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Titolo:
THE RECEPTOR FOR ADVANCED GLYCATION END-PRODUCTS (RAGE) IS A CENTRAL MEDIATOR OF THE INTERACTION OF AGE-BETA(2)MICROGLOBULIN WITH HUMAN MONONUCLEAR PHAGOCYTES VIA AN OXIDANT-SENSITIVE PATHWAY - IMPLICATIONS FOR THE PATHOGENESIS OF DIALYSIS-RELATED AMYLOIDOSIS
Autore:
MIYATA T; HORI O; ZHANG JH; YAN SD; FERRAN L; LIDA Y; SCHMIDT AM;
Indirizzi:
COLUMBIA UNIV COLL PHYS & SURG,DEPT SURG,630 W 168TH ST,P&S 11-518 NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT SURG NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT MED NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT PATHOL NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT PHYSIOL NEW YORK NY 10032 NAGOYA UNIV,SCH MED,BRANCH HOSP,DEPT INTERNAL MED NAGOYA AICHI 461 JAPAN
Titolo Testata:
The Journal of clinical investigation
fascicolo: 5, volume: 98, anno: 1996,
pagine: 1088 - 1094
SICI:
0021-9738(1996)98:5<1088:TRFAGE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADVANCED GLYCOSYLATION; INTERLEUKIN-6 PRODUCTION; POTENTIAL MECHANISM; LIPID-PEROXIDATION; ALZHEIMER-DISEASE; MAILLARD REACTION; VASCULAR-DISEASE; BINDING-PROTEINS; GENE-EXPRESSION; CELL-ADHESION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
T. Miyata et al., "THE RECEPTOR FOR ADVANCED GLYCATION END-PRODUCTS (RAGE) IS A CENTRAL MEDIATOR OF THE INTERACTION OF AGE-BETA(2)MICROGLOBULIN WITH HUMAN MONONUCLEAR PHAGOCYTES VIA AN OXIDANT-SENSITIVE PATHWAY - IMPLICATIONS FOR THE PATHOGENESIS OF DIALYSIS-RELATED AMYLOIDOSIS", The Journal of clinical investigation, 98(5), 1996, pp. 1088-1094

Abstract

An important component of amyloid fibrils in dialysis-related amyloidosis is a form of beta(2)microglobulin modified with advanced glycation end products (AGEs) of the Maillard reaction, known as AGE-beta(2)M. We demonstrate here that the interaction of AGE-beta(2)M with mononuclear phagocytes (MPs), cells important in the pathogenesis of the inflammatory arthropathy of dialysis-related amyloidosis, is mediated by the receptor for AGEs, or RAGE. I-125-AGE-beta(2)M bound to immobilizedRAGE or to MPs in a specific, dose-dependent manner (K-d approximate to 53.5 and approximate to 81.6 nM, respectively), a process inhibitedin the presence of RAGE blockade, AGE-beta(2)M-mediated monocyte chemotaxis was prevented by excess sRAGE or anti-RAGE IgG, Induction of tumor necrosis factor-alpha (TNF) expression by MPs exposed to AGE-beta(2)M resulted from engagement of RAGE, as appearances of TNF transcripts and TNF antigen release into culture supernatants were prevented by addition of sRAGE, a process mediated, at least in part, by oxidant stress, AGE beta(2)M reduced cytochrome c and the elaboration of TNF by MPs was inhibited by N-acetylcysteine. Consistent with these data, immunohistochemical studies of AGE-laden amyloid deposits of a long-term hemodialysis patient revealed positive staining for RAGE in the MPs infiltrating these lesions. These data indicate that RAGE is a central binding site for AGEs formed in vivo and suggest that AGE-beta(2)M-MP-RAGE interaction likely contributes to the initiation of an inflammatory response in amyloid deposits of long-term hemodialysis patients, a process which may ultimately lead to bone and joint destruction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 08:24:53