| Autor: |
Flesch, I., Schonhardt, T., Ferber, E. |
| Zdroj: |
Klinische Wochenschrift; Feb1989, Vol. 67 Issue 3, p119-122, 4p |
| Abstrakt: |
In contrast to many other cells, macrophages contain a phospholipase A, which preferentially liberates arachidonic acid from the main phospholipids. In unstimulated macrophages this acylchain-specific phsopholipase A is localized in the lipid-free cytosol and thus without function. After activation of protein kinase C with diacylglycerols, the cytosolic phospholipase A 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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