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Originally published In Press as doi:10.1074/jbc.M007065200 on October 17, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1564-1569, January 12, 2001
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Outside-in Signaling Pathway Linked to CD146 Engagement in Human Endothelial Cells*

Francine AnfossoDagger , Nathalie Bardin, Eric Vivier§, Florence Sabatier, José Sampol, and Françoise Dignat-George

From the INSERM EMI 00-19 Physiopathologie de l'Endothélium, UFR Pharmacie, Université de la Mediterranée, 13385 Marseille and the § Centre d'Immunologie INSERM-CNRS Marseille Luminy and Institut Universitaire de France, 13276 Marseille, France

CD146 (S-Endo 1 Ag or MUC18) is a transmembrane glycoprotein expressed on endothelial cells on the whole vascular tree. CD146 is located at the intercellular junction where it plays a role in the cohesion of the endothelial monolayer. CD146 engagement initiates an outside-in signaling pathway involving the protein tyrosine kinases FYN and FAK as well as paxillin. Here we report that CD146 engagement by its specific monoclonal antibody in human umbilical vein endothelial cells induces a Ca2+ influx that is sensitive to thapsigargin and EGTA treatment, indicating that CD146 engagement initiates a store-operated calcium mobilization. In addition, biochemical and pharmacological analysis revealed that CD146 engagement initiates the tyrosine phosphorylation of phospholipase C-gamma , Pyk2, and p130Cas. Pharmacological inhibition of Ca2+ flux with 1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acetoxymethyl ester and EGTA indicated that an increase in Ca2+ is required for Pyk2 and p130Cas tyrosine phosphorylation. Moreover, a complex association was observed between Pyk2, p130Cas, and paxillin. These results indicate that CD146 is coupled to a FYN-dependent pathway that triggers Ca2+ flux via phospholipase C-gamma activation leading subsequently to the tyrosine phosphorylation of downstream targets such as Pyk2, p130Cas, FAK, and paxillin. In addition to its role in cell-cell adhesion, CD146 is a signaling molecule involved in the dynamics of actin cytoskeleton rearrangement.

* This work was supported by Ministère de l'Education Nationale Grant UPRES EA.2195 and INSERM.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: EMI 00-19, Laboratoire d'Hématologie-Immunologie, UFR Pharmacie, 27 Bd. Jean Moulin, 13385 Marseille Cedex 5, France. Tel.: 33 4 91 83 56 00; Fax: 33 4 91 83 56 02; E-mail: anfosso@pharmacie.univ-mrs.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.