Abstract
5-Lipoxygenase (5-LO) is the key enzyme in the biosynthesis of proinflammatory leukotrienes from arachidonic acid (AA) [1]. Ca2+, phosphatidylcholine, ATP, and hydroperoxides stimulate the enzymatic activity of 5-LO in vitro [1]. However, the mechanisms involved in the agonist-induced 5-LO activation in intact cells are less clear. Stimuli that cause an elevation of the intracellular Ca2+ levels activate 5-LO. Ca2+ binds 5-LO in vitro at the enzyme’s C2 domain [2], which is a prerequisite for association with membranes [3].
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References
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© 2003 Springer Science+Business Media New York
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Werz, O. et al. (2003). 5-Lipoxygenase Activation by Mapkapk-2 and Erks. In: Yazici, Z., Folco, G.C., Drazen, J.M., Nigam, S., Shimizu, T. (eds) Advances in Prostaglandin, Leukotriene, and other Bioactive Lipid Research. Advances in Experimental Medicine and Biology, vol 525. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9194-2_26
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DOI: https://doi.org/10.1007/978-1-4419-9194-2_26
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