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The Journal of Immunology, 2004, 172: 4480-4485.
Copyright © 2004 by The American Association of Immunologists

Lysophosphatidic Acid Induces Chemotaxis, Oxygen Radical Production, CD11b Up-Regulation, Ca2+ Mobilization, and Actin Reorganization in Human Eosinophils via Pertussis Toxin-Sensitive G Proteins1

Marco Idzko2,*, Martin Laut2,*, Elisabeth Panther{dagger}, Stephan Sorichter*, Thorsten Dürk*, Joachim W. Fluhr{ddagger}, Yared Herouy{dagger}, Maja Mockenhaupt{dagger}, Daniel Myrtek*, Peter Elsner{ddagger} and Johannes Norgauer3,{ddagger}

Departments of * Pneumonology and {dagger} Experimental Dermatology, University of Freiburg, Freiburg, Germany; and {ddagger} Department of Dermatology, University of Jena, Jena, Germany

Lysophosphatidic acid (LPA) is a bioactive lipid mediator, which is generated by secretory type II phospholipase A2 and is thought to play a major role in the pathogenesis of atopic diseases. In this study, the biological activity of LPA on human eosinophils was characterized. We showed by reverse transcription and PCR that human eosinophils express the mRNA of the LPA receptors endothelial differentiation gene (EDG)-2 and EDG-7. Experiments revealed that LPA has chemotactic activity toward eosinophils, stimulates the production of reactive oxygen metabolites, and induces up-regulation of the integrin CD11b. Signal pathway measurements indicated Ca2+-mobilization from intracellular stores and transient actin polymerization upon stimulation with LPA. Cell responses elicited by LPA were inhibited by pertussis toxin indicating that in eosinophils the LPA receptor(s), presumably EDG-2 and/or EDG-7, are coupled to Gi/o proteins. Moreover, LPA-induced activation of eosinophils could be completely blocked by the EDG-2/EDG-7 antagonist diacylglycerol pyrophosphate. In addition, at optimal doses the changes induced by LPA were comparable to those obtained by the other well-characterized chemotaxins. These results indicate that LPA is a strong chemotaxin and activator of eosinophils. These findings point to a novel role of LPA in the pathogenesis of diseases with eosinophilic inflammation such as atopic diseases as chemotaxin as well as activator of proinflammatory effector functions.




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