The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.
Regulation of Cardiac L-Type Calcium Channels by Protein Kinase A and Protein Kinase C
Open accessAbstract
Abstract —Voltage-dependent L-type Ca 2+ channels are multisubunit transmembrane proteins, which allow the influx of Ca 2+ ( I Ca ) essential for normal excitability and excitation-contraction coupling in cardiac myocytes. A variety of different receptors and signaling pathways provide dynamic regulation of I Ca in the intact heart. The present review focuses on recent evidence describing the molecular details of regulation of L-type Ca 2+ channels by protein kinase A (PKA) and protein kinase C (PKC) pathways. Multiple G protein–coupled receptors act through cAMP/PKA pathways to regulate L-type channels. β-Adrenergic receptor stimulation results in a marked increase in I Ca , which is mediated by a cAMP/PKA pathway. Growing evidence points to an important role of localized signaling complexes involved in the PKA-mediated regulation of I Ca , including A-kinase anchor proteins and binding of phosphatase PP2a to the carboxyl terminus of the α 1C (Ca v 1.2) subunit. Both α 1C and β 2a subunits of the channel are substrates for PKA in vivo. The regulation of L-type Ca 2+ channels by Gq-linked receptors and associated PKC activation is complex, with both stimulation and inhibition of I Ca being observed. The amino terminus of the α 1C subunit is critically involved in PKC regulation. Crosstalk between PKA and PKC pathways occurs in the modulation of I Ca . Ultimately, precise regulation of I Ca is needed for normal cardiac function, and alterations in these regulatory pathways may prove important in heart disease.
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Calcium Signaling in Cardiac Myocytes
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Metadata
- Authors
- Kamp, T. J., & Hell, J. W.
- Venue
- Circulation Research
- Published
- 2000-12-08
- Volume
- 87
- Issue
- 12
- Pages
- 1095-1102
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2140205166
- Cited by
- 606
- References
- 91
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- bronze
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