Phospholipases and acyltransferases in macrophages |
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Authors: | I Flesch T Schonhardt E Ferber |
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Institution: | (1) Max-Planck-Institut für Immunbiologie, Freiburg |
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Abstract: | Summary In contrast to many other cells, macrophages contain a phospholipase A2, which preferentially liberates arachidonic acid from the main phospholipids. In unstimulated macrophages this acylchain-specific phsopholipase A2 is localized in the lipid-free cytosol and thus without function. After activation of protein kinase C with diacylglycerols, the cytosolic phospholipase A2 is translocated to cellular membranes. The same activator of protein kinase C causes an inhibition of the acyl-CoA: lysophosphatide acyltransferase. This enzyme regulates the availability of free arachidonic acid for eicosanoid synthesis by reacylation into phospholipids. Thus protein kinase C seems to regulate the level of free arachidonic acid by opposite effects on the two major enzymes, which are responsible for the control of free arachidonic acid. |
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Keywords: | Macrophage Phospholipase A2 Translocation Reacylation |
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