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A more recent version of this article appeared on June 1, 2008

Papers In Press, published online ahead of print February 27, 2008
J. Lipid Res., doi:10.1194/jlr.M700602-JLR200
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Submitted on December 28, 2007
Revised on February 22, 2008
Accepted on February 26, 2008

Inhibition of lipoxygenases and cyclooxygenases by linoleyl hydroxamic acid: Comparative in vitro studies

Igor A. Butovich and Svetlana M. Lukyanova

Ophthalmology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9057

Corresponding Author: igor.butovich{at}utsouthwestern.edu

In this first comparative in vitro study, linoleyl hydroxamic acid (LHA) – a simple and stable derivative of linoleic acid – was tested as inhibitor of several enzymes involved in arachidonic acid metabolism in mammals. The tested enzymes were human recombinant 5-lipoxygenase (hr5-LO), porcine leukocyte 12-LO, rabbit reticulocyte 15-LO, ovine cyclooxygenases 1/2 (COX1/COX2), and human microsomal prostaglandin E synthase-1 (mPGES-1). Potato and soybean lipoxygenases (ptLOX and sLOX, respectively) were studied for comparative purposes. LHA inhibited most of the tested enzymes with the exception of mPGES-1. The LHA inhibitory activity increased as follows: mPGES-1 (no inhibition)<


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