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Titolo:
Purification, molecular cloning and mechanism of action of graminelysin I,a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells
Autore:
Wu, WB; Chang, SC; Liau, MY; Huang, TF;
Indirizzi:
Natl Taiwan Univ, Coll Med, Dept Pharmacol, Taipei 10018, Taiwan Natl Taiwan Univ Taipei Taiwan 10018 ept Pharmacol, Taipei 10018, Taiwan Natl Taiwan Univ, Coll Med, Dept Microbiol, Taipei 10018, Taiwan Natl Taiwan Univ Taipei Taiwan 10018 ept Microbiol, Taipei 10018, Taiwan Natl Inst Prevent Med, Dept Hlth, Taipei 11513, Taiwan Natl Inst Prevent Med Taipei Taiwan 11513 ept Hlth, Taipei 11513, Taiwan
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 357, anno: 2001,
parte:, 3
pagine: 719 - 728
SICI:
0264-6021(20010801)357:<719:PMCAMO>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOCAL ADHESION KINASE; CROTALUS-ATROX VENOM; PLATELET-AGGREGATION; DISINTEGRIN-LIKE; HEMORRHAGIC METALLOPROTEINASES; BIOLOGICAL-ACTIVITY; PROTEASE ACTIVITY; FLOW-CYTOMETRY; ATROLYSIN-A; PROTEINS;
Keywords:
DNA fragmentation; endothelial cell detachment; extracellular matrix; metalloprotease; reprolysin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Huang, TF Natl Taiwan Univ, Coll Med, Dept Pharmacol, 1,Sec 1,Jen Ai Rd, Taipei 10018, Taiwan Natl Taiwan Univ 1,Sec 1,Jen Ai Rd Taipei Taiwan 10018, Taiwan
Citazione:
W.B. Wu et al., "Purification, molecular cloning and mechanism of action of graminelysin I,a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells", BIOCHEM J, 357, 2001, pp. 719-728

Abstract

Apoptosis, a programmed, physiological mode of cell death, is important intissue homoeostasis. Here we report that a new metalloproteinase, graminelysin I, purified from Trimeresurus gramineus venom, induced apoptosis of human endothelial cells as examined by electrophoresis and flow cytometry. Graminelysin I contains only a metalloproteinase domain. It is a single-chainproteinase with a molecular mass of 27020 Da. cDNA sequence analysis revealed that the disintegrin-like and cysteine-rich domains of the putative precursor protein of graminelysin I are likely to be processed post-translationally, producing the proteinase domain (graminelysin I). Graminelysin I cleaved the a chain of fibrinogen preferentially and cleaved the chain either on longer incubation or at higher concentration. Graminelysin I inhibited the adhesion of human umbilical-vein endothelial cells (HUVECs) to immobilized fibrinogen and induced HUVECs detachment in a dose-dependent manner. These effects on HUVECs were abolished when graminelysin I was pretreated withEDTA. However, graminelysin I did not inhibit the adhesion of HUVECs to immobilized collagen. HUVECs were susceptible to death after treatment with graminelysin I when they were cultured on immobilized fibrinogen. In contrast, HUVECs were rather resistant to treatment with graminelysin I if they were cultured on immobilized colla-en. Furthermore, graminelysin I induced apoptosis of HUVECs in a dose-dependent manner. Similarly, its apoptosis-inducing activity was blocked if it was treated with EDTA. These results suggest that the catalytic activity of graminelysin I on matrix proteins contributes to its apoptosis-inducing activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 21:42:26