Type II phospholipase A2

By definition, phospholipase A, (PI.Aj) is an enzyme that can remove fatty acids from the middle Isn-1 carbon atom of phosphoglycerides. Although several different phospholipase A2 enzymes occur in mammalian cells, only one of these - a 14 kDa type 2 PLA2 that is also called secretory PI.A, (sPLAO - has potent microbicidal properties. sPl.A, differs substantially from the type 1 PI..A, found in pancreatic secretions, both in its preference for phospholipid substrates such as phosphatidylethanolamine, which are prominent in bacterial membranes, over phosphatidylcholine, and in significant aspects of its primary structure.

sPLA, is present in secretory (nonazurophil) granules of human neutrophils and in the secretory granules of small intestinal Paneth cells. The entry of sPLA2 into the neutrophil's phagocytic vacuoles has been demonstrated by immunoelectron microscopy, sPLA2 is secreted extracellularly from neutrophils exposed to secretagogues, such as phorbol esters or calcium ionophore, and by Paneth cells exposed to bethanecol (a parasympathomimetic agonist), bacteria or LPS. Serum sPLA2 is greatly elevated in patients with bacterial infections or sepsis, and rises sharply within 3 hours of the experimental administration of LPS to uninfected patients. High concentrations of sPLA2 are also present in human tears.

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