The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL-1 through ERM proteins.

Maria Domínguez-Luis, Amalia Lamana, Jesús Vazquez, Rósula García-Navas, Faustino Mollinedo, Francisco Sánchez-Madrid, Federico Díaz-González, Ana Urzainqui

Servicio de Reumatología, Hospital Universitario de Canarias, La Laguna, Santa Cruz de Tenerife, Spain.

European journal of immunology 2011 Dec

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The P-selectin glycoprotein ligand-1 (PSGL-1) is involved in the initial contact of leukocytes with activated endothelium, and its adhesive function is regulated through its proteolytic processing. We have found that the metalloprotease ADAM8 is both associated with PSGL-1 through the ezrin–radixin–moesin actin-binding proteins and able to cause the proteolytic cleavage of this adhesion receptor. Accordingly, ADAM8 knockdown increases PSGL-1 expression, and functional assays show that ADAM8 is able to reduce leukocyte rolling on P-selectin and hence on activated endothelial cells. We conclude that ADAM8 modulates the expression and function of PSGL-1. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Citation

Maria Domínguez-Luis, Amalia Lamana, Jesús Vazquez, Rósula García-Navas, Faustino Mollinedo, Francisco Sánchez-Madrid, Federico Díaz-González, Ana Urzainqui. The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL-1 through ERM proteins. European journal of immunology. 2011 Dec;41(12):3436-42