The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2)
Department of Cancer Biology
Amino Acid Sequence; Animals; Antigens, Differentiation; Basement Membrane; Carbohydrates; Chromatography, Affinity; Chromatography, High Pressure Liquid; Female; Galectin 3; Laminin; Macrophages; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Molecular Sequence Data; Molecular Weight; Sequence Homology, Nucleic Acid
Current data indicate that cell adhesion to laminin, the major basement membrane glycoprotein, is mediated by specific integrins, a family of adhesion receptors. In addition, most cell types express a complement of high affinity non-integrin laminin binding proteins (LBPs). Despite considerable effort, the function of these LBPs has not been elucidated. We report here that the major non-integrin LBP of murine macrophages exhibits an Mr of 35,000 and is expressed on the cell surface. Protein microsequencing data revealed that this protein is identical to carbohydrate binding protein 35. This murine galactose-specific lectin is the macrophage antigen Mac-2. Thus, these data suggest that the non-integrin LBPs may contribute to laminin adhesion by a mechanism involving protein-carbohydrate interactions.
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Citation: J Biol Chem. 1990 May 5;265(13):7097-9.
Woo, Hee-Jong; Shaw, Leslie M.; Messier, Jeanne M.; and Mercurio, Arthur M., "The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2)" (1990). Cancer Biology Publications and Presentations. 116.