Group XV phospholipase A2, a lysosomal phospholipase A2
نویسندگان
چکیده
منابع مشابه
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...
متن کاملLysosomal 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 ...
متن کاملPositional 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...
متن کاملInhibition of phospholipase A2.
Phospholipases A2 are involved in inflammatory processes such as the liberation of free arachidonic acid from the membrane pool for the biosynthesis of eicosanoids. Inhibitors of these enzymes are proving useful in determining the biological roles of phospholipases A2 in complex cellular processes and may also have therapeutic potential. Inhibition of these lipolytic enzymes is more difficult t...
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ژورنال
عنوان ژورنال: Progress in Lipid Research
سال: 2011
ISSN: 0163-7827
DOI: 10.1016/j.plipres.2010.10.006