Embelin is a small-molecule inhibitor of X‑linked inhibitor of apoptosis protein (XIAP), and it induces apoptosis in tumor cells via the inhibition of XIAP. The aim of the present study was to investigate the anticancer effect of embelin on human gastric carcinoma cells and the mechanisms underlying this effect. Cell proliferation of SGC7901 human gastric carcinoma cells was measured using MTT assay, following treatment with embelin (5, 10 and 15 µM) on days 1, 3 and 5. Caspase‑3 and nuclear factor (NF)‑κB p65 activation in SGC7901 cells were assessed using commercial kits. Cellular and nuclear apoptosis were analyzed with an Annexin V‑FITC/PI Apoptosis Detection kit and DAPI staining assay, respectively. Phospho (p)‑p38 mitogen‑activated protein kinase (MAPK), p‑inhibitor of NF‑κB (p‑IκBα) and p‑IκB kinase α/β (p‑IKKα/β) protein expression levels were analyzed with western blot assay. In the present study, treatment with embelin decreased cell proliferation, induced caspase‑3 activation and suppressed NF‑κB p65 activation in SGC7901 cells. Furthermore, embelin administration reduced p‑IκBα and p‑IKKα/β protein expression levels. In conclusion, embelin induces cell apoptosis in human gastric carcinoma through activation of p38 MAPK and inhibition of the NF‑κB signaling pathways. It was further suggested that embelin may be used as a potential drug for the treatment of gastric carcinoma.
Rab11-family interacting proteins (Rab11‑FIPs) are associated with the progression of various tumors; however, their expression and clinical significance in colorectal cancer (CRC) remains largely undetermined. In this study, the clinical implications, functions and underlying mechanisms of Rab11‑FIP4 in CRC were investigated. Immunohistochemical analysis revealed that expression of Rab11‑FIP4 was significantly increased in human CRC tissues and correlated with poor prognosis of patients with CRC. Overexpression of Rab11‑FIP4 in the CRC cell line significantly promoted cell proliferation, migration and invasion in vitro and tumor metastasis in vivo. Furthermore, the results of a co‑immunoprecipitation assay and western blot analysis demonstrated that Rab11‑FIP4 interacted with Rab11 and insulin‑like growth factor 1 receptor, and increased the phosphorylation of extracellular signal‑regulated kinase 1/2 and AKT serine/threonine kinase. In addition, hypoxia contributed to the upregulation of Rab11‑FIP4 expression via hypoxia‑inducible factor‑1α activation of the Rab11‑FIP4 promoter. In conclusion, the results of the present study suggest that Rab11‑FIP4 may act as an oncogene in CRC, and may be a potential therapeutic target for the treatment of patients with CRC.
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