Huard T K, Malinoff H L, Wicha M S
Am J Pathol. 1986 May;123(2):365-70.
Laminin, a noncollagenous extracellular matrix glycoprotein, can serve as an attachment factor for epithelial and endothelial cells to basement membrane collagen. The authors have observed that inflammatory macrophages have the capacity to bind exogenous laminin in a time-, temperature- and dose-dependent manner. The laminin binds to these cells via a specific plasma membrane receptor which is detectable on several macrophage subpopulations as well as isolated macrophage membranes. The isolated receptor is a trypsin-sensitive protein with an apparent molecular weight of 70,000 which binds laminin with relatively high affinity, Kd approximately equal to 4 X 10(-9) M. The inflammatory macrophages attach preferentially to a substrate of laminin compared to Type I or Type IV collagen. Thus, the authors postulate that during tissue inflammation macrophages utilize the laminin receptor to bind to vascular basement membranes.
层粘连蛋白是一种非胶原细胞外基质糖蛋白,可作为上皮细胞和内皮细胞与基底膜胶原蛋白的附着因子。作者观察到,炎性巨噬细胞有能力以时间、温度和剂量依赖的方式结合外源性层粘连蛋白。层粘连蛋白通过一种特定的质膜受体与这些细胞结合,该受体在几个巨噬细胞亚群以及分离的巨噬细胞膜上均可检测到。分离出的受体是一种对胰蛋白酶敏感的蛋白质,表观分子量为70,000,它以相对较高的亲和力结合层粘连蛋白,解离常数(Kd)约等于4×10⁻⁹ M。与I型或IV型胶原蛋白相比,炎性巨噬细胞优先附着于层粘连蛋白底物。因此,作者推测在组织炎症期间,巨噬细胞利用层粘连蛋白受体与血管基底膜结合。