| Autor: |
Cicirelli, Michael F., Pelech, Steven L., Krebs, Edwin G. |
| Zdroj: |
FEBS Letters; January 1988, Vol. 241 Issue: 1 p195-201, 7p |
| Abstrakt: |
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 laevisoocytes 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. |
| Databáze: |
Supplemental Index |
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