Regulation of Cav3.2 Ca<SUP>2+</SUP> channel activity by protein tyrosine phosphorylation

초록

Calcium entry through Ca(v)3.2 Ca2+ channels plays essential roles for various physiological events including thalamic oscillation, muscle contraction, hormone secretion, and sperm acrosomal reaction. In this study, we examined how protein tyrosine phosphatases or protein tyrosine kinases affect Ca(v)3.2 Ca2+ channels reconstituted in Xenopus oocytes. We found that Ca(v)3.2 channel activity was reduced by 25% in response to phenylarsine oxide (tyrosine phosphatase inhibitor), whereas it was augmented by 19% in response to Tyr A47 or herbimycin A (tyrosine kinase inhibitors). However, other biophysical properties of Cav3.2 currents were not significantly changed by the drugs. These results imply that Ca(v)3.2 channel activity is capable of being increased by activation of tyrosine phosphatases, but is decreased by activation of tyrosine kinases.

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