J Biochem Mol Biol Biophys 2002 Apr 01;62:107-11. doi: 10.1080/10258140290027234.

Disappearance of M(r) 25,000 protein, a new protein kinase substrate, in parallel with a kind of serpin during embryogenesis.

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M(r) 25,000 protein (pp25) is a protein kinase substrate detected recently in Xenopus laevis oocytes [Hashimoto, E. et al. (1995) J. Biochem. 118, 453-460], but the physiological role of this protein remains to be determined. In order to elucidate some characteristics of pp25, a polyclonal antibody was raised against it and the distribution and quantitative changes of this protein were examined using various tissues and biological systems. In Western blot analysis, pp25 was detected only in Xenopus oocytes and not in other frog tissues when the heat-stable cytosolic fraction from each tissue was examined. Although the amount of pp25 apparently did not change during oocyte maturation induced by progesterone, pp25 disappeared in embryos around Nieuwkoop/Faber stages 45-48 in parallel with the change of pNiXa (a kind of serpin). These results suggest that pp25 plays some specific role(s) in Xenopus oocytes and that the level of pp25 changes dramatically during embryonic development.

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Species referenced: Xenopus laevis
Genes referenced: serpina6 tbx2