HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Weller, P. F. Articles by Jaffe, J. J. Search for Related Content PubMed PubMed Citation Articles by Weller, P. F. Articles by Jaffe, J. J.

Leukotriene C₄ Synthesis Catalyzed by Dirofilaria Immitis Glutathione S-Transferase

The biologically active sulfidopeptide leukotriene, leukotriene C₄, is formed by the enzymatic action of leukotriene C₄ synthase, which conjugates glutathione with leukotriene A₄. We have found that a filarial glutathione S-transferase can function as a leukotriene C₄ synthase. Glutathione S-transferase was purified from the cytosol of adult Dirofilaria immitis by glutathione-agarose affinity chromatography and was reacted with 25 µM leukotriene A₄ methyl ester and 10 mM glutathione. The filarial enzyme catalyzed the formation of leukotriene C₄ methyl ester, as shown by reverse phase high pressure liquid chromatographic analyses. The finding that filarial glutathione S-transferase can function as a leukotriene C₄ synthase provides a mechanism whereby filarial parasites could form lipoxygenase pathway derived sulfidopeptide leukotrienes.