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目的探讨胰腺癌中泛素-蛋白酶体途径对凝溶胶蛋白(gelsolin)的降解作用。方法用特异性蛋白酶体抑制剂lactacystin处理胰腺癌细胞系BxPC-3和PANC-1,经Western blot检测凝溶胶蛋白的表达,免疫沉淀细胞内凝溶胶蛋白,分析沉淀蛋白的泛素化。结果BxPC-3细胞系经lactacystin作用12h后,细胞内凝溶胶蛋白含量较对照组和处理前明显升高(P<0.05),而且细胞内的凝溶胶蛋白表现出与泛素分子的相互作用。结论泛素-蛋白酶体途径对凝溶胶蛋白的降解作用,可能是胰腺癌中凝溶胶蛋白表达降低的原因之一。
Objective To investigate the degradation of gelsolin by ubiquitin-proteasome pathway in pancreatic cancer. Methods The pancreatic cancer cell lines BxPC-3 and PANC-1 were treated with a specific proteasome inhibitor lactacystin. The expression of gelsolin was detected by Western blot. The gelsolin was immunoprecipitated and the ubiquitination of precipitated protein was analyzed. Results After treated with lactacystin for 12 hours, the content of gelsolin in BxPC-3 cells was significantly increased (P <0.05) compared with the control group and before treatment, and the intracellular gelsolin showed an interaction with ubiquitin molecules. Conclusion The degradation of gelsolin by the ubiquitin-proteasome pathway may be one of the reasons for the decrease of gelsolin expression in pancreatic cancer.