Evidence that (a) serine specific protein kinase(s) different from protein kinase C is responsible for the insulin‐stimulated actin phosphorylation by placental membrane

FEBS Letters

Wieland, O.H.¹  Carrascosa, J.M.¹ 

[1] Institut für Diabetesforschung, Krankenhaus München-Schwabing, Kölner Platz 1, 8000 München 40, FRG

关键词: Actin phosphorylation;    Protein kinase C;    Placental membrane;    Insulin action;   

DOI  :  10.1016/0014-5793(86)80574-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown