Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity
العنوان: | Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity |
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المؤلفون: | Ingunn Holen, P. B. Gordon, Per Ottar Seglen |
المصدر: | Scopus-Elsevier |
سنة النشر: | 1992 |
مصطلحات موضوعية: | Male, Indoles, Calmodulin, Carbazoles, Vacuole, Biology, Tritium, Biochemistry, Piperazines, Indole Alkaloids, chemistry.chemical_compound, Alkaloids, Raffinose, Ethers, Cyclic, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, Okadaic Acid, Autophagy, Phosphoprotein Phosphatases, Animals, Protein Phosphatase Inhibitor, Cytoskeleton, Protein kinase A, Molecular Biology, Protein Kinase Inhibitors, Cells, Cultured, Calcium-Calmodulin-Dependent Protein Kinases, Sulfonamides, Rats, Inbred Strains, Cell Biology, Okadaic acid, Isoquinolines, Cell biology, Rats, Kinetics, chemistry, Liver, biology.protein, Protein Kinases, Research Article |
الوصف: | The protein phosphatase inhibitor okadaic acid suppressed autophagy completely in isolated rat hepatocytes, as measured by the sequestration of electroinjected [3H]raffinose into sedimentable autophagic vacuoles. Okadaic acid was effectively antagonized by the general protein kinase inhibitors K-252a and KT-5926, the calmodulin antagonist W-7, and by KN-62, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II (CaMK-II). These inhibitors also antagonized a cytoskeleton-disruptive effect of okadaic acid, manifested as the disintegration of cell corpses after breakage of the plasma membrane. CaMK-II, or a closely related enzyme, would thus seem to play a role in the control of autophagy as well as in the control of cytoskeletal organization. |
اللغة: | English |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c95b7cd7e732a5a45fba46dc1b8fbc6dTest https://europepmc.org/articles/PMC1132582Test/ |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....c95b7cd7e732a5a45fba46dc1b8fbc6d |
قاعدة البيانات: | OpenAIRE |
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