Insulin increases membrane protein kinase C activity in rat diaphragm |
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Authors: | S I Walaas R S Horn A Adler K A Albert O Walaas |
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Affiliation: | 1. Institute of Medical Biochemistry, University of Oslo, PO Box 1112 Blindern, 0317 Oslo 3, Norway;2. Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021 USA;3. California Metabolic Research Foundation, La Jolla, CA 92038, USA |
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Abstract: | Calcium/phospholipid-dependent protein kinase activity (protein kinase C) was identified in rat diaphragm membrane and cytosol fractions by means of in vitro phosphorylation either of histones or of a specific 87 kDa protein substrate, combined with phosphopeptide-mapping techniques. Both insulin and tumor-promoting phorbol ester treatment of the diaphragm preparations led to increased protein kinase C activity in the membrane fractions. In contrast to the phorbol ester, however, insulin did not induce a concomitant decrease in cytosolic activity, indicating that translocation of the enzyme had not taken place. Thus, insulin appears to increase specifically membrane protein kinase C activity in rat skeletal muscle, possibly through a mechanism not identical to that induced by phorbol esters. |
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