Positional specificity of lysosomal phospholipase A2

Positional specificity of lysosomal phospholipase A2.

Lysosomal phospholipase A(2) (Lpla2) is highly expressed in alveolar macrophages and may mediate the phospholipid metabolism of surfactant. Studies on the properties of this phospholipase are consistent with the presence of both phospholipase A(1) and phospholipase A(2) activities. These activities were studied through the production of O-acyl compounds, produced by the transacylase activity of...

Lysosomal phospholipase A2 and phospholipidosis.

A lysosomal phospholipase A2, LPLA2, was recently characterized and shown to have substrate specificity for phosphatidylcholine and phosphatidylethanolamine. LPLA2 is ubiquitously expressed but is most highly expressed in alveolar macrophages. Double conditional gene targeting was employed to elucidate the function of LPLA2. LPLA2-deficient mice (Lpla2-/-) were generated by the systemic deletio...

Lysosomal phospholipase A2 Lysosomal Phospholipase A2 is Selectively Expressed in Alveolar Macrophages*

Lung surfactant is the surface-active agent comprised of phospholipids and proteins that lines pulmonary alveolae. Surfactant stabilizes the alveolar volume by reducing surface tension. Previously, we identified a phospholipase A2, termed LPLA2, with specificity towards phosphatidylcholine and phosphatidylethanolamine. The phospholipase is localized to lysosomes, is calcium independent, has an ...

Structure and function of lysosomal phospholipase A2

Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase

Lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structurally uncharacterized family of key lipid-metabolizing enzymes responsible for lung surfactant catabolism and for reverse cholesterol transport, respectively. Whereas LPLA2 is predicted to underlie the development of drug-induced phospholipidosis, somatic mutations in LCAT cause fish eye diseas...