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目的 探讨Activin A对成纤维细胞微丝肌动蛋白的作用以及其信号机制.方法 出生 24 h 内的C57BL/6 乳鼠皮肤成纤维细胞分离培养.实验分为PBS 组、Activin A组以及JNK特异性抑制剂SP600125 组、ERK特异性抑制剂SL327 组、p38 特异性抑制剂SB202190 组.3～5 代成纤维细胞,提取细胞总蛋白,Western blot 检测JNK、ERK、p38 的磷酸化活性并且通过Phallotoxins 染色观察成纤维细胞肌动蛋白变化.结果 Activin A 可诱导成纤维细胞肌动蛋白聚集,给予JNK 特异性抑制剂SP600125后,成纤维细胞肌动蛋白聚集现象完全被抑制;给予ERK 特异性抑制剂SL327 后,成纤维细胞肌动蛋白聚集现象减弱,但是尚未完全被抑制;而p38 特异性抑制剂SB202190 处理后,成纤维细胞肌动蛋白聚集未被抑制.结论 Activin A通过JNK 和ERK 信号通路诱导成纤维细胞肌动蛋白重组聚集.“,”Objective To explore whether Activin A regulate the filamentous actin of fibroblasts via MAPK signaling pathway. Methods Fibroblasts were Isolated and cultured from C57BL/6 rat skin which was born within 24 hours. The experiments were divided into PBS group, Activin A group, JNK specific inhibitor SP600125 group, ERK specific inhibitor SL327 group and p38 specific inhibitor SB202190 group. When cells were passaged for 3～5 generations, the total protein of cells was extracted, and the phosphorylation activity of JNK, ERK and p38 was detected by western blot. The changes of F-actin were observed by Phallotoxins staining. Results Activin A could induce the accumulation of F-actin in fibroblasts. After the use of JNK specific inhibitor SP600125, the F-actin aggregation of fibroblasts was completely inhibited. When the ERK specific inhibitor SL327 was used, the fibroblast F-actin aggregation was weakened, but not yet completely inhibited while P38 specific inhibitor SB202190 did not suppress the fibroblast F-actin aggregation. Conclusion Activin A can induce the F-actin recombination of fibroblasts via JNK and ERK signaling pathway.