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Titolo:
PROPERTIES OF FIBRINOGEN CLEAVED BY JARARHAGIN, A METALLOPROTEINASE FROM THE VENOM OF BOTHROPS-JARARACA
Autore:
KAMIGUTI AS; SLUPSKY JR; ZUZEL M; HAY CRM;
Indirizzi:
UNIV LIVERPOOL,ROYAL LIVERPOOL HOSP,DEPT HAEMATOL,PRESCOT ST LIVERPOOL L69 3BX ENGLAND
Titolo Testata:
Thrombosis and haemostasis
fascicolo: 2, volume: 72, anno: 1994,
pagine: 244 - 249
SICI:
0340-6245(1994)72:2<244:POFCBJ>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET-AGGREGATION; SNAKE-VENOM; ALPHA-CHAIN; GAMMA-CHAIN; POLYMERIZATION SITES; BLOOD-COAGULATION; HEMORRHAGIC METALLOPROTEINASES; ACTIVATED PLATELETS; RECOGNITION SITE; BINDING-SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
A.S. Kamiguti et al., "PROPERTIES OF FIBRINOGEN CLEAVED BY JARARHAGIN, A METALLOPROTEINASE FROM THE VENOM OF BOTHROPS-JARARACA", Thrombosis and haemostasis, 72(2), 1994, pp. 244-249

Abstract

Haemorrhagic metalloproteinases from Bothrops jararaca and other venoms degrade vessel-wall and plasma proteins involved in platelet plug and fibrin clot formation. These enzymes also cause proteolytic digestion of fibrinogen which has been suggested to cause defective platelet function. Fibrinogen degradation by jararhagin, a metalloproteinase from B. jararaca, and the effect of jararhagin fibrinogenolysis on both platelet aggregation and fibrin clot formation were investigated. Jararhagin was found to cleave human fibrinogen in the C-terminal region of the A alpha-chain giving rise to a 285-290 kDa fibrinogen molecule lacking the A alpha-chain RGD 572-574 platelet-binding site. Platelet binding and aggregation of ADP-activated platelets is unaffected by this modification. This indicates that the lost site is not essential forplatelet aggregation, and that the remaining platelet binding sites located in the N-terminal portion of Aa: chains (RGD 95-97) and the C-terminal of gamma chains (dodecapeptide 400-411) are unaffected by jararhagin-digestion of fibrinogen. Fibrin clot formation with thrombin ofthis remnant fibrinogen molecule was defective, with poor polymer ization of fibrin monomers but normal release of FPA. The abnormal polymerization could be explained by the loss of one of the two complementary polymerization sites required for side-by-side association of fibrinprotofibrils. Jararhagin-induced inhibition of platelet function, an important cause of haemorrhage in envenomed patients, is not caused byproteolysis of fibrinogen, as had been thought, and the mechanism remains to be elucidated.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:37:40