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Inactivation of bradykinin and kallidin by cathepsin G and mast cell chymase.

Abstract：

:Human neutrophil cathepsin G and human skin chymase can inactivate bradykinin by cleavage at the carboxy terminal phenylalanyl-arginyl peptide bond of this polypeptide. The mast cell enzyme is far more effective than cathepsin G, the rates of hydrolysis being comparable to that found for angiotensin I to angiotensin II conversion (C.F. Reilly, D. Tewksbury, N. Schechter, and J. Travis, J. Biological Chemistry 257:8619-8622). This ability to both inactivate bradykinin and accelerate the production of angiotensin II may be of significance in the development of biochemical events associated with inflammation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Reilly CF,Schechter NB,Travis J

doi

10.1016/s0006-291x(85)80180-7

subject

Has Abstract

pub_date

1985-03-15 00:00:00

pages

443-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)80180-7

journal_volume

127

pub_type

杂志文章

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