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Properties and nature of a cysteine proteinase inhibitor located in keratohyalin granules of rat epidermis.

作者信息

Takahashi M, Tezuka T, Towatari T, Katunuma N

机构信息

Department of Dermatology, Kinki University School of Medicine, Osaka, Japan.

出版信息

FEBS Lett. 1990 Jul 16;267(2):261-4. doi: 10.1016/0014-5793(90)80940-k.

DOI:10.1016/0014-5793(90)80940-k
PMID:2199217
Abstract

The pI 4.7, 14.5 kDa hematoxylin-stainable protein (HSP) from rat epidermis inhibited the activities of the cysteine proteinases papain, ficin, cathepsins B, H and L with similar inhibitory characteristics as recombinant cystatin-alpha. Proteinases of other classes were not inhibited. The inhibitory activity of HSP was heat stable in the wide pH range of 3.0-10.0. Polyclonal antibodies against HSP cross-reacted with cystatin-alpha and the molecular mass of HSP was similar to that of cystatin-alpha, though its isoelectric point was different. The in vivo location of both HSP and cystatin-alpha is on keratohyalin granules in epidermis as detected by indirect immunofluorescence technique using individual antibodies. Therefore it is highly probable that HSP is a cystatin-alpha derivative or a very similar proteinase inhibitor belonging to a family of cystatins.

摘要

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