Stanniocalcin 2 (STC2), a secretory glycoprotein hormone, regulates many biological processes including cell proliferation, apoptosis, tumorigenesis and atherosclerosis. However, the effect of STC2 on proliferation, migration and epithelial-mesenchymal transition (EMT) progression in human colorectal cancer (CRC) cells remains poorly understood. The expression level of STC2 was determined by quantitative real-time polymerase chain reaction (qPCR) and western blot analysis. Cell Counting Kit-8 (CCK-8) was used to detect the viability of SW480 cells. The invasion and migration of cells were identified by wound healing and Transwell assays. The mRNA and protein expression levels of β-catenin, matrix metalloproteinase (MMP)-2, MMP-9, E-cadherin and vimentin were assessed by qPCR and western blot analysis. In the present study, it was demonstrated that STC2 was highly expressed in the CRC cell lines. After silencing of STC2 , the cell viability, migration and invasion were significantly reduced. Silencing of STC2 in the CRC Sw480 cells increased the expression of E-cadherin and decreased the expression of vimentin, MMP-2 and MMP-9, compared to those in the normal and empty vector group. Furthermore, the expression of β-catenin in the STC2 gene silenced group was suppressed, and the expression of β-catenin was reversed by Wnt activator, SB216763. These results demonstrated that STC2 participates in the development and progression of CRC by promoting CRC cell proliferation, survival and migration and activating the Wnt/β-catenin signaling pathway.

Kallikrein-related peptidase 12 (KLK12) is overexpressed in cancer tissues including gastric, breast and prostate cancer. However, the role of KLK12 in colorectal cancer is not fully understood. In the present study, the level of KLK12 was determined by performing reverse transcription-polymerase chain reaction (RT-qPcR) in colorectal cancer tissues and cell lines. Lipofectamine ® 2000 was used to transfect HT-29 cells to overexpress and knockdown KLK12. cell viability, migration, invasion and apoptosis were detected by MTT, wound healing, Transwell and flow cytometry assays, respectively. The mRNA and protein expression levels of EMT-associated proteins, apoptosis-associated proteins, phosphorylated adenosine monophosphate-activated protein kinase (p-AMPK) and phosphorylated mammalian target of rapamycin (p-mTOR) were determined by RT-qPcR and western blot analysis. It was identified that the KLK12 mRNA levels were increased significantly in colorectal cancer tissues and cell lines. KLK12 small interfering RNA inhibited cell viability, migration and invasion. Furthermore, epithelial-mesenchymal transition (EMT)-associated proteins were altered by siKLK12. cell apoptosis was induced by KLK12 downregulation, which was demonstrated by the changes in apoptosis-associated proteins; however, KLK12 overexpression produced the opposite effect. SiKLK12 enhanced the expression of p-AMPK and suppressed the expression of p-mTOR, while KLK12 overexpression had the opposite effect. Promotion of KLK12 overexpression-induced cell viability was reversed by 5-aminoimidazole-4-carboxamide ribonucleotide, an activator of the AMPK signaling pathway, and rapamycin, a specific inhibitor of the mTOR signaling pathway. Taken together, the results of the present study indicated that KLK12 was overexpressed in colorectal cancer and may regulate cell behavior, potentially via the AMPK and mTOR pathways.