A Bifunctional Role for Group IIA Secreted Phospholipase A2 in Human Rheumatoid Fibroblast-like Synoviocyte Arachidonic Acid Metabolism

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Selective inhibition of human group IIA-secreted phospholipase A2 (hGIIA) signaling reveals arachidonic acid metabolism is associated with colocalization of hGIIA to vimentin in rheumatoid synoviocytes.

Human group IIA secreted phospholipase A2 (hGIIA) promotes tumor growth and inflammation and can act independently of its well described catalytic lipase activity via an alternative poorly understood signaling pathway. With six chemically diverse inhibitors we show that it is possible to selectively inhibit hGIIA signaling over catalysis, and x-ray crystal structures illustrate that signaling i...

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Functionally selective inhibition of human secreted phospholipase A2. Selective inhibition of human group IIA secreted phospholipase A2 (hGIIA) signaling reveals arachidonic acid metabolism is associated with colocalization of hGIIA to vimentin in rheumatoid synoviocytes *

Background: Group IIA secreted phospholipase A2 (hGIIA) is a bifunctional protein that regulates arachidonic acid metabolism by both catalysis-dependent and catalysis–independent mechanisms. Results: Selective inhibition of the catalysisindependent signaling function perturbs a hGIIA-vimentin interaction in rheumatoid synoviocytes. Conclusion: The signaling and catalytic functions of hGIIA are ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2011

ISSN: 0021-9258

DOI: 10.1074/jbc.m110.123927