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目的：研究粘附分子整合素的细胞内信号传导途径之一——酪氨酸磷酸化在成纤维细胞表达原胶原基因中的作用。方法：利用抗整合素单抗及相应二抗的交联作用，模拟整合素在成纤维细胞表面簇集而诱导酪氨酸磷酸化，用蛋白印迹和ＲＴ－ＰＣＲ技术分别检测诱导生成的酪氨酸磷酸化蛋白和Ⅰ型原胶原ｍＲＮＡ水平；并观察阻断酪氨酸磷酸化后，酪氨酸磷酸化蛋白和Ⅰ型原胶原ｍＲＮＡ的变化。结果：整合素β１亚基在成纤维细胞表面簇集可诱导相对分子质量分别为９８０００和６５０００的酪氨酸磷酸化蛋白，且Ⅰ型原胶原ｍＲＮＡ的表达显著增加（Ｐ＜０．０１）；阻断酪氨酸磷酸化，不仅酪氨酸磷酸化蛋白显著减少（Ｐ＜０．０１），而且Ⅰ型原胶原ｍＲＮＡ的表达也降低（Ｐ＜０．０５）。结论：整合素β１亚基在成纤维细胞表面簇集诱导的酪氨酸磷酸化蛋白在Ⅰ型原胶原基因表达中具有重要作用。
AIM: To investigate the role of tyrosine phosphorylation, one of the intracellular signaling pathways of adhesion molecule integrin, in the expression of procollagen in fibroblasts. Methods: By using anti-integrin monoclonal antibody and its corresponding secondary antibody, the integrin was induced to cluster in the surface of fibroblasts to induce tyrosine phosphorylation. Western blotting and RT-PCR were used to detect tyrosine Acid phosphatase and type Ⅰ procollagen mRNA levels were observed. The changes of tyrosine phosphorylated protein and type Ⅰ procollagen mRNA were observed after tyrosine phosphorylation was blocked. Results: The integrin β1 subunit clustered on the surface of fibroblasts induced a tyrosine phosphorylated protein with relative molecular mass of 98000 and 65000 respectively, and the expression of type Ⅰ procollagen mRNA was significantly increased (P <0.01). Blocking tyrosine phosphorylation not only significantly reduced tyrosine phosphorylated protein (P <0.01), but also decreased the expression of type Ⅰ procollagen mRNA (P <0.05). CONCLUSION: The integrin β1 subunit has an important role in the type Ⅰ procollagen gene expression induced by cluster-induced tyrosine phosphorylation on the surface of fibroblasts.