PROPERTIES AND NATURE OF A CYSTEINE PROTEINASE-INHIBITOR LOCATED IN KERATOHYALIN GRANULES OF RAT EPIDERMIS

被引：16

作者：

TAKAHASHI, M ^{[1
]}

TEZUKA, T ^{[1
]}

TOWATARI, T ^{[1
]}

KATUNUMA, N ^{[1
]}

机构：

[1] UNIV TOKUSHIMA,INST ENZYME RES,DIV ENZYME CHEM,TOKUSHIMA 770,JAPAN

来源：

FEBS LETTERS | 1990年 / 267卷 / 02期

关键词：

Cystatin-α; Cysteine proteinase inhibitor; Hematoxylin stainable protein; Keratohyalin granule;

D O I：

10.1016/0014-5793(90)80940-K

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The pI4.7, 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-α. 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-α and the molecular mass of HSP was similar to that of cystatin-α, though its isoelectric point was different. The in vivo location of both HSP and cystatin-α 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-α derivative or a very similar proteinase inhibitor belonging to a family of cystatins. © 1990.

引用

页码：261 / 264

页数：4

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