Mohammed_2019_Oncol.Rep_41_973

Lysophospholipase1 (LYPLA1) also known as acylprotein thioesterase1 (APT1) belongs to the superfamily of alpha/beta hydrolase. It has been found to have the properties of a homodimer by manifesting depalmitoylation as well as lysophospholipase activity. LYPLAs are under the control of both microRNAs, miR138 and miR424. They were observed to be significantly overexpressed in chronic lymphocytic leukemia cells. To date, LYPLAs are the sole enzymes recognized to activate depalmitoylation. In this study, we provide the expression pattern of LYPLA1 in nonsmall cell lung cancer (NSCLC) using four different NSCLC cell lines. Western blot analysis and RTPCR were performed to detect the protein expression and mRNA expression of LYPLA1 in NSCLC cell lines. We detected the highest LYPLA1 protein expression level in SPCA1 cells followed by A549 cells, and the highest LYPLA1 mRNA expression level was detected in the SPCA1 cells followed by the H1299 cell line. We found that suppression of LYPLA1 expression using smallinterfering RNA significantly inhibited proliferation, migration and invasion of the LYPLA1transfected NSCLC cells. Furthermore, we explored the involvement of LYPLA1 in the regulation of epithelialmesenchymal transition (EMT). The epithelial marker Ecadherin was significantly increased, while mesenchymal markers Ncadherin, vimentin and SNAIL were markedly decreased in the LYPLA1silenced cells. Collectively the results of the present study suggest that the LYPLA1 gene plays a tumorpromotor role in NSCLC cells in vitro.