DOI: 10.1152/ajpheart.1997.273.4.h1775. Modulation of Kv4 channels, key components of rat ventricular transient outward K<sup>+</sup> current, by PKC

Modulation of Kv4 channels, key components of rat ventricular transient outward K+ current, by PKC

10.1152/ajpheart.1997.273.4.h1775

Crossref journal-article

American Physiological Society

American Journal of Physiology-Heart and Circulatory Physiology (24)

Abstract

Current evidence suggests that members of the Kv4 subfamily may encode native cardiac transient outward current ( I to). Antisense hybrid-arrest with oligonucleotides targeted to Kv4 mRNAs specifically inhibited rat ventricular I to, supporting this hypothesis. To determine whether protein kinase C (PKC) affects I to by an action on these molecular components, we compared the effects of PKC activation on Kv4.2 and Kv4.3 currents expressed in Xenopus oocytes and rat ventricular I to. Phorbol 12-myristate 13-acetate (PMA) suppressed both Kv4.2 and Kv4.3 currents as well as native I to, but not after preincubation with PKC inhibitors (e.g., chelerythrine). An inactive stereoisomer of PMA had no effect. Phenylephrine or carbachol inhibited Kv4 currents only when coexpressed, respectively, with α1C-adrenergic or M1 muscarinic receptors (this inhibition was also prevented by chelerythrine). The voltage dependence and inactivation kinetics of Kv4.2 were unchanged by PKC, but small effects on the rates of inactivation and recovery from inactivation of native I to were observed. Thus Kv4.2 and Kv4.3 proteins are important subunits of native rat ventricular I to, and PKC appears to reduce this current by affecting the molecular components of the channels mediating I to.

Bibliography

Nakamura, T. Y., Coetzee, W. A., Vega-Saenz De Miera, E., Artman, M., & Rudy, B. (1997). Modulation of Kv4 channels, key components of rat ventricular transient outward K+ current, by PKC. American Journal of Physiology-Heart and Circulatory Physiology, 273(4), H1775âH1786.

Authors 5

Tomoe Y. Nakamura (first)
William A. Coetzee (additional)
Eleazar Vega-Saenz De Miera (additional)
Michael Artman (additional)
Bernardo Rudy (additional)

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Dates

Type	When
Created	7 years, 8 months ago (Dec. 21, 2017, 5:55 p.m.)
Deposited	5 years, 11 months ago (Sept. 8, 2019, 12:22 p.m.)
Indexed	1 year, 2 months ago (June 17, 2024, 3:58 p.m.)
Issued	27 years, 11 months ago (Oct. 1, 1997)
Published	27 years, 11 months ago (Oct. 1, 1997)
Published Print	27 years, 11 months ago (Oct. 1, 1997)

Funders 0

None

BibTeX

@article{Nakamura_1997, title={Modulation of Kv4 channels, key components of rat ventricular transient outward K+ current, by PKC}, volume={273}, ISSN={1522-1539}, url={http://dx.doi.org/10.1152/ajpheart.1997.273.4.h1775}, DOI={10.1152/ajpheart.1997.273.4.h1775}, number={4}, journal={American Journal of Physiology-Heart and Circulatory Physiology}, publisher={American Physiological Society}, author={Nakamura, Tomoe Y. and Coetzee, William A. and Vega-Saenz De Miera, Eleazar and Artman, Michael and Rudy, Bernardo}, year={1997}, month=oct, pages={H1775–H1786} }

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  "abstract": "<jats:p> Current evidence suggests that members of the Kv4 subfamily may encode native cardiac transient outward current ( I <jats:sub>to</jats:sub>). Antisense hybrid-arrest with oligonucleotides targeted to Kv4 mRNAs specifically inhibited rat ventricular I <jats:sub>to</jats:sub>, supporting this hypothesis. To determine whether protein kinase C (PKC) affects I <jats:sub>to</jats:sub> by an action on these molecular components, we compared the effects of PKC activation on Kv4.2 and Kv4.3 currents expressed in Xenopus oocytes and rat ventricular I <jats:sub>to</jats:sub>. Phorbol 12-myristate 13-acetate (PMA) suppressed both Kv4.2 and Kv4.3 currents as well as native I <jats:sub>to</jats:sub>, but not after preincubation with PKC inhibitors (e.g., chelerythrine). An inactive stereoisomer of PMA had no effect. Phenylephrine or carbachol inhibited Kv4 currents only when coexpressed, respectively, with \u03b1<jats:sub>1C</jats:sub>-adrenergic or M<jats:sub>1</jats:sub> muscarinic receptors (this inhibition was also prevented by chelerythrine). The voltage dependence and inactivation kinetics of Kv4.2 were unchanged by PKC, but small effects on the rates of inactivation and recovery from inactivation of native I <jats:sub>to</jats:sub> were observed. Thus Kv4.2 and Kv4.3 proteins are important subunits of native rat ventricular I <jats:sub>to</jats:sub>, and PKC appears to reduce this current by affecting the molecular components of the channels mediating I <jats:sub>to</jats:sub>. </jats:p>",
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