Cloning and expression of multiple protein kinase C cDNAs
Identifieur interne : 002A50 ( Istex/Corpus ); précédent : 002A49; suivant : 002A51Cloning and expression of multiple protein kinase C cDNAs
Auteurs : John L. Knopf ; Myung-Ho Lee ; Lisa A. Sultzman ; Ronald W. Kriz ; Carson R. Loomis ; Rodney M. Hewick ; Robert M. BellSource :
- Cell [ 0092-8674 ] ; 1986.
English descriptors
- Teeft :
- Amino, Amino acid sequence, Amino acid sequences, Biol, Brain cdna library, Brain protein kinase, Cdna, Cdna clones, Cells transfected, Chem, Clone, Coding region, Cysteine, Cysteine residues, Encode, Ester, Experimental procedures, Expression vector, Guessmer, Hannun, Homogenization buffer, Homology, Kinase, Mrna, Nishizuka, Northern blot analysis, Nucleotide, Oligonucleotide, Pdbu, Peptide, Phorbol, Phorbol ester binding, Phorbol esters, Phosphatidylserine, Phospholipid, Polypeptide, Protein, Protein kinase, Protein kinase activity, Protein kinases, Protein sequences, Receptor, Sequence analysis, Specific binding, Tissue distribution, Transfected, Tryptic, Tyrodes solution.
Abstract
Abstract: Three different protein kinase C related cDNA clones were isolated from a rat brain cDNA library and designated PKC-I, PKC-II, and PKC-III. These each encode very similar, but distinct, polypeptides that contain a region homologous with other protein kinases. COS cells transfected with either PKC-I or PKC-II specifically bind at least 5-fold more 3H-PDBu (phorbol ester) than control cells. An increase in Ca2+, phosphatidylserine, and diacylglycerol/phorbol-ester-dependent protein kinase activity is also observed in COS cells transfected with either PKC-I or PKC-II. The physiological implications of the discovery of three protein-kinase-C-related cDNAs are discussed.
Url:
DOI: 10.1016/0092-8674(86)90874-3
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: Three different protein kinase C related cDNA clones were isolated from a rat brain cDNA library and designated PKC-I, PKC-II, and PKC-III. These each encode very similar, but distinct, polypeptides that contain a region homologous with other protein kinases. COS cells transfected with either PKC-I or PKC-II specifically bind at least 5-fold more 3H-PDBu (phorbol ester) than control cells. An increase in Ca2+, phosphatidylserine, and diacylglycerol/phorbol-ester-dependent protein kinase activity is also observed in COS cells transfected with either PKC-I or PKC-II. The physiological implications of the discovery of three protein-kinase-C-related cDNAs are discussed.</div>
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<abstract xml:lang="en"><p>Abstract: Three different protein kinase C related cDNA clones were isolated from a rat brain cDNA library and designated PKC-I, PKC-II, and PKC-III. These each encode very similar, but distinct, polypeptides that contain a region homologous with other protein kinases. COS cells transfected with either PKC-I or PKC-II specifically bind at least 5-fold more 3H-PDBu (phorbol ester) than control cells. An increase in Ca2+, phosphatidylserine, and diacylglycerol/phorbol-ester-dependent protein kinase activity is also observed in COS cells transfected with either PKC-I or PKC-II. The physiological implications of the discovery of three protein-kinase-C-related cDNAs are discussed.</p>
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<ce:abstract-sec><ce:simple-para>Three different protein kinase C related cDNA clones were isolated from a rat brain cDNA library and designated PKC-I, PKC-II, and PKC-III. These each encode very similar, but distinct, polypeptides that contain a region homologous with other protein kinases. COS cells transfected with either PKC-I or PKC-II specifically bind at least 5-fold more <ce:sup loc="pre">3</ce:sup>
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, phosphatidylserine, and diacylglycerol/phorbol-ester-dependent protein kinase activity is also observed in COS cells transfected with either PKC-I or PKC-II. The physiological implications of the discovery of three protein-kinase-C-related cDNAs are discussed.</ce:simple-para>
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