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Protein kinase C dependent and independent activation of phospholipase A 2 under calcium ionophore (A23187) exposure in rabbit pulmonary arterial smooth muscle cells
Author(s) -
Chakraborti Sajal,
Michael John R.,
Patra Samir K.
Publication year - 1991
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 - 10.1016/0014-5793(91)80735-l
Subject(s) - ionophore , protein kinase c , cytosol , phospholipase a2 , calcium , sphingosine , arachidonic acid , phospholipase c , endocrinology , medicine , chemistry , biology , biochemistry , kinase , enzyme , receptor
Exposure of rabbit pulmonary arterial smooth muscle cells to the calcium ionophore A23187, dose‐dependently stimulates arachidonic acid (AA) release and phospholipase A 2 (PLA 2 ) activity. The protein kinase C (PKC) inhibitor, sphingosine does not prevents AA release and PLA 2 activity caused by low doses of A23187. In contrast, sphingosine markedly prevents AA release and PLA 2 activity caused by higher doses of A23187. PKC activity profile indicates that treatment of the cells with low doses of A23187 does not cause significant alteration of PKC translocation from cytosol to membrane whereas higher concentrations of the ionophore dose‐dependently enhance PKC translocation from Cytosol to membrane in the smooth muscle cells.