Protein kinase C dependent and independent activation of phospholipase A2 under calcium ionophore (A23187) exposure in rabbit pulmonary arterial smooth muscle cells

FEBS Letters

Patra, Samir K.¹  Michael, John R.²  Chakraborti, Sajal¹ 

[1] Department of Biochemistry and Biophysics, University of Kalyani, Kalyani 741 235, India;Department of Medicine, University of Utah Health Sciences Center, Salt Lake City, Utah 84132, USA

关键词: Calcium ionophore;    Phospholipase A2;    Arachidonic acid;    Sphingosine;    Protein kinase C;    Smooth muscle cell;    Calcium signalling;    AA;    arachidonic acid;    PLA2;    phospholipase A2;    A23187;    calcium ionophore;    PKC;    protein kinase C;    PBS;    phosphate buffered saline;    FCS;    fetal calf serum;    HEPES;    4-(2-hydroxyethyl)-1-piperazine N-2-ethanesulfonate;    ATP;    adenosine triphosphate;    HBPS;    Hank's buffered physiological solution;   

DOI  :  10.1016/0014-5793(91)80735-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Exposure of rabbit pulmonary arterial smooth muscle cells to the calcium ionophore A23187, dose-dependently stimulates arachidonic acid (AA) release and phospholipase A₂ (PLA₂) activity. The protein kinase C (PKC) inhibitor, sphingosine does not prevents AA release and PLA₂ activity caused by low doses of A23187. In contrast, sphingosine markedly prevents AA release and PLA₂ 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.

【 授权许可】

Unknown