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Regulation of $Ca_v3.2Ca^{2+}$ Channel Activity by Protein Tyrosine Phosphorylation  

Huh, Sung-Un (Department of Life Science, Sogang University)
Kang, Ho-Won (Department of Life Science, Sogang University)
Park, Jin-Yong (Department of Life Science, Sogang University)
Lee, Jung-Ha (Department of Life Science, Sogang University)
Publication Information
Journal of Microbiology and Biotechnology / v.18, no.2, 2008 , pp. 365-368 More about this Journal
Abstract
Calcium entry through $Ca_v3.2Ca^{2+}$ 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 $Ca_v3.2Ca^{2+}$ channels reconstituted in Xenopus oocytes. We found that $Ca_v3.2$ 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 $Ca_v3.2$ currents were not significantly changed by the drugs. These results imply that $Ca_v3.2$ channel activity is capable of being increased by activation of tyrosine phosphatases, but is decreased by activation of tyrosine kinases.
Keywords
$Ca_v3.2$; Xenopus oocyte; protein tyrosine kinase inhibitor; protein tyrosine phosphatase inhibitor; voltage clamping;
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