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HLJ1 is a novel caspase-3 substrate and its expression enhances UV-induced apoptosis in non-small cell lung carcinoma
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Lung cancer is the most common cause of cancer deaths in the world. Cancer is often caused by gene alterations including genetic mutations, aberration of epigenetic regulation and gene expression. Tumorigenesis is determined by the balance of cell proliferation and death rates. HLJ1, a member of the DnaJ-like Hsp40 family, is a newly identified tumor suppressor protein whose expression is highly associated with relapse and survival in non-small cell lung cancer (NSCLC) patients. However, the role of HLJ1 in apoptosis is still unknown. Recently, it has been demonstrated that heat shock proteins (HSPs) can regulate apoptosis. In this study, NSCLC cell lines with the varying HLJ1 expression levels were subjected to UV irradiation, followed by flow cytometry analysis. Interestingly, cell apoptosis in these cell lines were positively correlated with HLJ1 expression. To understand the role of HLJ1 during cell apoptosis, a human lung adenocarcinoma cell line with enforced expression of HLJ1 was established and exposed to UV irradiation. The enforcing expression of HLJ1 in low HLJ1-expressing cells promoted UV-induced apoptosis through enhancing JNK and caspase-3 activation. Additionally, UV irradiation led to the decrease of HLJ1 predominantly in apoptotic cells. The pan-caspase inhibitor, zVAD-fmk, and caspase-3-specific inhibitor, DEVD-fmk, prevented UV-induced degradation of HLJ1 by the late stage of apoptosis. Furthermore, we found a non-typical caspase-3 cleavage site (MEID) at amino acid 125-128 of HLJ1. Cleavage of HLJ1 led to more apoptosis and inhibited cancer cell anchorage independent growth. Moreover, the caspase-resistant mutant HLJ1 inhibited apoptosis and promoted tumor growth as compared to wild-type HLJ1. Take together, our results suggest that HLJ1 is a novel substrate of caspase-3 and the expression of HLJ1 is positively correlated with apoptosis.
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