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1. Endothelin-1 stimulated phospholipase D in A10 vascular smooth muscle derived cells is dependent on tyrosine kinase. Evidence for involvement in stimulation of mitogenesis

Author

Lesley C. Wilkes, Viral Patel, Michael R. Boarder, and John R. Purkiss

Subjects
medicine.medical_specialty, Vascular smooth muscle, Biophysics, Biology, Tritium, Biochemistry, Endothelin, Muscle, Smooth, Vascular, 03 medical and health sciences, 0302 clinical medicine, Structural Biology, Internal medicine, Mitogenesis, Genetics, medicine, Phospholipase D, Animals, Molecular Biology, Tyrosine kinase, Protein kinase C, Cells, Cultured, Protein Kinase C, 030304 developmental biology, 0303 health sciences, Phospholipase C, PLD2, Endothelins, Cell Biology, Protein-Tyrosine Kinases, FLT4, Endothelin 1, Cell biology, Rats, Endocrinology, Smooth muscle cell, 030217 neurology & neurosurgery, Cell Division, Thymidine
Abstract

The mechanism whereby endothelin stimulates motogenesis of vascular smooth muscle cells is not understood. Here we show that endothelin-1 stimulates phospholipase D by a protein kinase C and tyrosine kinase dependent mechanism, and present evidence that implicate the phosphatidic acid formed by phospholipase D in the mitogenic response.

Published
1993

2. Phospholipase D activation regulates endothelin-1 stimulation of phosphoinositide-specific phospholipase C in SK-N-MC cells

Author

R. A. John Challiss, Viral Patel, Lesley C. Wilkes, John R. Purkiss, and Michael R. Boarder

Subjects
Indoles, Butanols, Inositol Phosphates, Biophysics, SK-N-MC cell, Stimulation, Biology, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Structural Biology, Protein kinase C, Phospholipase C, Inositol 1,4,5-trisphosphate, Genetics, Tumor Cells, Cultured, Phospholipase D, Humans, Inositol, Inositol phosphate, Molecular Biology, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Endothelin-1, Endothelins, Cell Biology, Molecular biology, Endothelin 1, Enzyme Activation, chemistry, Cell culture, Type C Phospholipases, Tetradecanoylphorbol Acetate, lipids (amino acids, peptides, and proteins), 030217 neurology & neurosurgery
Abstract

Endothelin-1 (ET-1) is known to stimulate phospholipase C (PLC) activity in SK-N-MC human neuroblastoma/epithelioma cells: here we show that phospholipase D(PLD) is also stimulated. The generation of inositol 1,4,5-trisphosphate (Ins(1,4,5)P 3 ) by ET-1-stimulated PLC was attenuated by protein kinase C (PKC) activation and enhanced by PKC inhibition. An enhancement of ET-1-stimulated Ins(1,4,5)P 3 accumulation was also seen when the product of PLD activity was either diverted into phosphatidyl butanol in the presence of butanol, or phosphatidate phosphohydrolase (PPH) activity was inhibited by dl -propranolol. We conclude that there is an inhibitory, PKC-mediated, feedback loop in these cells which is dependent, in part, on the activation of PKC by product(s) of the PLD/PPH pathway. This provides a novel role for agonist-stimulated PLD activation.

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