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Cross‐modulation of glycine‐activated Cl − channels by protein kinase C and cAMP‐dependent protein kinase in the rat
Author(s) -
Gu Yanping,
Huang L.Y. M.
Publication year - 1998
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1111/j.1469-7793.1998.331bw.x
Subject(s) - protein kinase c , protein kinase a , microbiology and biotechnology , patch clamp , chemistry , glycine , kinase , endogeny , biophysics , biology , biochemistry , receptor , amino acid
1 The cross‐modulation of glycine responses by cyclic‐AMP‐dependent protein kinase (PKA) and protein kinase C (PKC) was determined in acutely dissociated trigeminal neurons. 2 Whole‐cell glycine‐evoked Cl − current ( I Gly ) was recorded using the patch clamp technique. Protein kinases and their inhibitors were intracellularly perfused into the cells. 3 Both PKA and PKC when applied separately potentiated I Gly . 4 When PKA and PKC were sequentially applied, PKC could not increase the I Gly any further after the glycine responses were enhanced by PKA. 5 In 42 % of our cells, I Gly increased spontaneously. Endogenous PKA was found to mediate the increase. PKC had no effects on I Gly in these cells. 6 The effect of PKA on I Gly was studied in PKC‐pretreated cells. PKA failed to potentiate I Gly in these cells, suggesting that the PKA action also depends on the activity of PKC inside the cells. 7 These results suggest that the PKC action on I Gly is conditional upon the modulation of the currents by PKA and vice versa. This cross‐regulation of ligand‐gated channel activity by protein kinases may play a role in neuronal integration and synaptic plasticity.