CHARACTERIZATION OF THE ELASTIN/LAMININ RECEPTOR

细胞表面的特殊分子起到中介作用 从细胞外到细胞内的信息传递 车厢。这些分子大多是结合在一起的受体。 可溶刺激，如激素和生长因子，而其他 与组件相互作用的分子是固定在另一个 细胞或细胞外基质，并起到细胞中介作用 黏附或细胞运动。加在一起，这些不同类型的 相互作用对许多流程的增长、开发和 损伤的修复。因此，受体的识别 参与细胞-细胞和细胞-基质相互作用已成为一种 细胞生物学的重要目标。 我们最近的研究主要集中在识别和 结合两种弹性蛋白的细胞表面受体的特性 和层粘连蛋白，并在基质组装和细胞中发挥作用 迁移。弹性蛋白产生细胞上的这种受体是一种复合体 三种蛋白质：两个61和55 kDa的跨膜亚基 通过与细胞骨架相互作用的细胞质结构域(S)， 和一个结合67 kDa亚基的胞外区。67岁的 KDA组分包含一个蛋白质结合部位，可以识别 半乳糖苷糖，以及结合一个或两个的细胞结合部位 跨膜亚单位的比例。 这项提案的总体目标是更好地描述 这种受体的结构和功能。具体目标 是纯化和鉴定受体亚基，并 确定受体复合体在基质中的作用 集合。我们还希望确定 受体在调节细胞表型中的作用。进一步的目标将是 为了更好地定义层粘连蛋白和弹性蛋白中的氨基酸序列 由受体识别，并确定细胞内的变化如何 氨基酸序列改变了受体与配体的结合。最后，我们 计划开发弹性蛋白/层粘连蛋白受体的分子克隆 复合体及其基因。

Specialized molecules on the surface of cells serve to mediate information transfer from the extracellular to the intracellular compartments. Most of these molecules are receptors that bind soluble stimuli such as hormones and growth factors, whereas others are molecules that interact with components fixed either to other cells or to extracellular matricides and serve to mediate cell adhesion or cell movement. Together, these various types of interactions are critical to many processes growth, development and repair of injury. Therefore, the identification of receptors involved in cell-cell and cell-matrix interactions has become an important goal of cell biology. Our recent studies have focused on the identification and characterization of a cell surface receptor that binds both elastin and laminin, and plays a role in matrix assembly and cell migration. This receptor on elastin-producing cells is a complex of three proteins: two transmembrane subunits of 61 and 55 kDa with a cytoplasmic domain(s) that interacts with the cytoskeleton, and an extracellular domain that binds a 67 kDa subunit. The 67 kDa component contains a protein binding site that recognizes galactoside sugars, and a cell binding site that binds one or both of the transmembrane subunits. The overall objective of this proposal is to characterize better the structure and function of this receptor. The specific aims are to purify and characterize the receptor subunits and to ascertain the role played by the receptor complex in matrix assembly. We also wish to identify possible functions of the receptor in regulating cellular phenotypes. A further aim will be to better define the amino acid sequences in laminin and elastin recognized by the receptor, and determine how alterations in the amino acid sequences alter receptor-ligand binding. Finally, we plan to develop molecular clones of the elastin/laminin receptor complex and its genes.