| Autor: | Alicia Nuñez, Margarita Fernández-Renart |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Bisindolylmaleimide
biology medicine.diagnostic_test Kinase Proteolysis Clinical Biochemistry macromolecular substances Cell Biology General Medicine biology.organism_classification Dictyostelium discoideum Cell biology chemistry.chemical_compound Biochemistry chemistry medicine Staurosporine Phosphorylation Protein kinase A Molecular Biology Protein kinase C medicine.drug |
| Zdroj: | Molecular and Cellular Biochemistry. 175:177-185 |
| ISSN: | 0300-8177 |
| DOI: | 10.1023/a:1006809202539 |
| Popis: | In the search for MBP phosphorylating activities in Dictyostelium discoideum, we have found a proteolysis-activated protein kinase. This activity which is distributed between the soluble and the particulate fractions of the cell, uses MBP and histone as substrate and has a molecular mass of 140 kDa as detected in an ’in situ' assay. This protein kinase has several features shared by the protein kinase C family, such as substrate specificity and sensitivity to proteolysis, but its molecular mass is much larger than that described for the known protein kinase C isoforms. To better characterize this activity we have studied its sensitivity to several protein kinase C inhibitors and activators. This protein kinase is activated neither by phorbol ester nor by phosphatidylserine or Ca2+. The activity is inhibited by staurosporine and PKC ζ pseudosubstrate, but is not affected by the specific protein kinase C inhibitor bisindolylmaleimide. These data lead us to propose that proteolytically activated Dictyostelium protein kinase belongs to the recently described protein kinase C-related family. |
| Databáze: | OpenAIRE |
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