COMPARISON OF SNAKE-VENOM REPROLYSIN AND MATRIX METALLOPROTEINASES ASMODELS OF TNF-ALPHA CONVERTING-ENZYME

Authors
VANDYK DE MARCHAND P BRUCKNER RC FOX JW JAFFEE BD GUNYUZLU PL DAVIS GL NURNBERG S COVINGTON M DECICCO CP TRZASKOS JM MAGOLDA RL COPELAND RA
Citation
De. Vandyk et al., COMPARISON OF SNAKE-VENOM REPROLYSIN AND MATRIX METALLOPROTEINASES ASMODELS OF TNF-ALPHA CONVERTING-ENZYME, Bioorganic & medicinal chemistry letters, 7(10), 1997, pp. 1219-1224
Citations number
19
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
7
Issue
10
Year of publication
1997
Pages
1219 - 1224
Database
ISI
SICI code
0960-894X(1997)7:10<1219:COSRAM>2.0.ZU;2-4
Abstract
The reprolysin ht-d was compared to several human MMPs for the ability to cleave a peptide substrate representing the processing site of hum an pro-TNF. The rank order of inhibitor potency for a series of hydrox amic acids was also compared among these enzymes and for inhibition of TNF release from human white blood cells. The results suggest that ht -d is a better model TNF convertase than are the human MMPs. (C) 1997 The DuPont Merck Pharmaceutical Company.