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Papers In Press, published online ahead of print August 16, 2002
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Submitted on June 13, 2002
Molecular and Biomedical Pharmacology, University of Kentucky, Lexington, KY 40536-0298
Corresponding Author: spost{at}uky.edu
Class A macrophage scavenger receptors (SR-A) are multifunctional receptors with roles in modified lipoprotein uptake, innate immunity, and macrophage adhesion. Our previous studies conducted in mouse peritoneal macrophages demonstrated that pertussis toxin (PTX) mediated inhibition of Gi/o attenuated SR-A-dependent uptake of modified lipoprotein. The finding that SR-A-mediated lipoprotein internalization was PTX-sensitive led us to hypothesize that SR-A-mediated cell adhesion might be similarly regulated by Gi/o-dependent signaling pathways. To test this hypothesis, SR-A was expressed in HEK cells under inducible control. Relative to HEK cells that lack SR-A, SR-A expressing cells displayed enhanced adhesion to tissue culture dishes. SR-A-mediated adhesion was significantly reduced following PTX treatment and was insensitive to chelating divalent cations with EDTA. SR-A-expressing cells exhibited a distinct cell morphology characterized by fine filopodia-like projections. Both polymerized actin and vinculin were codistributed with SR-A in the filopodia-like projections indicating the formation of focal adhesion complexes. Overall, our results indicate that the ability of SR-A to enhance cell adhesion involves Gi/o activation and formation of focal adhesion complexes.
Revised on August 6, 2002
Accepted on August 7, 2002
Class A scavenger receptors mediate cell adhesion via activation of Gi/o and formation of focal adhesion complexes
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