Woo H J, Shaw L M, Messier J M, Mercurio A M
Laboratory of Cancer Biology, New England Deaconess Hospital, Boston, Massachusetts 02115.
J Biol Chem. 1990 May 5;265(13):7097-9.
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.
目前的数据表明，细胞与层粘连蛋白（主要的基底膜糖蛋白）的黏附是由特定的整合素介导的，整合素是一类黏附受体。此外，大多数细胞类型都表达一系列高亲和力的非整合素层粘连蛋白结合蛋白（LBP）。尽管付出了巨大努力，但这些LBP的功能尚未阐明。我们在此报告，小鼠巨噬细胞的主要非整合素LBP的分子量为35000，且在细胞表面表达。蛋白质微序列分析数据显示，该蛋白与碳水化合物结合蛋白35相同。这种小鼠半乳糖特异性凝集素就是巨噬细胞抗原Mac-2。因此，这些数据表明，非整合素LBP可能通过涉及蛋白质-碳水化合物相互作用的机制促进与层粘连蛋白的黏附。
