The role of protein kinases in ACTH-stimulated steroidogenesis. |
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Authors: | K Hofmann J J Kim F M Finn |
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Institution: | Protein Research Laboratory University of Pittsburgh School of Medicine Pittsburgh, Pennsylvania 15261 USA |
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Abstract: | The effect of highly purified bovine cytosolic adrenal cortical protein kinase isozyme II catalytic subunit (ATP: Protein Phosphotransferase EC 2.7.1.37) on the formation of pregnenolone from cholesterol in rat and bovine adrenal mitochondrial extracts has been investigated. No stimulation was observed although a low level incorporation of 32P] from 32P]-ATP into a component or components of the extract was detected. The mitochondrial extracts contained alkaline phosphatase activity that was inhibited by L-cysteine and dithiothreitol. It is concluded that the acute stimulation by ACTH of corticoid production in the rat adrenal does not involve protein kinase mediated phosphorylation of a component or components of the cholesterol sidechain cleavage mixed-function oxygenase system. |
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Keywords: | ACTH adrenocorticotropic hormone BSA bovine serum albumin DTT DL-dithiothreitol TCA trichloroacetic acid U unit(s) |
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