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3 results on '"Phospholipase Cδ1"'

1. Phospholipase Cδ1 does not mediate Ca2+ responses in neonatal rat cardiomyocytes

Author

Woodcock, Elizabeth A., Mitchell, Christopher J., and Biden, Trevor J.

Subjects
*PHOSPHOLIPASE C, *ADENOVIRUSES
Abstract

Phospholipase C (PLC) activation in neonatal rat ventricular cardiomyocytes (NRVM) generates inositol(1,4,5)trisphosphate (Ins(1,4,5)P3) in response to elevations in Ca2+ or inositol(1,4)bisphosphate in response to G protein stimulation. Overexpression of PLCδ1 increased total [3H]inositol phosphate (InsP) content and elevated [3H]Ins(1,4,5)P3, but failed to increase [3H]InsP responses to the Ca2+ ionophore A23187. Antisense PLCδ1 expression reduced endogenous PLCδ1 content but did not decrease the A23187 response. In permeabilized NRVM, [3H]InsP responses to elevated Ca2+ were not inhibited by Ins(1,4,5)P3, even at concentrations 1000-fold greater than required for selective inhibition of PLCδ1. Taken together these data provide evidence that PLCδ1 does not mediate the InsP response to elevated Ca2+ in NRVM. [Copyright &y& Elsevier]

Published
2003
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2. Phospholipase Cdelta(1) does not mediate Ca(2+) responses in neonatal rat cardiomyocytes

Author

Elizabeth A. Woodcock, Chris J. Mitchell, and Trevor J. Biden

Subjects
medicine.medical_specialty, G protein, Biophysics, Stimulation, Endogeny, Cardiomyocyte, Inositol 1,4,5-Trisphosphate, Phospholipase, Biology, Biochemistry, Rats, Sprague-Dawley, chemistry.chemical_compound, Phospholipase C delta, Structural Biology, Internal medicine, Genetics, medicine, Adenovirus, Animals, Inositol, Inositol phosphate, Molecular Biology, Cells, Cultured, chemistry.chemical_classification, Phospholipase C, Myocardium, Cell Biology, Phospholipase Cδ1, Rats, Isoenzymes, Endocrinology, chemistry, Animals, Newborn, Type C Phospholipases, Calcium
Abstract

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 PLCdelta(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 PLCdelta(1) expression reduced endogenous PLCdelta(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 PLCdelta(1). Taken together these data provide evidence that PLCdelta(1) does not mediate the InsP response to elevated Ca(2+) in NRVM.

Published
2003

3. Regulation of phospholipase C-delta by GTP-binding proteins-rhoA as an inhibitory modulator

Author

Joanne S Lymn, Christopher C. Ashley, Alun D. Hughes, and Elizabeth A.M. Hodson

Subjects
RHOA, Botulinum Toxins, G protein, Antidotes, GTPgammaS, Guanosine, GTP-binding protein, Chemical Fractionation, Deferoxamine, Sulfur Radioisotopes, GTP Phosphohydrolases, chemistry.chemical_compound, Phospholipase C delta, GTP-binding protein regulators, Adenosine Triphosphate, GTP-Binding Proteins, Animals, Molecular Biology, Exoenzyme C3, ADP Ribose Transferases, Adenosine Diphosphate Ribose, Phospholipase C, biology, Guanosine 5'-O-(3-Thiotriphosphate), RhoA, Cell Biology, Molecular biology, Phospholipase Cδ1, Enzyme Activation, Isoenzymes, chemistry, Biochemistry, Type C Phospholipases, biology.protein, Sodium Fluoride, Cattle, rhoA GTP-Binding Protein
Abstract

The regulation of Phospholipase C (PLC)delta activity remains obscure. These studies show that PLCdelta1 activity is significantly enhanced by both guanosine thiotriphosphate (GTPgammaS) and Clostridium botulinum exoenzyme C3 (C3) but not by aluminium fluoride. C3 ADP ribosylated a 21-kDa protein in the PLCdelta1 preparation and Western blotting identified rhoA in these samples. RhoA acts as an inhibitory modulator of PLCdelta activity.

Published
1998

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