Baicalein retards proliferation and collagen deposition by activating p38MAPK-JNK via microRNA-29.

Immoderate proliferation and deposition of collagen generally result in hypertrophic scars and even keloids. microRNA-29 (miR-29) has been proved as a crucial regulator in these pathological processes. Although mounting evidence have proved baicalein (BAI) impairs scar formation, it is still incompletely understood whether miR-29 participated in the underlying mechanism. In the present study, NIH-3T3 cells were stimulated with BAI, and then cell viability was analyzed by cell counting kit-8 (CCK-8) and Western blot. We further analyzed total soluble collagen, collagen 1, and alpha-smooth muscle actin (α-SMA) in NIH-3T3 cells, which were exposed to transforming growth factor beta 1 (TGF-β1)/BAI, using a Sircol assay kit, quantitative reverse transcription-PCR (qRT-PCR) and Western blot, respectively. Besides, the miR-29 inhibitor was transduced and its transfection efficiency was verified by qRT-PCR. Finally, the phosphorylated p38 mitogen-activated protein kinase (p38MAPK) and c-Jun N-terminal kinase (JNK) were examined by Western blot. BAI effectively retarded NIH-3T3 proliferation in a dose-dependent manner. Besides, TGF-β1-induced deposition of total soluble collagen and synthesis of collagen 1 and α-SMA were repressed by BAI at mRNA and protein levels. However, miR-29 inhibitor reversed the effects of BAI. Remarkably, BAI promoted phosphorylated expression of p38MAPK and JNK while miR-29 inhibitor reversed its effects on the phosphorylated expression of p38MAPK and JNK. BAI effectively weakened the cell viability and repressed TGF-β1-induced total soluble collagen as well as collagen 1 and α-SMA by upregulating miR-29. Mechanically, BAI activates the p38MAPK/JNK pathway by promoting miR-29.