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Phospholipase Cδ 1 does not mediate Ca 2+ responses in neonatal rat cardiomyocytes
Author(s) -
Woodcock Elizabeth A.,
Mitchell Christopher J.,
Biden Trevor J.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00608-2
Subject(s) - chemistry , phospholipase c , calcium , biophysics , medicine , microbiology and biotechnology , endocrinology , biochemistry , biology , enzyme , organic chemistry
Phospholipase C (PLC) activation in neonatal rat ventricular cardiomyocytes (NRVM) generates inositol(1,4,5)trisphosphate (Ins(1,4,5)P 3 ) in response to elevations in Ca 2+ or inositol(1,4)bisphosphate in response to G protein stimulation. Overexpression of PLCδ 1 increased total [ 3 H]inositol phosphate (InsP) content and elevated [ 3 H]Ins(1,4,5)P 3 , but failed to increase [ 3 H]InsP responses to the Ca 2+ ionophore A23187. Antisense PLCδ 1 expression reduced endogenous PLCδ 1 content but did not decrease the A23187 response. In permeabilized NRVM, [ 3 H]InsP responses to elevated Ca 2+ were not inhibited by Ins(1,4,5)P 3 , even at concentrations 1000‐fold greater than required for selective inhibition of PLCδ 1 . Taken together these data provide evidence that PLCδ 1 does not mediate the InsP response to elevated Ca 2+ in NRVM.