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Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human μCANP and mCANP.

Authors :
Saito, Ken-Ichi
Nixon, Ralph
Source :
Neurochemical Research; Feb1993, Vol. 18 Issue 2, p231-233, 3p
Publication Year :
1993

Abstract

We investigated the relative inhibition of purified human μCANP and mCANP by five cysteine proteinase inhibitors including N-acetyl-Leu-Leu-nor-leucinal (C-I) and N-acetyl-Leu-Leu-methioninal (C-II), calpeptin, E64, and leupeptin. Based on IC measurements, calpeptin and C-I were stronger inhibitors by one to two orders of magnitude than C-II, leupeptin or E64. None of the five inhibitors, however, exhibited greater specificity for human μCANP or mCANP. These results indicate that, although the inhibition of a given cellular event by these compounds may suggest CANP involvement, effects on μCANP cannot be discriminated from those on mCANP. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03643190
Volume :
18
Issue :
2
Database :
Complementary Index
Journal :
Neurochemical Research
Publication Type :
Academic Journal
Accession number :
70612497
Full Text :
https://doi.org/10.1007/BF01474689