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Titolo:
Glucose-modified proteins modulate essential functions and apoptosis of polymorphonuclear leukocytes
Autore:
Cohen, G; Rudnicki, M; Walter, F; Niwa, T; Horl, WH;
Indirizzi:
Univ Vienna, Med Klin 3, Dept Med, Div Nephrol, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 d, Div Nephrol, A-1090 Vienna, Austria Nagoya Univ, Branch Hosp, Dept Internal Med, Nagoya, Aichi, Japan Nagoya Univ Nagoya Aichi Japan , Dept Internal Med, Nagoya, Aichi, Japan
Titolo Testata:
JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY
fascicolo: 6, volume: 12, anno: 2001,
pagine: 1264 - 1271
SICI:
1046-6673(200106)12:6<1264:GPMEFA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOSYLATION END-PRODUCTS; NEUTROPHIL APOPTOSIS; DIALYSIS PATIENTS; HEXOSE-TRANSPORT; UREMIC PATIENTS; GLYCATION; CHEMOTAXIS; SERUM; HEMODIALYSIS; DYSFUNCTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Horl, WH Univ Vienna, Med Klin 3, Dept Med, Div Nephrol, Wahringer Gurtel 18-20, A-1090 Vienna, Austria Univ Vienna Wahringer Gurtel 18-20 Vienna Austria A-1090 Austria
Citazione:
G. Cohen et al., "Glucose-modified proteins modulate essential functions and apoptosis of polymorphonuclear leukocytes", J AM S NEPH, 12(6), 2001, pp. 1264-1271

Abstract

Any modulation of the activity of polymorphonuclear leukocytes (PMNL) is apotential cause of the altered immune response in uremia, Because the level of glycation products is elevated in uremic sera and peritoneal effluents, the effect of glycated proteins on essential functions and on apoptosis of PMNL was investigated. Proteins from sera of healthy donors were incubated with and without glucose. The extent of early glycation was monitored by boronate chromatography and the fructosamine assay. The formation of late glycation products was assessed by fluorescence spectroscopy and Western blotting that used a specific antibody for imidazolone, a late glycation product. With the addition of aminoguanidine, a compound that inhibits the formation of late but not of early glycation products, protein samples with early glycation only were obtained. Glucose-modified proteins increased chemotaxis and activation of the 2-deoxy-D-glucose uptake of PMNL obtained from healthy donors, compared with those of unmodified proteins. PMNL apoptosis, assessed by morphologic changes, by detecting DNA strand breaks, and by measurement of the caspase 3 activity, was increased in the presence of glucose-modified serum proteins. It was found that the formation of late glycationproducts is necessary for the effect on PMNL chemotaxis. In contrast, early glycation of proteins is responsible for the increase of glucose uptake and apoptosis. It was concluded that the accumulation of glycated proteins in uremic sera and peritoneal fluid may contribute to the diminished immune function observed in uremia, by modulation of essential PMNL functions and acceleration of PMNL apoptosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:16:48