Phosphatidate-dependent protein phosphorylation
| Autor: | John H. Exton, Stephen B. Bocckino, Pamela B. Wilson |
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| Rok vydání: | 1991 |
| Předmět: |
Male
inorganic chemicals Phosphatidic Acids macromolecular substances Biology environment and public health Phosphatidate chemistry.chemical_compound Adenosine Triphosphate Cytosol Testis Animals Protein phosphorylation Phosphorylation Protein kinase A Lung Protein kinase C Multidisciplinary Kinase Myocardium Brain Proteins Rats Inbred Strains Phosphoproteins Molecular biology Rats Molecular Weight Kinetics enzymes and coenzymes (carbohydrates) Liver chemistry Biochemistry Organ Specificity bacteria Electrophoresis Polyacrylamide Gel Adenosine triphosphate Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 88:6210-6213 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.88.14.6210 |
| Popis: | Phosphatidate-dependent protein phosphorylation was observed in soluble extracts from rat liver, brain, lung, and testis. The phosphorylation was stimulated by free Ca2+ in the range of 360-800 nM. Incubation mixtures containing phosphatidate provided markedly different profiles of protein phosphorylation from those with phosphatidylserine plus 1,2-diolein. Phosphatidate-dependent phosphorylation of a 30-kDa protein in the soluble fraction from heart was also observed. This phosphorylation did not require Ca2+. Soluble fractions from liver, testis, brain, and lung phosphorylated the 30-kDa heart protein in a phosphatidate-dependent Ca(2+)-independent manner. We propose that part of the action of phosphatidate in cells may be mediated by a protein kinase(s). |
| Databáze: | OpenAIRE |
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