KP-10, a novel protein kinase C substrate in intact mouse epidermal cells, is phosphorylated by novel protein kinase C eta and/or zeta
| Autor: | Norie Murayama, Kiyotaka Nishikawa, Motoko Ishihara, Haruna Nagumo, Satoshi Yamamoto, Ryuichi Kato |
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| Rok vydání: | 1994 |
| Předmět: |
Immunoprecipitation
Blotting Western Molecular Sequence Data Phosphatidylserines Biology PKC alpha Substrate Specificity chemistry.chemical_compound Mice Western blot medicine Animals Amino Acid Sequence Phosphorylation Protein kinase C Cells Cultured Protein Kinase C Skin medicine.diagnostic_test Kinase Cell Biology Phosphoproteins Molecular biology Cell biology Isoenzymes chemistry Phorbol Tetradecanoylphorbol Acetate Intracellular Signal Transduction |
| Zdroj: | Cellular signalling. 6(5) |
| ISSN: | 0898-6568 |
| Popis: | Recently this group found an endogenous substrate protein for Ca(2+)-independent novel protein kinase C (nPKC), i.e. KP-10 (pI 4.7/25,500 M(r)), in primary cultured mouse epidermal cells [Nishikawa, K. et al. (1992) Cell. Signal. 4, 757-776]. In the present study, the nPKC isozymes which phosphorylate KP-10 in these cells were determined. Western blot analysis revealed that PKC alpha, eta and zeta were present in epidermal cell 105,000 g supernatants and that the content of PKC zeta was much higher than those of PKC alpha and eta. Neither PKC beta, delta nor epsilon was detected in the 105,000 g supernatants. Phosphatidylserine and phorbol 12-myristate 13-acetate (PMA)-dependent KP-10 phosphorylating activity was immunoprecipitated by anti-PKC eta and zeta antibodies, but not by antiPKC alpha antibody. These results suggest that PKC eta and/or zeta phosphorylate KP-10 and play pivotal roles in intracellular signal pathways in intact epidermal cells. |
| Databáze: | OpenAIRE |
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