FEBS Lett 1988 Dec 05;2411-2:195-201.

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

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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.

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Species referenced: Xenopus laevis
Genes referenced: ins