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.
Research Article|June 15 1992
Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity
P B Gordon;
Biochem J (1992) 284 (3): 633-636.
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I Holen, P B Gordon, P O Seglen; Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity. Biochem J 15 June 1992; 284 (3): 633–636. doi: https://doi.org/10.1042/bj2840633
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