Abstract
Scavenger receptors bind modified low-density lipoproteins (LDL) on a collagen-like domain which possesses a lysine cluster at the carboxy end. We previously constructed a receptor model peptide containing the lysine cluster. In the present study, we evaluated the ligand specificity of the receptor model peptide. It selectively bound modified-LDLs, and not LDL. The binding of acetylated-LDL (Ac-LDL) was inhibited by dextran sulfate, fucoidan, and sulfatides in a manner similar to that of the natural receptor. Both polyguanylic and polyinosinic acids inhibit the Ac-LDL binding whereas polycytidylic acid did not. These results indicate that the lysine cluster in the collagen-like domain has important roles in both ligand binding and ligand specificity.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cell Adhesion Molecules*
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Cells, Cultured
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Collagen / chemistry*
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Dextran Sulfate / pharmacology
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Humans
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Kinetics
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Ligands
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Lipoproteins, LDL / metabolism*
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Lysine*
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Macrophages, Peritoneal / metabolism*
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Membrane Proteins*
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Mice
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Molecular Sequence Data
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Polysaccharides / pharmacology
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Receptors, Immunologic / chemistry*
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Receptors, Immunologic / drug effects
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Receptors, Immunologic / metabolism*
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Receptors, LDL / chemistry
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Receptors, LDL / drug effects
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Receptors, LDL / metabolism*
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Receptors, Lipoprotein*
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Receptors, Scavenger
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Scavenger Receptors, Class B
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Substrate Specificity
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Sulfoglycosphingolipids / pharmacology
Substances
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Cell Adhesion Molecules
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Ligands
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Lipoproteins, LDL
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Membrane Proteins
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Peptide Fragments
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Polysaccharides
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Receptors, Immunologic
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Receptors, LDL
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Receptors, Lipoprotein
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Receptors, Scavenger
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Scarb1 protein, mouse
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Scavenger Receptors, Class B
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Sulfoglycosphingolipids
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acetyl-LDL
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Collagen
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Dextran Sulfate
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fucoidan
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Lysine