Comparison of snake venom reprolysin and matrix metalloproteinases as models of TNF-alpha converting enzyme

被引：10

作者：

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

机构：

[1] DUPONT CO INC,MERCK RES LABS,INFLAMMATORY DIS RES & CHEM & PHYS SCI,WILMINGTON,DE 19880

[2] UNIV VIRGINIA,DEPT MICROBIOL,CHARLOTTESVILLE,VA 22908

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1997年 / 7卷 / 10期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0960-894X(97)00148-0

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The reprolysin ht-d was compared to several human MMPs for the ability to cleave a peptide substrate representing the processing site of human pro-TNF. The rank order of inhibitor potency for a series of hydroxamic 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.

引用

页码：1219 / 1224

页数：6

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