Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism

Article Abstract:

A study was conducted to examine the crystal structure of human cytosolic phospholipase A2. Results indicate that the human cytosolic phospholipase A2 is composed of a distinct catalytic unit and a N-terminal calcium-dependent lipid-binding/C2 domain. Its main function is to stimulate the biosynthesis of prostaglandins, leukotrienes and platelet-activating factor that mediates the pathophysiology of asthma and arthritis.

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The secretory granule protein syncollin binds to syntaxin in a Ca2+-sensitive manner

Article Abstract:

Syncollin, an 18-kDa protein, that binds to syntaxin at low Ca2+ concentrations and dissociates at concentrations known to stimulate exocytosis is present in the membranes of exocrine secretory granules. Syncollin exhibited no significant homology with any known protein. The findings indicate that syncollin functions as a Ca2+-sensitive regulator of exocytosis in exocrine tissues.

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Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells

Article Abstract:

Nonpancreatic secretory phospholipase A2 (sPLA2) may be involved in cell signaling during the inflammatory response. This enzyme degrades phospholipids in microvesicles shed from Ca2+-loaded erythrocytes, apparently increasing in activity during sphingomyelin hydrolysis. Phosphatidic acid is converted to the lipid mediator lysophosphatidic acid by sPLA2.

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