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Evidence for metal inhibition of tumour membrane-bound neutral protease and the control of tumour-induced target cell cytolysis.

Abstract：

:Previous studies have characterized the enzymatic properties and inhibition of a trypsin-like neutral protease on the surface of Ehrlich ascites cells by means of kinetic analysis. The present study links these kinetic studies with the recently reported role of a tumour-cell membrane-bound serine protease in tumour-induced target cell lysis. Low-mol.-wt inhibitors of this cell-surface trypsin-like neutral protease exhibited a corresponding ability to prevent tumour-induced haemolysis. High-mol.-wt inhibitors of trypsin in free solution had no inhibitory action either on the tumour-bound enzyme or on the ability of tumour cells to lyse erythrocytes. Fragments of tumour-cell membrane retain both the trypsin-like neutral protease activity and the ability for haemolysis. This study represents a correlation between an easily assayed membrane-bound enzyme on tumour cells and a function of possible biological relevance.

journal_name

Br J Cancer

journal_title

British journal of cancer

authors

Steven FS,Hulley TP,Griffin MM,Itzhaki S

doi

10.1038/bjc.1982.304

subject

Has Abstract

pub_date

1982-12-01 00:00:00

pages

934-9

issue

6

eissn

0007-0920

issn

1532-1827

journal_volume

46

pub_type

杂志文章

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