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Titolo:
Diabetes and mass spectrometry
Autore:
Lapolla, A; Fedele, D; Traldi, P;
Indirizzi:
Univ Padua, Cattedra Malattie Metab, Dipartimento Sci Med & Chirurg, I-35100 Padua, Italy Univ Padua Padua Italy I-35100 o Sci Med & Chirurg, I-35100 Padua, Italy CNR, Ctr Studio Stabil & Reativita Composti Coordinaz, I-35100 Padua, Italy CNR Padua Italy I-35100 ativita Composti Coordinaz, I-35100 Padua, Italy
Titolo Testata:
DIABETES-METABOLISM RESEARCH AND REVIEWS
fascicolo: 2, volume: 17, anno: 2001,
pagine: 99 - 112
SICI:
1520-7552(200103/04)17:2<99:DAMS>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOSYLATION END-PRODUCTS; NON-ENZYMATIC GLYCOSYLATION; MAILLARD REACTION INVIVO; FC FRAGMENT FUNCTION; IN-VITRO GLYCATION; NONENZYMATIC GLYCATION; PROTEIN GLYCATION; OXIDATIVE STRESS; IMMUNOGLOBULIN-G; GLYCO-OXIDATION;
Keywords:
diabetes; non-enzymatic protein glycation; mass spectrometry; immunoglobulins; haemoglobin;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
87
Recensione:
Indirizzi per estratti:
Indirizzo: Lapolla, A Univ Padua, Cattedra Malattie Metab, Dipartimento Sci Med & Chirurg, Via Vendramini 7, I-35100 Padua, Italy Univ Padua Via Vendramini 7 Padua Italy I-35100 0 Padua, Italy
Citazione:
A. Lapolla et al., "Diabetes and mass spectrometry", DIABET M R, 17(2), 2001, pp. 99-112

Abstract

Mass spectrometry (MS) has been successfully employed to investigate nonenzymatic protein glycation, a process relevant in diabetic disease. The highsensitivity and specificity of this technique allowed the development of methods that can individuate and evaluate some glycation markers to be validly employed in monitoring diabetes. More recent mass spectrometric techniques, such as the matrix-assisted laser desorption/ionization (MALDI), are able to determine the molecular weight of intact proteins. They were first employed in studying the in vitro reaction between hexoses and different proteins. Once the validity of the results obtained by this analytical approachwas confirmed, a series of investigations on plasma proteins were undertaken in healthy and diabetic subjects. The method led to the evaluation of the number of glucose molecules condensed on the protein being studied, and consequently can be validly used for an accurate follow-up of metabolic control in diabetic patients. When applied to studies on haemoglobin glycation,the method showed that both alpha- and beta -globins are glycated to a similar extent and that the simply glycated molecules are accompanied by glyco-oxidized species therefore giving information on the oxidative stress experimented on in the subject. Furthermore, in the case of immunoglobulins, MALDI/MS was able to determine not only the total glycation level of IgG, butalso to establish that the fragment antigen binding (Fab) moiety is the most glycated one, thus suggesting that the possible immunological impairmentsometimes invoked in diabetes is related to the inhibition of the process of molecular recognition between antibody and antigen. Copyright (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 18:46:35