Peroxiredoxin1 promotes cell proliferation, migration and invasion of colorectal cancer via p38MAPK signaling.

Abstract

Peroxiredoxin1 (PRDX1), a class of thiol peroxidases, is a multifunctional protein. We aimed at analyzing the effect of PRDX1 on proliferation, apoptosis, migration and invasion of colorectal cancer and to investigate the potential mechanism. Western blot and PCR were used to validate the silencing efficiency in SW480 cell by transfection of PRDX1-siRNA. The cell proliferation was detected by Cell Counting Kit-8 (CCK-8) test. Flow cytometry Annexin V/PI double staining was used to analyze cell apoptosis. Transwell and scratch test were used to detect the migration and invasion of cells. Signal pathway protein expression was analyzed by Western blot. The expression of PRDX1 in SW480 cells could be reduced by siRNA effectively. The cell proliferation, migration and invasion were reduced significantly compared with control group after down-regulation of PRDX1 (p<0.05), while the cell apoptosis was enhanced significantly (p<0.05). The ratio of phospho-p38 mitogen-activated protein kinases (p-p38) /p38 mitogen-activated protein kinases (p38) was down-regulated after the down-regulation of PRDX1 (p<0.05). The ratio of phospho-c-Jun N-terminal protein kinase (p-JNK)/c-Jun N-terminal protein kinase (JNK) and phospho-extracellular regulated protein kinases (p-ERK)/extracellular regulated protein kinases (ERK) showed changes with no significant difference (p>0.05). Down-regulation of PRDX1 in colorectal cancer SW480 cells could inhibit the cell proliferation, migration, invasion, and induce cell apoptosis. This is very likely to be achieved by activating the p38MAPK-signaling pathway.