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Heterogeneous signaling pattern of PKC activity associated with the Ca v 1.2 calcium channel current
Author(s) -
Kobrinsky E,
Thomas S,
Masoudieh A,
Mager D A,
Abernethy D R,
Soldatov N M
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1155-c
Subject(s) - protein kinase c , microbiology and biotechnology , chemistry , biophysics , depolarization , phosphatase , voltage dependent calcium channel , protein tyrosine phosphatase , calcium signaling , signal transduction , calcium , t type calcium channel , patch clamp , phosphorylation , biochemistry , biology , receptor , organic chemistry
The role of L‐type Ca v 1.2 voltage gated calcium channels in regulation of protein kinase C (PKC) activity has been studied using FRET‐based reporter of PKC and phosphatase activity in COS1 and rat atrial cells under whole‐cell patch‐clamped conditions. The 2D continuous wavelet transform analysis was applied for detection of signaling microdomains in the plasma membrane. Periodic activation of the calcium current through calcium channels by depolarization pulses to +20 mV for few minutes resulted in appearance of plasma membrane transient microdomains of high phosphatase activity similar to the ones observed on PKC activation with phorbol (Kobrinsky et al., 2005). After prolong stimulation of calcium channels (10–15 minutes), FRET signal along the plasma membrane became more homogeneous and revealed microdomains of high PKC activity only. Results of our study show that Ca current through the native and recombinant Ca v 1.2 channels generates a heterogeneous signaling pattern of PKC activity along the plasma membrane.