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Protein kinase C-mediated calcium signaling as the basis for cardiomyocyte plasticity
- Source :
- Archives of biochemistry and biophysics. 701
- Publication Year :
- 2020
-
Abstract
- Protein kinase C is the superfamily of intracellular effector molecules which control crucial cellular functions. Here, we for the first time did the percentage estimation of all known PKC and PKC-related isozymes at the individual cadiomyocyte level. Broad spectrum of PKC transcripts is expressed in the left ventricular myocytes. In addition to the well-known ‘heart-specific’ PKCα, cardiomyocytes have the high expression levels of PKCN1, PKCδ, PKCD2, PKCe. In general, we detected all PKC isoforms excluding PKCη. In cardiomyocytes PKC activity tonically regulates voltage-gated Ca2+-currents, intracellular Ca2+ level and nitric oxide (NO) production. Imidazoline receptor of the first type (I1R)-mediated induction of the PKC activity positively modulates Ca2+ release through ryanodine receptor (RyR), increasing the Ca2+ leakage in the cytosol. In cardiomyocytes with the Ca2+-overloaded regions of > 9–10 μm size, the local PKC-induced Ca2+ signaling is transformed to global accompanied by spontaneous Ca2+ waves propagation across the entire cell perimeter. Such switching of Ca2+ signaling in cardiac cells can be important for the development of several cardiovascular pathologies and/or myocardial plasticity at the cardiomyocyte level.
- Subjects :
- 0301 basic medicine
Male
SERCA
Biophysics
Imidazoline receptor
Biochemistry
03 medical and health sciences
Animals
Myocytes, Cardiac
Calcium Signaling
Rats, Wistar
Molecular Biology
Protein kinase C
Protein Kinase C
Calcium signaling
030102 biochemistry & molecular biology
Ryanodine receptor
Chemistry
Effector
Ryanodine Receptor Calcium Release Channel
Cell biology
Rats
Isoenzymes
Cytosol
030104 developmental biology
Intracellular
Subjects
Details
- ISSN :
- 10960384
- Volume :
- 701
- Database :
- OpenAIRE
- Journal :
- Archives of biochemistry and biophysics
- Accession number :
- edsair.doi.dedup.....8afcb507a45e177b0283143b0f8e6f40