Modulation of Phospholipase A2 Lytic Activity by Actin and Myosin
Abstract
Prostacylin (PGI2) productions closely coupled with endothelial cell shape and F-actin distribution in vitro. These findings may implicate cytoskeletal constituents in a mechanism regulating eicosanoid metabolism. To determine the potential for such a regulatory mechanism, cytoskeletal protein effects on the rate-limiting eicosanoid cascade enzyme (phospholipase A2, PLA2) were studied. Membrane phospholipid degradation was indirectly determined by spectrophotometric measurement of PLA 2 induced rat red blood cell ghost (RBC-G) hemolysis. PLA 2 was incubated with actin (skeletal, smooth, or non-muscle cell) at a non-muscle cell concentration (100 micromoles and then exposed to the RBC-G Comparisons in the presence or absence of actin revealed that F-actin stimulated whereas G-action suppressed PLA2 lytic behavior significantly (P< 0.05). When a 10: or 100: 1 F-actin to myosin-ratio was used, the F-actin stimulatory effect was significantly (P<0.05) reduced. These finding s suggest that the in vitro correlation between PGI 2 production and endothelial cell shape may be the result of PLA 2 regulation by cytoskeletal elements that impart cellular form.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1989
- Accession Number
- ADA206245
Entities
People
- D. A. Dubose
- D. Shepro
- H. B. Hechtman
Organizations
- United States Army Research Institute of Environmental Medicine