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Titolo:
DETECTION AND CHARACTERIZATION OF METALLOPROTEINASES WITH GELATINOLYTIC, FIBRONECTINOLYTIC AND FIBRINOGENOLYTIC ACTIVITIES IN BROWN SPIDER (LOXOSCELES INTERMEDIA) VENOM
Autore:
FEITOSA L; GREMSKI W; VEIGA SS; ELIAS MCQB; GRANER E; MANGILI OC; BRENTANI RR;
Indirizzi:
UNIV FED PARANA,DEPT CELL BIOL,JARDIM AMER BR-81531990 CURITIBA PARANA BRAZIL UNIV FED PARANA,DEPT CELL BIOL BR-81531990 CURITIBA PARANA BRAZIL LUDWIG INST CANC RES SAO PAULO BRAZIL UNIV FED PARANA,DEPT PHYSIOL BR-81531990 CURITIBA PARANA BRAZIL UNICAMP,DEPT ORAL PATHOL PIRACICABA BRAZIL
Titolo Testata:
Toxicon (Oxford)
fascicolo: 7, volume: 36, anno: 1998,
pagine: 1039 - 1051
SICI:
0041-0101(1998)36:7<1039:DACOMW>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATRIX METALLOPROTEINASES; IV COLLAGENASE; HEMORRHAGIC METALLOPROTEINASES; CROTALUS-ATROX; SEQUENCE; PROTEINS; GENE; FIBROBLAST; INHIBITORS; CLEAVAGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
L. Feitosa et al., "DETECTION AND CHARACTERIZATION OF METALLOPROTEINASES WITH GELATINOLYTIC, FIBRONECTINOLYTIC AND FIBRINOGENOLYTIC ACTIVITIES IN BROWN SPIDER (LOXOSCELES INTERMEDIA) VENOM", Toxicon (Oxford), 36(7), 1998, pp. 1039-1051

Abstract

By studying Loxosceles intermedia (Brown spider) venom we were able to detect a proteolytic action on fibronectin and fibrinogen but an inability to degrade full length laminin, type I and type IV collagens. By studying enzyme inhibitors we observed that divalent metal chelatorsas EDTA and 1,10-phenanthroline completely blocked this cleaving action whereas serine-protease inhibitors, thiol-protease inhibitor and acid-protease inhibitor showed little or no effect on the proteolytic activity of the venom indicating involvement of a metalloproteinase. Zymogram analysis of venom detected a 35 kDa molecule with gelatinolytic activity. The metalloproteinase nature was further supported by its sensitivity to 4-aminophenyl mercuric acetate (APMA) treatment which decreased its molecular weight to 32 kDa, inhibition of its gelatinolyticeffect by 1,10-phenanthroline and its elution from gelatin-sepharose affinity beads. In addition, zymogram experiments using fibronectin and fibrinogen as substrates detected a fibronectinolytic and fibrinogenolytic band at 28 kDa which changed its electrophoretic mobility to 20kDa band after organomercurial treatment. The inhibitory effect of 1,10 phenanthroline and APMA sensitivity on this proteolytic effect confirmed the presence of a second metalloproteinase in the venom. The data presented herein describe two invertebrate metalloproteinases in L. intermedia venom with different specificities one gelatinolytic and another, fibronectinolytic and fibrinogenolytic, probably involved in the harmful effects of the venom. (C) 1998 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 08:14:31