Calcium-independent phospholipase A2 mediates CREB phosphorylation in double-stranded RNA-stimulated endothelial cells. J Lipid Res 2003 Sep;44(9):1686-91
Date
06/18/2003Pubmed ID
12810819DOI
10.1194/jlr.M300018-JLR200Scopus ID
2-s2.0-0141682494 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
One of the products of a calcium-independent phospholipase A2 (iPLA2) attack of plasmenylcholine, lysoplasmenylcholine, has previously been shown to activate cAMP-dependent protein kinase (PKA). Because endothelial cells respond to some agonists in part by the activation of iPLA2, the present study was designed to determine whether double-stranded RNA (dsRNA), the primary activator of the antiviral response in endothelial cells, elicits cAMP response element binding protein (CREB) phosphorylation through a mechanism mediated by iPLA2. dsRNA stimulated CREB phosphorylation in bovine pulmonary artery endothelial cells that was inhibited by the iPLA2 inhibitor, bromoenol lactone, and the PKA inhibitor, H-89. Additionally, the product of iPLA2 hydrolysis of plasmenylcholine and lysoplasmenylcholine elicited CREB phosphorylation in bovine pulmonary endothelial cells. Taken together, the present studies suggest that dsRNA as well as other agonists of endothelial cells elicit signaling mechanisms that include in part CREB phosphorylation mediated by iPLA2.
Author List
Martinson BD, Albert CJ, Corbett JA, Wysolmerski RB, Ford DAAuthor
John A. Corbett PhD Chair, Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCarrier Proteins
Cattle
Cells, Cultured
Cyclic AMP Response Element-Binding Protein
Cyclic AMP-Dependent Protein Kinases
Endothelial Cells
Group VI Phospholipases A2
Intracellular Signaling Peptides and Proteins
Lipopolysaccharides
Lysophospholipids
Phospholipases A
Phospholipases A2
Phosphorylation
Poly I-C
Pulmonary Artery
RNA, Double-Stranded
Tetradecanoylphorbol Acetate
