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Titolo:
Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways
Autore:
Sousa, MM; Du Yan, S; Fernandes, R; Guimaraes, A; Stern, D; Saraiva, MJ;
Indirizzi:
Columbia Univ, Inst Mol & Cellular Biol, New York, NY 10032 USA Columbia Univ New York NY USA 10032 Cellular Biol, New York, NY 10032 USA Columbia Univ, Dept Pathol, New York, NY 10032 USA Columbia Univ New YorkNY USA 10032 , Dept Pathol, New York, NY 10032 USA Columbia Univ, Dept Surg, New York, NY 10032 USA Columbia Univ New York NY USA 10032 iv, Dept Surg, New York, NY 10032 USA Columbia Univ, Dept Physiol & Cellular Biophys, New York, NY 10032 USA Columbia Univ New York NY USA 10032 lular Biophys, New York, NY 10032 USA Hosp Geral de Santo Antonio, P-4150180 Oporto, Portugal Hosp Geral de Santo Antonio Oporto Portugal P-4150180 0 Oporto, Portugal Inst Ciencias Biomed Abel Salazar, P-4099003 Oporto, Portugal Inst Ciencias Biomed Abel Salazar Oporto Portugal P-4099003 to, Portugal
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 19, volume: 21, anno: 2001,
pagine: 7576 - 7586
SICI:
0270-6474(20011001)21:19<7576:FAPRFA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; ELECTRON-MICROSCOPE; PERIPHERAL-NERVE; CELL STRESS; PEPTIDE; TRANSTHYRETIN; RAGE; TOXICITY; NEUROTOXICITY; AGGREGATION;
Keywords:
familial amyloidotic polyneuropathy; amyloid; transthyretin; RAGE; caspase-3; inducible nitric oxide synthase; inflammatory cytokine;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Saraiva, MJ IBMC, Amyloid Unit, R Campo Alegre 823, P-4150180 Oporto, Portugal IBMC R Campo Alegre 823 Oporto Portugal P-4150180 o, Portugal
Citazione:
M.M. Sousa et al., "Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways", J NEUROSC, 21(19), 2001, pp. 7576-7586

Abstract

Familial amyloid polyneuropathy (FAP) is a neurodegenerative disorder associated with extracellular deposition of mutant transthyretin (TTR) amyloid fibrils, particularly in the peripheral nervous system. We have hypothesized that binding of TTR fibrils to the receptor for advanced glycation end products (RAGE) on critical cellular targets is associated with a destructivestress response underlying peripheral nerve dysfunction. Analysis of nervebiopsy samples from patients with FAP (n = 16) at different stages of disease (0-3), compared with age-matched controls (n = 4), by semiquantitative immunohistology and in situ hybridization showed increased levels of RAGE, beginning at the earliest stages of the disease (FAP 0; p < 0.02) and especially localized In axons. Upregulation of proinflammatory cytokines (tumor necrosis factor-a and interleukin-1<beta>) (approximately threefold; p < 0.02) and the inducible form of nitric oxide synthase (iNOS) (<similar to>2.5-fold; p < 0.04) was also observed in a distribution overlapping RAGE expression. Tyrosine nitration and increased activated caspase-3 in axons from FAP patients (p < 0.03) were apparent. Although these data suggest the presence of ongoing neuronal stress, there was no upregulation of neurotrophins (nerve growth factor and neurotrophin-3) in FAP nerves. Studies on culturedneuronal-like, Schwann, and endothelial cells incubated with TTR fibrils displayed RAGE-dependent expression of cytokines and iNOS at early times (6 and 12 hr, respectively), followed by later (24 hr) activation of caspase-3and DNA fragmentation. We propose that the interaction of TTR fibrils withRAGE may contribute to cellular stress and toxicity in FAR Furthermore, there is an apparent lack of responsiveness of Schwann cells in FAP nerve to provide neurotrophic factors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 17:19:41