Macrophage Scavenger Receptor A Mediates Adhesion to Apolipoproteins A-I and E | Zendy

Claudine Neyen | Zendy; Annette Plüddemann | Zendy; Pietro Roversi | Zendy; Benjamin Thomas | Zendy; Lei Cai | Zendy; Deneys R. van der Westhuyzen | Zendy; Robert B. Sim | Zendy; Siamon Gordon | Zendy

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Macrophage Scavenger Receptor A Mediates Adhesion to Apolipoproteins A-I and E

Author(s) -

Claudine Neyen,

Annette Plüddemann,

Pietro Roversi,

Benjamin Thomas,

Lei Cai,

Deneys R. van der Westhuyzen,

Robert B. Sim,

Siamon Gordon

Publication year - 2009

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi9013769

Subject(s) - scavenger receptor , chemistry , macrophage , vitronectin , cell adhesion , apolipoprotein e , inflammation , integrin , glycation , receptor , extracellular matrix , cell adhesion molecule , pattern recognition receptor , glycosylation , microbiology and biotechnology , biochemistry , innate immune system , immunology , biology , lipoprotein , cell , cholesterol , medicine , pathology , disease , in vitro

Macrophage scavenger receptor A (SR-A) is a multifunctional, multiligand pattern recognition receptor with roles in innate immunity, apoptotic cell clearance, and age-related degenerative pathologies, such as atherosclerosis and Alzheimer's disease. Known endogenous SR-A ligands are polyanionic and include modified lipoproteins, advanced glycation end products, and extracellular matrix proteins. No native plasma ligands have been identified, but it is known that SR-A recognition of unidentified serum components mediates integrin-independent macrophage adhesion, which may drive chronic local inflammation. In this study, we used a high-throughput fractionation and screening method to identify novel endogenous SR-A ligands that may mediate macrophage adhesion. SR-A was found to recognize the exchangeable apolipoproteins A-I and E (apo A-I and apo E, respectively) in both lipid-free and lipid-associated form, suggesting the shared amphipathic alpha-helix as a potential recognition motif. Adhesion of RAW 264.7 macrophages to surfaces coated with apo A-I and apo E4 proved to be integrin-independent and could be blocked by anti-SR-A antibodies. The presence of apo A-I and apo E in pathological deposits, such as atherosclerotic lesions and neurotoxic Alzheimer's plaques, suggests a possible contribution of SR-A-dependent adhesion of macrophages to an inflammatory microenvironment.

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