High expression of PDLIM5 facilitates cell tumorigenesis and migration by maintaining AMPK activation in prostate cancer

// Xi Liu 1, 3, * , Lu Chen 1, * , Hai Huang 1, 3, * , Jian-Min Lv 1, * , Ming Chen 3 , Fa-Jun Qu 2 , Xiu-Wu Pan 2 , Lin Li 2 , Lei Yin 3 , Xin-Gang Cui 2 , Yi Gao 1 and Dan-Feng Xu 1 1 Department of Urinary Surgery, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai 200025, China 2 Department of Urinary Surgery, Third Affiliated Hospital, Second Military Medical University, Shanghai 201805, China 3 Department of Urinary Surgery, Changzheng Hospital, Second Military Medical University, Shanghai 200003, China * These authors have contributed equally to this work Correspondence to: Xin-Gang Cui, email: xingangcui@126.com Yi Gao, email: gaoyismmu@163.com Dan-Feng Xu, email: danfengxu_urology@163.com Keywords: PDLIM5, epithelial-mesenchymal transition, prostate cancer, migration, AMPK Received: July 13, 2017     Accepted: August 27, 2017     Published: September 18, 2017 ABSTRACT PDZ and LIM domain 5 (PDLIM5) is a cytoskeleton-associated protein and has been shown to bind to a variety of proteins through its specific domain, thereby acting to regulate cell migration and tumor progression. Here, we found that PDLIM5 was abnormally upregulated in prostate cancer (PCa) tissues as compared with that in normal prostate tissue. ONCOMINE microarray data mining showed that PDLIM5 was closely correlated with the prognosis of PCa in terms of Gleason score, tumor metastasis and biochemical recurrence. Lentivirus-mediated short hairpin RNA (shRNA) knockdown of PDLIM5 inhibited cell proliferation and colony formation, arrested hormone independent PCa cells DU145 and PC-3 in G2/M phase, and induced apoptosis. Meanwhile, silencing PDLIM5 inhibited migration and invasion of tumor cells by reversing the mesenchymal phenotype and a similar result was confirmed in a xenograft nude mouse model. Finally, we found PDLIM5 plays a crucial role in regulating malignant tumor cell proliferation, invasion and migration by binding to AMPK and affecting its activation and degradation, and may therefore prove to be a potential oncogenic gene in the development and progression of PCa.