PROTEOLYTIC ACTIVATION OF PROTEIN KINASE-C-EPSILON

被引：61

作者：

SCHAAP, D ^{[1
]}

HSUAN, J ^{[1
]}

TOTTY, N ^{[1
]}

PARKER, PJ ^{[1
]}

机构：

[1] LUDWIG INST CANC RES,91 RIDING HOUSE ST,LONDON W1P 8BT,ENGLAND

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 191卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19139.x

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：

Proteolysis of native protein kinase C‐ɛ (PKC‐ɛ) is shown to occur through tryptic attack at multiple sites within the PKC‐ɛ V2/V3 domain. Following initial cleavage of PKC‐ɛ with trypsin, the kinase activity using a synthetic peptide substrate was found to be lipid/phorbol‐ester independent, as observed for other members of this kinase family. Interestingly, there is also an increase in the histone kinase activity, indicating that there is an influence of the regulatory domain of the enzyme on substrate specificity. This is discussed in the context of alternatively spliced PKC‐ɛ mRNAs that are shown to be present in brain and lung tissues. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：431 / 435

页数：5

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