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Title

Phospholipase A2-regulated lipid droplet formation in leukocytes

AuthorsBalsinde, Jesús
KeywordsLipid droplet
Arachidonic acid
Phospholipase A2
Issue Date2013
Citation5th International Conference on Phospholipase A2 Mediated Signaling in Translational Medicine (2013)
Abstract[Background]: Lipid droplets (LD) are cytosolic inclusions present in most eukaryotic cells that contain a core rich in neutral lipids such as triacylglycerol (TAG) and cholesteryl esters (CE) and are surrounded by a phospholipid monolayer decorated with a variety of proteins. [Objective]: We have examined the pathways for LD biosynthesis in human monocytes exposed to free arachidonic acid (AA), and studied the signaling cascade and intracellular events leading to LD formation in human monocytes. [Methods]: Mass spectrometry analyses of neutral lipids were conducted to delineate the composition of LD in monocytes exposed to AA. [Results]: Exposure of human peripheral blood monocytes to AA results in the rapid induction of LD formation by these cells. This effect appears specific for AA in that it is not mimicked by other fatty acids, whether saturated or unsaturated. LD are formed by two different routes, namely (i) the direct entry of AA into triacylglycerol and (ii) activation of intracellular signaling leading to increased triacylglycerol and cholesteryl ester formation utilizing fatty acids coming from the de novo biosynthetic route. LD formation can be completely inhibited by selective inhibition of the group IVA cytosolic phospholipase A2α (cPLA2α), pointing out this enzyme as a key regulator of AA-induced signaling. LD formation in AA-treated monocytes can also be blocked by the combined inhibition of the mitogen-activated protein kinase family members p38 and JNK, which correlates with inhibition of cPLA2α activation by phosphorylation. [Conclusions]: These results suggest that concomitant activation of both p38 and JNK by AA cooperate to activate cPLA2α, which is in turn required for LD formation possibly by facilitating biogenesis of this organelle, not by regulating neutral lipid synthesis.
DescriptionTrabajo presentado al 5th International Conference on Phospholipase A2 Mediated Signaling in Translational Medicine celebrado en New Orleans (US) del 20 al 21 de mayo de 2013.
URIhttp://hdl.handle.net/10261/117253
Appears in Collections:(IBGM) Comunicaciones congresos
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