Abstract
The liberation of arachidonic acid (AA) is thought to be the rate-limiting step in prostanoid synthesis of rat-liver macrophages (RLM)1. The best known pathway for AA-liberation is elicited by the activation of a phospholipase (PL)A2 hydrolysing the ester-bond in sn-2-position of phospholipids2. It has been shown that RLM express a cPLA2 very similar to cPLA2 recently identified in U937 cells2: the enzyme has an apparant molecular weight of 100 kDa in SDS-polyacrylamide-gelelectrophoresis (PAGE), an alkaline pH-optimum, is strictly dependent on the presence of Ca2+ in the range from 10−7–10−6 M and shows a Ca2+-dependent translocation to cellular membranes1,2. cPLA2 phosphorylation by mitogen activated protein (MAP) kinase is also discussed as a mechanism for cPLA2 activation3. Another pathway leading to AA-release in RLM involves the activation of a PLC leading to free diacylglycerol (DAG), which serves as substrate for DAG-lipase to liberate free AA4.KeywordsArachidonic AcidU937 Cells2Kinase AssayExtracellularly Regulate KinaseArachidonic Acid ReleaseThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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