Identification of receptors for laminin

层粘连蛋白受体的鉴定

• 批准号: 11670817
• 负责人: UTANI Atsushi
• 金额: $ 1.92万
• 依托单位: Chiba University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 1999
• 资助国家: 日本
• 起止时间: 1999 至 2000
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-11670817/
• 关键词: laminin; integrins; syndecans; インテグリン; 基底膜; 受容体; 細胞外基質

The laminin-5 is localized at skin basement membrane and supports structural stability of epidermo-dermal linkage and regulates various cellular functions. Here we analyze the heparin binding and cell adhesion activities in α3 chain carboxyl terminal globular domain (LG1〜LG5 domain) utilizing recombinant proteins made in mammalian cells as well as synthetic peptides. Immortalized human keratinocyte line HaCat cells and human dermal fibroblasts bound to LG4 domain specifically and in a dose-dependent manner. By inhibition studies, cell binding to the #75' within LG4 was mediated by cell surface heparan sulfate proteoglycan. Solid-phase assays demonstrated that syndecan-2 interacted with the #75'. Cloned 293T cells expressing syndecan specifically attached to #75' as well as to LG4. These data indicate that syndecan mediate cell adhesion to the laminin α3 LG4 domain.

层粘连蛋白-5定位于皮肤基底膜，支持表皮-真皮连接的结构稳定性并调节各种细胞功能。在这里，我们分析了肝素结合和细胞粘附活性的α3链羧基末端球状结构域（LG 1和LG 5结构域）利用重组蛋白在哺乳动物细胞以及合成肽。永生化的人角质形成细胞系HaCat细胞和人真皮成纤维细胞特异性地且以剂量依赖性方式与LG 4结构域结合。通过抑制研究，细胞与LG 4内的#75'的结合由细胞表面硫酸乙酰肝素蛋白聚糖介导。固相分析证明syndecan-2与#75 '相互作用。表达特异性连接至#75'以及LG 4的多配体蛋白聚糖的克隆的293 T细胞。这些数据表明，多配体蛋白聚糖介导细胞粘附层粘连蛋白α3 LG 4结构域。