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Published online before print September 28, 2007, 10.1110/ps.073007207
Protein Science (2007), 16:2531-2541. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Cd36, a class B scavenger receptor, functions as a monomer to bind acetylated and oxidized low-density lipoproteins

Catherine A. Martin1, Emma Longman2, Carol Wooding1, Sarah J. Hoosdally1, Saira Ali1, Timothy J. Aitman1, Daniel A.P. Gutmann3, Paul S. Freemont3, Bernadette Byrne3, and Kenneth J. Linton1

1 MRC Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN, United Kingdom
2 Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom
3 Division of Molecular Biosciences, Imperial College, South Kensington Campus, London SW7 2AZ, United Kingdom

(RECEIVED May 17, 2007; FINAL REVISION August 9, 2007; ACCEPTED August 13, 2007)

Cd36 is a small-molecular-weight integral membrane protein expressed in a diverse, but select, range of cell types. It has an equally diverse range of ligands and physiological functions, which has implicated Cd36 in a number of diseases including insulin resistance, diabetes, and, most notably, atherosclerosis. The protein is reported to reside in detergent-resistant microdomains within the plasma membrane and to form homo- and hetero-intermolecular interactions. These data suggest that this class B scavenger receptor may gain functionality for ligand binding, and/or ligand internalization, by formation of protein complexes at the cell surface. Here, we have overexpressed Cd36 in insect cells, purified the recombinant protein to homogeneity, and analyzed its stability and solubility in a variety of nonionic and zwitterionic detergents. Octylglucoside conferred the greatest degree of stability, and by analytical ultracentrifugation we show that the protein is monomeric. A solid-phase ligand-binding assay demonstrated that the purified monomeric protein retains high affinity for acetylated and oxidized low-density lipoproteins. Therefore, no accessory proteins are required for interaction with ligand, and binding is a property of the monomeric fold of the protein. Thus, the highly purified and functional Cd36 should be suitable for crystallization in octylglucoside, and the in vitro ligand-binding assay represents a promising screen for identification of bioactive molecules targeting atherogenesis at the level of ligand binding.

Keywords: Cd36; scavenger receptor; ligand binding; protein purification; low-density lipoprotein; oxidized LDL; atherosclerosis; membrane protein


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