Document Detail

Exosomes account for vesicle-mediated transcellular transport of activatable phospholipases and prostaglandins.
MedLine Citation:
PMID:  20424270     Owner:  NLM     Status:  MEDLINE    
Exosomes are bioactive vesicles released from multivesicular bodies (MVB) by intact cells and participate in intercellular signaling. We investigated the presence of lipid-related proteins and bioactive lipids in RBL-2H3 exosomes. Besides a phospholipid scramblase and a fatty acid binding protein, the exosomes contained the whole set of phospholipases (A2, C, and D) together with interacting proteins such as aldolase A and Hsp 70. They also contained the phospholipase D (PLD) / phosphatidate phosphatase 1 (PAP1) pathway leading to the formation of diglycerides. RBL-2H3 exosomes also carried members of the three phospholipase A2 classes: the calcium-dependent cPLA(2)-IVA, the calcium-independent iPLA(2)-VIA, and the secreted sPLA(2)-IIA and V. Remarkably, almost all members of the Ras GTPase superfamily were present, and incubation of exosomes with GTPgammaS triggered activation of phospholipase A(2) (PLA(2))and PLD(2). A large panel of free fatty acids, including arachidonic acid (AA) and derivatives such as prostaglandin E(2) (PGE(2)) and 15-deoxy-Delta(12,14)-prostaglandinJ(2) (15-d PGJ(2)), were detected. We observed that the exosomes were internalized by resting and activated RBL cells and that they accumulated in an endosomal compartment. Endosomal concentrations were in the micromolar range for prostaglandins; i.e., concentrations able to trigger prostaglandin-dependent biological responses. Therefore exosomes are carriers of GTP-activatable phospholipases and lipid mediators from cell to cell.
Caroline Subra; David Grand; Karine Laulagnier; Alexandre Stella; Gérard Lambeau; Michael Paillasse; Philippe De Medina; Bernard Monsarrat; Bertrand Perret; Sandrine Silvente-Poirot; Marc Poirot; Michel Record
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-27
Journal Detail:
Title:  Journal of lipid research     Volume:  51     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-15     Completed Date:  2010-10-20     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2105-20     Citation Subset:  IM    
Metabolism, Oncogenesis and Cell Differentiation Group, INSERM Research Center 563, Pathophysiology Center of Toulouse Purpan, Hôpital Purpan, Toulouse, France.
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MeSH Terms
Biological Transport
Cell Line
Dinoprostone / metabolism
Endosomes / metabolism
Enzyme Activation / drug effects
Exosomes / drug effects,  metabolism*
Guanosine Triphosphate / pharmacology
Phosphatidate Phosphatase / metabolism
Phospholipase D / metabolism
Phospholipases / metabolism*
Phospholipases A2 / metabolism
Prostaglandin D2 / analogs & derivatives,  metabolism
Prostaglandins / metabolism*
Proteome / metabolism
Reg. No./Substance:
0/Prostaglandins; 0/Proteome; 363-24-6/Dinoprostone; 41598-07-6/Prostaglandin D2; 60203-57-8/9-deoxy-delta-9-prostaglandin D2; 86-01-1/Guanosine Triphosphate; EC 3.1.-/Phospholipases; EC A2; EC Phosphatase; EC 3.1.4.-/phospholipase D2; EC D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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