Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human mu CANP and mCANP.
We investigated the relative inhibition of purified human mu CANP 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 IC50 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 mu CANP or mCANP. These results indicate that, although the inhibition of a given cellular event by these compounds may suggest CANP involvement, effects on mu CANP cannot be discriminated from those on mCANP.
Saito
K
K
Laboratories for Molecular Neuroscience, Mailman Research Center, McLean Hospital, Belmont, MA 02178.
Nixon
R A
RA
D000595:Amino Acid Sequence; D002154:Calpain / Q000037:antagonists & inhibitors*; D006801:Humans; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology*
D011480:Protease Inhibitors; D002154:Calpain