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Digitale Medien

Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human μCANP and mCANP (1993)

Saito, Ken-Ichi ; Nixon, Ralph A.

Springer

Neurochemical research 18 (1993), S. 231-233

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ISSN: 1573-6903

Schlagwort(e): Calcium-activated neutral proteinases ; calpains ; calpeptin ; leupeptin ; E64 ; human brain ; proteinase inhibitors

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: 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 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 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01474689

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