Evidence that (a) serine specific protein kinase(s) different from protein kinase C is responsible for the insulin‐stimulated actin phosphorylation by placental membrane
- 26 May 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 201 (1) , 81-86
- https://doi.org/10.1016/0014-5793(86)80574-9
Abstract
Partially purified phospholipid- and Ca2+-dependent protein kinase C from human placenta catalyzes the Mg-ATP-dependent phosphorylation of serine residues of purified rabbit muscle actin. Two tryptic [32P]-phosphopeptides were found on HPLC separation. Confirming the previous report by Machicao and Wieland [(1985) Curr. Top. Cell. Regul. 27, 95-105], actin is phosphorylated at serine residues by human placental membranes, and this is stimulated by insulin. In the absence of insulin trypsin treatment yielded eight [32P]phosphopeptides, two of which coincided with the ones due to protein kinase C. Insulin led to the appearance of three new [32P]phosphopeptides. These results suggest that insulin stimulates (a) serine protein kinase(s) which, like protein kinase C, is present in placental membranes.Keywords
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