title: CLA-1 is an 85-kD plasma membrane glycoprotein that acts as a high-affinity receptor for both native (HDL, LDL, and VLDL) and modified (OxLDL and AcLDL) lipoproteins.
abstract: Lipoprotein metabolism is regulated by the functional interplay between lipoprotein components and the receptors and enzymes with which they interact. Recent evidence indicates that the structurally related glycoproteins CD36 and SR-BI act as cell surface receptors for some lipoproteins. Thus, CD36 has been reported to bind oxidized LDL (OxLDL) and acetylated LDL (AcLDL), while SR-BI also binds native LDL and HDL. The cDNA of human CLA-1 predicts a protein 509 amino acids long that displays a 30% and an 80% amino acid identity with CD36 and mouse or hamster SR-BI, respectively. In this report, we describe the structural characterization of CLA-1 as an 85-kD plasma membrane protein enriched in N-linked carbohydrates. The expression of CLA-1 on mammalian and insect cells has been used to demonstrate that CLA-1 is a high-affinity specific receptor for the lipoproteins HDL, LDL, VLDL, OxLDL, and AcLDL. Northern blot analysis of the tissue distribution of CLA-1 in humans indicated that its expression is mostly restricted to tissues performing very active cholesterol metabolism (liver and steroidogenic tissues). This finding, in the context of the capability of this receptor to bind to both native and modified lipoproteins, strongly suggests that the CLA-1 receptor contributes to lipid metabolism and atherogenesis.
authors.affiliation: Hospital de la Princesa, Madrid, Spain.
authors.forename: D
authors.initials: D
authors.lastname: Calvo
authors.forename: D
authors.initials: D
authors.lastname: Gómez-Coronado
authors.forename: M A
authors.initials: MA
authors.lastname: Lasunción
authors.forename: M A
authors.initials: MA
authors.lastname: Vega
mesh_terms: D000107:Acetylation; D000818:Animals; D018955:CD36 Antigens / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D002522:Chlorocebus aethiops; D002784:Cholesterol / Q000378:metabolism; D006224:Cricetinae; D018076:DNA, Complementary / Q000235:genetics; D005822:Genetic Vectors / Q000235:genetics; D006031:Glycosylation; D006801:Humans; D008074:Lipoproteins / Q000378:metabolism*; D008075:Lipoproteins, HDL / Q000378:metabolism; D008077:Lipoproteins, LDL / Q000378:metabolism; D008079:Lipoproteins, VLDL / Q000378:metabolism; D008545:Melanoma / Q000473:pathology; D008565:Membrane Proteins; D051379:Mice; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000378:metabolism; D017924:Nucleopolyhedroviruses / Q000235:genetics; D009928:Organ Specificity; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000032:analysis; D011971:Receptors, Immunologic / Q000187:drug effects; D018110:Receptors, Lipoprotein / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D051116:Receptors, Scavenger; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D051122:Scavenger Receptors, Class B; D013045:Species Specificity; D018411:Spodoptera; D014407:Tumor Cells, Cultured
chemical_list: D018955:CD36 Antigens; D018076:DNA, Complementary; D008074:Lipoproteins; D008075:Lipoproteins, HDL; D008077:Lipoproteins, LDL; D008079:Lipoproteins, VLDL; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D011971:Receptors, Immunologic; D018110:Receptors, Lipoprotein; D051116:Receptors, Scavenger; D011993:Recombinant Fusion Proteins; C495124:SCARB1 protein, human; C454739:Scarb1 protein, mouse; D051122:Scavenger Receptors, Class B; C032629:acetyl-LDL; C099252:oxidized low density lipoprotein; D002784:Cholesterol