ACTIVATION OF GROUP VI PHOSPHOLIPASE A2 ISOFORMS IN CARDIAC ENDOTHELIAL CELLS
Washington University, Saint Louis MO
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Abstract
This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The endothelium comprises a cellular barrier between the circulation and tissues. We have previously shown that activation of protease-activated receptor-1 (PAR-1) and PAR-2 on the surface of human coronary artery endothelial cells (HCAEC) by tryptase or thrombin increases Group VIA phospholipase A2 (iPLA2[unreadable]) activity and results in production of multiple phospholipid-derived inflammatory metabolites.
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