Am J Physiol 1994 Dec 01;2676 Pt 1:C1717-22. doi: 10.1152/ajpcell.1994.267.6.C1717.

Protooncogene product, c-mos kinase, is involved in upregulating Na+/H+ antiporter in Xenopus oocytes.

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Progesterone-stimulated Xenopus laevis oocytes undergo an increase in their intracellular pH from 7.3 to 7.7 because of the activation of Na+/H+ antiporters in their plasma membrane. Activation of Na+/H+ exchangers (NHE) in other cell systems appears to be regulated by phosphorylation of the NHE protein. In the current study we demonstrated that cytoplasm taken from steroid-stimulated oocytes rapidly induced an increase in intracellular pH when microinjected into full-grown stage VI recipient oocytes. The protein within the cytoplasm that appears to be responsible for this activity is c-mos kinase. Microinjected pure mosxe kinase protein rapidly activated the Na+/H+ exchangers in full-grown recipient oocytes. Furthermore, injected mosxe protein rapidly activated the Na+/H+ exchangers in smaller progesterone-insensitive stage IV oocytes. Therefore, it appears that the protooncogene product, p39 c-mos kinase, which is normally synthesized in full-grown stage VI oocytes in response to progesterone stimulation, is involved in the upregulation of the Na+/H+ antiporters during oocyte meiotic maturation.

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Species referenced: Xenopus laevis
Genes referenced: mos slc9a1