Platelet-activating Factor Acetylhydrolases

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Selective inhibitor of platelet-activating factor acetylhydrolases 1b2 and 1b3 that impairs cancer cell survival.

Platelet-activating factor acetylhydrolases (PAFAHs) 1b2 and 1b3 are poorly characterized serine hydrolases that form a complex with a noncatalytic protein (1b1) to regulate brain development, spermatogenesis, and cancer pathogenesis. Determining physiological substrates and biochemical functions for the PAFAH1b complex would benefit from selective chemical probes that can perturb its activity ...

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Platelet-activating factor.

Platelet-activating factor is a phospholipid with diverse potent physiological effects. Its actions are achieved at concentrations as low as IO-‘” M in some systems and almost always by lo-’ M as an intercellular messenger. The molecular structure of PAF was discovered through parallel investigations of two different biological activities: a factor in the blood of rabbits undergoing anaphylaxis...

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Platelet-activating factor.

Our ability to chemically characterize and synthesize this autacoid of allergy and inflammation has given us a unique opportunity to study these important molecules in a highly disciplined fashion. It has also opened the door to a vista of research approaches to define PAF's normal physiologic role as well as its actions as an immunopathologic mediator. Recent work is described.

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Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme.

Platelet-activating factor acetylhydrolases (PAF-AHs) are a group of enzymes that hydrolyze the sn-2 acetyl ester of PAF (phospholipase A(2) activity) but not phospholipids with two long fatty acyl groups. Our previous studies showed that membrane-bound human plasma PAF-AH (pPAF-AH) accesses its substrate only from the aqueous phase, which raises the possibility that this enzyme can hydrolyze a...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1997

ISSN: 0021-9258

DOI: 10.1074/jbc.272.29.17895