Abstract
On fertilization of a sea urchin egg, marked changes occur in the cytoplasmic concentration of calcium and hydrogen ions. These ionic signals represent the necessary and sufficient stimuli for the increased metabolism, protein synthesis and DNA synthesis that constitute egg activation1–3. Cytoplasmic alkalinization, the major immediate cause of the increased rate of protein synthesis which occurs at fertilization4, arises because the sperm-induced intracellular calcium transient activates a coupled flux of sodium ions and hydrogen ions across the oolemma5–7. The experiments reported here suggest that the second messenger which links the activation of the Na/H exchange to the calcium transient may be a substance which stimulates protein kinase C8, as 12-O-tetradecanoyl phorbol acetate (TPA), a known activator of protein kinase C9, appears to stimulate protein synthesis by turning on the Na/H exchanger and causing a cytoplasmic alkalinization. Our data indicate that one consequence of treating other tissues with TPA, a tumour promoter, may be an increase in intracellular pH10–12.
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Swann, K., Whitaker, M. Stimulation of the Na/H exchanger of sea urchin eggs by phorbol ester. Nature 314, 274–277 (1985). https://doi.org/10.1038/314274a0
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DOI: https://doi.org/10.1038/314274a0
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