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Titolo:
Pathogenesis, diagnosis and treatment of systemic amyloidosis
Autore:
Pepys, MB;
Indirizzi:
Royal Free & Univ Coll Med Sch, Dept Med, Ctr Amyloidosis & Acute Phase Prot, London NW3 2PF, England Royal Free & Univ Coll Med Sch London EnglandNW3 2PF n NW3 2PF, England
Titolo Testata:
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES
fascicolo: 1406, volume: 356, anno: 2001,
pagine: 203 - 210
SICI:
0962-8436(20010228)356:1406<203:PDATOS>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
APOLIPOPROTEIN-A-I; P COMPONENT SCINTIGRAPHY; HAMSTER FEMALE PROTEIN; LIVER-TRANSPLANTATION; ALZHEIMERS-DISEASE; FIBRIL FORMATION; SYRIAN-HAMSTER; HUMAN LYSOZYME; VARIANT; DEPOSITS;
Keywords:
amyloidosis; diagnosis; serum amyloid P component; treatment;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Pepys, MB Royal Free & Univ Coll Med Sch, Dept Med, Ctr Amyloidosis & Acute Phase Prot, Rowland Hill St, London NW3 2PF, England Royal Free & Univ Coll Med Sch Rowland Hill St London England NW3 2PF
Citazione:
M.B. Pepys, "Pathogenesis, diagnosis and treatment of systemic amyloidosis", PHI T ROY B, 356(1406), 2001, pp. 203-210

Abstract

Amyloidosis is a disorder of protein folding in which normally soluble proteins are deposited as abnormal, insoluble fibrils that disrupt tissue structure and cause disease. Although about 20 different unrelated proteins canform amyloid fibrils in vivo, all such fibrils share a common cross-beta core structure. Some natural wild-type proteins are inherently amyloidogenic, form fibrils and cause amyloidosis in old age or if present for long periods at abnormally high concentration. Other amyloidogenic proteins are acquired or inherited variants, containing amino-acid substitutions that renderthem unstable so that they populate partly unfolded states under physiological conditions, and these intermediates then aggregate in the stable amyloid fold. In addition to the fibrils, amyloid deposits always contain the non-fibrillar pentraxin plasma protein, serum amyloid P component (SAP), because it undergoes specific calcium-dependent binding to amyloid fibrils. SAPcontributes to amyloidogeneses, probably by stabilizing amyloid fibrils and retarding their clearance. Radiolabelled SAP is an extremely useful, safe, specific, non-invasive, quantitative tracer for scintigraphic imaging of systemic amyloid deposits. Its use has demonstrated that elimination of thesupply of amyloid fibril precursor proteins leads to regression of amyloiddeposits with clinical benefit. Current treatment of amyloidosis comprisescareful maintenance of impaired organ function, replacement of end-stage organ failure by dialysis or transplantation, and vigorous efforts to control underlying conditions responsible for production of fibril precursors. New approaches under development include drugs for stabilization of the native fold of precursor proteins, inhibition of fibrillogenesis, reversion of the amyloid to the native fold, and dissociation of SAP to accelerate amyloid fibril clearance in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 12:18:24