PROTEIN-KINASES IN HUMAN RENAL CELL-CARCINOMA AND RENAL CORTEX - COMPARISON OF ISOENZYME DISTRIBUTION AND OF RESPONSIVENESS TO ADENOSINE 3'-5'-CYCLIC MONOPHOSPHATE

被引：53

作者：

FOSSBERG, TM ^{[1
]}

DOSKELAND, SO ^{[1
]}

UELAND, PM ^{[1
]}

机构：

[1] UNIV BERGEN,INST PRECLIN,CELL BIOL RES GRP,N-5000 BERGEN,NORWAY

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1978年 / 189卷 / 02期

关键词：

D O I：

10.1016/0003-9861(78)90224-2

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：

Two major isozyme forms of cyclic AMP-dependent protein kinase (termed protein kinase I and II according to their order of elution from DEAE-cellulose) were resolved by DEAE-cellulose chromatography of extracts from human renal cortex and renal cell carcinoma. The ratio between protein kinase I and protein kinase II in carcinoma extracts was about twice that in extracts of renal cortex. The total soluble cyclic AMP-dependent protein kinase activity was similar in extracts from the normal and malignant tissue. Protein kinase isozymes prepared from renal cortex or carcinoma were highly dependent on cyclic AMP for activity under appropriate assay conditions, were activated to the same degree by various concentrations of cyclic AMP, and had similar affinity for the nucleotide, indicating that the mechanism for regulation of protein kinase activity by cyclic AMP was intact for the tumor kinases. The kinetics of endogenous phosphorylation of protein kinase II was similar for enzyme derived from normal or malignant tissue. © 1978.

引用

页码：372 / 381

页数：10

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