Insulin and progesterone activate a common synthetic ribosomal protein S6 peptide kinase in Xenopus oocytes

FEBS Letters

Cicirelli, Michael F.¹  Pelech, Steven L.¹  Krebs, Edwin G.¹ 

[1] The Howard Hughes Medical Institute, University of Washington, Mail Stop SL-15, Seattle, WA 98195, USA

关键词: S6 kinase;    Insulin;    Progesterone;    Oocyte maturation;   

DOI  :  10.1016/0014-5793(88)81060-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A synthetic peptide Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala, the structure of which is based on that of a phosphorylated sequence in ribosomal protein S6, was employed as a probe for stimulated kinase activity in Xenopus laevis oocytes induced to mature with insulin or progesterone. Insulin elicited an early (20–30 min) 3-fold stimulation of S6 peptide phosphorylating activity that was not evident with progesterone. However, both hormones produced a delayed 7–12-fold stimulation of S6 peptide phosphorylating activity at the time of germinal vesicle breakdown. The results of DEAE-Sephacel, Sephacryl S-200, TSK-400, and heparin-Sepharose chromatographic fractionation experiments imply that a common S6 peptide kinase is activated as a consequence of short and long term insulin exposure, as well as in long term progesterone treatment of oocytes. Omission of potassium from the oocyte culture medium greatly facilitated insulin-induced meiotic maturation.

【 授权许可】

Unknown