Abstract
The chromosome 2 open reading frame 40 (C2ORF40) gene is a candidate tumor suppressor gene for a variety of tumors. Previous results by the present authors revealed that the C2ORF40 protein is a secreted protein. However, the exact biological function of secreted C2ORF40 protein in carcinogenesis has not been thoroughly investigated. In the present study, the signal peptide sequence of the C2ORF40 cDNA was initially removed to produce secreted recombinant human C2ORF40 protein (rhC2ORF40). Soluble rhC2ORF40 was successfully expressed and purified, which was evaluated for the first time, to the best of our knowledge, for tumor-suppressing function in vivo in esophageal cancer. The present results revealed that soluble purified rhC2ORF40 was concentrated with a purity of >95%. Furthermore, rhC2ORF40 inhibited esophageal cancer cell growth in vivo in a dose-dependent manner compared with a control group (P<0.05). In addition, the present study demonstrated for the first time that rhC2ORF40 decreased telomerase activity using telomeric repeat amplification protocol-enzyme-linked immunosorbent assay (P<0.05), without affecting the expression levels of telomerase-component RNA (P>0.05), as shown with polymerase chain reaction. Overall, the present results demonstrated that soluble rhC2ORF40 inhibited tumor cell growth in vivo by decreasing telomerase activity in esophageal squamous cell carcinoma. Therefore, soluble rhC2ORF40 with a high purity and biological activity may be a potential biological therapy drug for esophageal cancer.