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Effects of S-lactoylglutathione and inhibitors of glyoxalase I on histamine release from human leukocytes

Naturevolume 277pages135137 (1979) | Download Citation

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Abstract

THE enzyme responsible for the conversion of methylglyoxal to lactic acid by animal tissues was first named glyoxalase1,2. It was later shown that there are two glyoxalase enzymes3. The first (glyoxalase I). converts methylglyoxal and reduced glutathione to S-lactoylglutathione and the second (glyoxalase II). converts this compound to D-lactic acid, regenerating glutathione in the process. These enzymes are very widely distributed4 and as yet have no clearly defined function(s). I describe here the enhancement of anti-IgE-induced histamine release by S-lactoylglutathione and its inhibition by an inhibitor of and an alternative substrate for glyoxalase I. These two compounds should, of course, decrease the production of endogenous S-lactoylglutathione. These experiments were undertaken for two reasons. First, a study from my laboratory has provided evidence that S-lactoylglutathione modulates microtubule assembly in vitro5 while the release of histamine from leukocytes is a secretory process thought to require an intact microtubule system6,7. Second, concanavalin A has been shown to cause histamine release from human leukocytes8,9 and has also been found to activate the two glyoxalase enzymes in lymphocytes and polymorphonuclear leukocytes10.

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Affiliations

  1. Division of Clinical Immunology, Department of Medicine, The Johns Hopkins University, School of Medicine at The Good Samaritan Hospital, 5601 Loch Raven Boulevard, Baltimore, Maryland, 21239

    • ELIZABETH GILLESPIE

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https://doi.org/10.1038/277135a0

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