Abstract
Plasmalogens-phospholipids containing a characteristic vinyl ether group-are precursors of lipids important for cellular signaling such as arachidonic acid. Plasmalogen catabolism involves cleavage of the vinyl ether bond, but the identity of the corresponding enzyme that cleaves the sn-1 vinyl ether bond was unknown. New research shows that cytochrome c, with some help from another lipid, catalyzes the oxidative cleavage of this bond. This discovery, and the subsequent mechanistic dissection, provides exciting new directions for lipid signaling research.
Highlights
Plasmalogens are a type of phospholipid defined by the presence of an alkene group next to an ether linkage (Fig. 1)
Sensitivity to ROS has led to the proposal that plasmalogens could serve as protection against ROS; in this model, hydrolysis by an unknown ROS-consuming mechanism could be reversed by a well-known acyl-CoA– dependent reaction [2]
Cyt c can function as a peroxidase, which is induced by the binding of the mitochondrial lipid cardiolipin (CL), resulting in a change in the conformation of the protein and a dramatic change in its redox potential from ϩ260 to Ϫ400 mV
Summary
Plasmalogens are a type of phospholipid defined by the presence of an alkene group next to an ether linkage (Fig. 1). Sensitivity to ROS has led to the proposal that plasmalogens could serve as protection against ROS; in this model, hydrolysis by an unknown ROS-consuming mechanism could be reversed by a well-known acyl-CoA– dependent reaction [2]. The pathway by which plasmalogens are produced in animal cells is known: An oxygen-dependent desaturation creates the characteristic double bond from a saturated substrate [1].
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