XB-ART-6418
FEBS Lett
2002 Oct 09;5292-3:203-7. doi: 10.1016/s0014-5793(02)03340-9.
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Coexpression of a Ca(v)1.2 protein lacking an N-terminus and the first domain specifically suppresses L-type calcium channel activity.
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L-type Ca(2) channels play a critical role in many types of cells, including nerve, muscle and endocrine cells. The most popular and effective tools for analyzing the roles of L-type calcium channels (L-channels) are specific antagonists such as dihydropyrigines. With these drugs however, it is difficult to target specific cells. One solution is to develop a genetically targetable inhibitor coded by DNA. As a candidate for such an inhibitor, a dominant negative mutant of Ca(v)1.2 was designed by mimicking an ascidian 3-domain-type alpha1 subunit (that inhibits the full-length subunit's current). The 3-domain-type Ca(v)1.2 subunit significantly inhibited wild-type Ca(v)1.2 current, but not other ionic currents such as Ca(v)2.1 and Na(v) channels in Xenopus oocyte expression systems. Western blot analysis showed that the expression of the wild-type protein into the plasma membrane was significantly suppressed on coexpression with the truncated protein. These findings support that an N-terminus-truncated mutant could serve as a specific genetically encoded inhibitor for L-channels.
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Species referenced: Xenopus
Genes referenced: cacna1c