Differential inhibition by staurosporine of phorbol ester, bryostatin and okadaic acid effects on mouse skin
| Autor: | Friedrich Marks, Michael Gschwendt, Dieter Lindner, Walter Kittstein |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Cancer Research
medicine.medical_specialty Pharmacology 12-O-Tetradecanoylphorbol-13-acetate Lactones Mice chemistry.chemical_compound Alkaloids Ethers Cyclic Internal medicine Edema Cyclosporin a Okadaic Acid medicine Animals Staurosporine Bryostatin Protein Kinase C Protein kinase C Skin integumentary system Activator (genetics) Chemistry Okadaic acid Bryostatins Endocrinology Oncology Cyclosporine Tetradecanoylphorbol Acetate Female Macrolides medicine.symptom medicine.drug |
| Zdroj: | Cancer Letters. 66:139-146 |
| ISSN: | 0304-3835 |
| DOI: | 10.1016/0304-3835(92)90226-l |
| Popis: | The tumor promoters 12-O-tetradecanoylphorbol-13-acetate (TPA), a strong activator of protein kinase C (PKC) and okadaic acid, which is ineffective in this respect, induce a rapidly developing (‘early’) edema of the mouse ear. Bryostatin, another potent activator of PKC, is unable to induce an ‘early’ edema but causes a more delayed development of edema at a time when most of the PKC is down-regulated. The PKC inhibitor staurosporine neither inhibits the early TPA-nor the late bryostatin-induced edema, but suppresses the okadaic acid-induced edema very effectively. TPA as well as bryostatin, but not okadaic acid cause a down-regulation of PKC, which is not inhibited by staurosporine. The calmodulin antagonist cyclosporine A, which does not suppress PKC activity, very effectively inhibits the TPA-induced edema and down regulation of PKC. Hence we conclude that protein phosphorylation catalyzed by staurosporine-suppressable PKC is not involved in the induction of edema and PKC down-regulation by TPA but that a calmodulin dependent process may play a critical role in these and other TPA effects in mouse skin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|