The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL‐1 through ERM proteins
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2011
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Wiley
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Domínguez‐Luis, Maria, et al. «The Metalloprotease ADAM8 Is Associated with and Regulates the Function of the Adhesion Receptor PSGL‐1 through ERM Proteins». European Journal of Immunology, vol. 41, n.o 12, diciembre de 2011, pp. 3436-42. https://doi.org/10.1002/eji.201141764.
Abstract
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.
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This work was supported by grants from the Spanish Ministry of Health (Fondo de Investigaciones Sanitarias) to A. Urzainqui (FIS-PI080894) and to F. Díaz González (FIS 09/02209), by grants from Ministerio de Ciencia e Innovación to F. S. M. (SAF2008-02635) and to F. M. (SAF2008-02251) and by the Redes RIER, RTICC (RD06/0020/1037) and RECAVA del Instituto de Salud Carlos III and RTICCR.