or urine by chemical characterization of that oligosaccharide alteration. Content: The biochemical synthesis steps and catabolic pathways important in determining glycoprotein function are outlined with emphasis on alterations that lead to modified function. Clinical and biochemical aspects of thediagnosis are described for inherited diseases such as I-cell disease, congenital disorders of glycosylation, leukocyte adhesion deficiency type II, hereditary erythroblastic multinuclearity with a positive acidified serum test, and Wiskott-Aldrich syndrome. We also review the laboratory use of measurements of glycoforms related to acquired diseases such as alcoholism andcancer. Conclusions: Identification of glycoprotein glycoforms is becoming an increasingly important laboratory contribution to the diagnosis and management of human diseases as more diseases are found to result from glycan structural alterations, (C) 2000 American Association for Clinical Chemistry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 19:57:29