Protein Kinase C Located in Rat Liver Nuclei
نویسندگان
چکیده
منابع مشابه
Presence of multiple protein kinase activities in rat liver nuclei.
The phosphorylation of nuclear proteins has been suggested to play a role in the control of gene readout in mammalian tissues (1,2,3). Phosphorylation of histones has been shown to occur in rat liver in response to hormonal agents (4), and a histone phosphokinase has been isolated from calf liver (5). I.n addition, many of the non-histone (acidic) proteins of the nucleus are phosphoproteins. Th...
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Selective substrates and inhibitors have been used to measure kinases phosphorylating endogenous proteins in rat liver nuclei during growth and regeneration after partial hepatectomy. Peaks in activity were found at 5, 22, and 29 hours after partial hepatectomy. Administration of alpha 1 and beta adrenergic blockers suggested that the Be2+ sensitive and cyclic AMP-dependent protein kinases were...
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Protein kinase C mu (PKC mu) displays unusual structural features like a pleckstrin homology domain and an amino-terminal hydrophobic region with a putative leader peptide and transmembrane sequence. As a discrete location often is a direct clue to the potential biological function of a kinase, antibodies directed against unique amino- and carboxy-terminal domains of PKC mu were used to localiz...
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A cardiolipin- and protease-activated protein kinase (PAK) has been isolated from cytoplasmic extracts of rat liver. The enzyme (PAK-1) phosphorylates the ribosomal protein S6-(229-239) peptide analogue and can be activated by limited proteolysis. Partial amino acid sequences of tryptic peptides derived from both the purified 116-kDa PAK-1 holoenzyme and its active catalytic fragment reveal tha...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85068-8