Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1
Biochemistry, ISSN: 0006-2960, Vol: 37, Issue: 44, Page: 15481-15490
1998
- 53Citations
- 38Captures
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Metrics Details
- Citations53
- Citation Indexes53
- 53
- CrossRef43
- Captures38
- Readers38
- 38
Article Description
Lipoxygenases catalyze the biosynthesis of leukotrienes, lipoxins, and other lipid-derived mediators that are involved in a wide variety of pathophysiological processes, including inflammation, allergy, and tumorigenesis. Mammalian lipoxygenases are activated by a calcium-mediated translocation to intracellular membranes upon cell stimulation, and cooperate with cytosolic phospholipase A at the membrane surface to generate eicosanoids. Although it has been documented that plant cell stimulation increases intracellular Ca concentration and activates cytosolic phospholipase A, followed by lipoxygenase-catalyzed conversion of the liberated linolenic acid to jasmonic acid, no evidence is available for Ca-regulated membrane binding and activity of plant lipoxygenases. Plant lipoxygenases, unlike their mammalian counterparts, are believed to function independently of calcium or membranes. Here we present spectroscopic evidence for a calcium-regulated membrane-binding mechanism of soybean lipoxygenase-1 (L-1). Both calcium and membrane binding affect the structure and the mode of action of L-1. Free L-1 in solution is less accessible to the polar solvent and converts linoleic acid to conjugated dienes, whereas surface binding increases solvent accessibility and stimulates conjugated ketodiene production. Calcium exerts a biphasic effect on the structure and activity of L-1. Our results uncover a new regulatory mechanism for plant lipoxygenases and delineate common features in animal and plant cell signaling pathways.
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