PPARs are thus important proteins in OA regulation, which may have significant importance in OA therapeutics.S100 calcium binding protein A16 (S100A16) is the most recent member of the S100 calcium-binding protein family. The function of S100A16 has been associated with various types of cancer; however, its role in colorectal cancer (CRC) remains unknown. Therefore, the aim of the present study was to investigate the role of S100A16 in CRC progression. The Oncomine dataset used in the current study revealed that the expression of S100A16 was decreased in CRC compared with normal colorectal tissues. Similar results were also determined via immunohistochemistry. In addition, a negative association was identified between S100A16 expression and the prognosis of patients with CRC. Further functional experiments revealed that S100A16 knockdown promoted the proliferation, migration and invasion of HCT116 and SW480 cells, and vice versa in Lovo cells. Epithelial-mesenchymal transition (EMT) was promoted and the JNK/p38 MAPK pathway was activated in HCT116 cells following S100A16 knockdown, as determined via western blotting. Furthermore, S100A16 silencing promoted the migration and invasion of cells. EMT was also reversed when cells were treated with the JNK inhibitor (SP600125) or the p38 inhibitor (SB203580). In summary, the results of the present study demonstrated that S100A16 suppressed the proliferation, migration and invasion of CRC cells partially via the JNK/p38 MAPK signalling pathway and subsequent EMT mediation.JNK serves critical roles in numerous types of inflammation‑ and oxidative stress‑induced disease, including acute lung injury (ALI). JNK‑IN‑8 is the first irreversible JNK inhibitor that has been described. However, whether JNK‑IN‑8 can prevent lipopolysaccharide (LPS)‑induced ALI by inhibiting JNK activation and its downstream signaling is poorly understood. The objective of the present study was to investigate the specific therapeutic effects of JNK‑IN‑8 on LPS‑induced ALI and the molecular mechanisms involved. JNK‑IN‑8 attenuated myeloperoxidase activity, malondialdehyde and superoxide dismutase content and the lung wet/dry ratio, and improved the survival rate following lethal injection of LPS. Additionally, JNK‑IN‑8 decreased bronchoalveolar lavage fluid protein levels, lactate dehydrogenase activity, neutrophil infiltration and the number of macrophages (as demonstrated by flow cytometry), as well as the production of TNF‑α, IL‑6 and IL‑1β (as evaluated via ELISA). In addition, reverse transcription‑quantitative PCR and ELISA showed that JNK‑IN‑8 attenuated LPS‑induced inflammatory cytokine production and oxidative stress in primary murine peritoneal macrophages and RAW264.7 cells in vitro. Furthermore, the present study demonstrated that the JNK/NF‑κB signaling pathway was involved in the therapeutic effect of JNK‑IN‑8 against LPS‑induced injury both in vivo and in vitro. In conclusion, these findings indicated that JNK‑IN‑8 had a therapeutic effect on LPS‑induced ALI in mice. The mechanism may be associated with inhibition of the JNK/NF‑κB signaling pathway. JNK‑IN‑8 may be a potential therapeutic agent for the treatment of ALI.Estrogen receptor‑associated receptor α (ERRα) is an orphan nuclear receptor that lacks corresponding ligands. ERRα recruits co‑regulators to regulate gene transcription and plays an important role in human physiological functions. Peroxisome proliferator‑activated receptor γ (PPARγ) is also a nuclear receptor that regulates the expression of target genes via a ligand‑dependent mechanism, thereby participating in a series of physiological processes. Both ERRα and PPARγ are involved in the process of energy metabolism and tumorigenesis. In the present review, a concise overview of the important roles governed by ERRα and PPARγ in metabolism and their association with various disease are provided.Recent studies have reported that aberrant PR domain zinc finger protein 14 (PRDM14) expression is associated with the therapeutic sensitivity of cancer cells to drugs. However, its role in lung adenocarcinoma (LUAD) remains unclear. The present study aimed to determine the functions of knockdown or overexpression of PRDM14 in the chemosensitivity and glycolysis of LUAD cells. PRDM14 expression was analyzed in lung cancer tissues from patients resistant and sensitive to cisplatin (DDP), as well as in LUAD cell lines A549 and DDP‑resistant A549 (A549/DDP) using reverse transcription quantitative‑PCR and western blotting. Additionally, apoptosis was analyzed by flow cytometry, and flow cytometry and biochemical analysis was used to analyze glycolysis, indicated by glucose uptake and lactate release. The results of the present study demonstrated that PRDM14 expression was upregulated in patients with DDP‑resistant LUAD and DDP‑resistant cell lines. Overexpression of PRDM14 suppressed the sensitivity of A549 cells to DDP and silencing of PRDM14 using shRNA targeting PRDM14 promoted the sensitivity of A549/DDP cells to DDP, compared with that in the respective control groups. In mice with xenograft tumors, knockdown of PRDM14 using shRNA targeting PRDM14 inhibited the A549/DDP cell‑derived tumor growth compared with scramble shRNA. The results of the glycolysis assays demonstrated that PRDM14 silencing inhibited glucose uptake, lactate release and glucose transporter 1 expression in A549/DDP cells compared with those in the control cells. PRDM14 overexpression relieved the inhibitory effects of 3‑bromopyruvate, a potent glycolytic inhibitor for glycolysis, on glucose uptake and lactate release in A549 cells compared with those in the control cells. Therefore, the results of the present study suggested that PRDM14 may inhibit the chemosensitivity and promote glycolysis in human LUAD cells.The present study aimed to investigate the expression of ATPase Ca++ transporting plasma membrane 4 (PMCA4) in mouse testis and to determine its role in spermatogenesis. Reverse transcription‑quantitative PCR, western blotting and immunofluorescence were performed to evaluate the expression levels of PMCA4 in mouse testes at various weeks postnatal in wild type mice, and in testes from Sertoli cell‑specific androgen receptor knockout and androgen receptor knockout (ARKO) mice. Luciferase assay, androgen receptor (AR) overexpression and AR antagonist experiments were used to confirm that AR regulated the expression of PMCA4. The results demonstrated that PMCA4 was highly expressed in mouse testes at 3‑8 weeks postnatal. selleck products PMCA4 expression levels in ARKO mouse testes were decreased compared with wild type. In addition, activation of AR by testosterone administration resulted in an increase in the activity of the PMCA4 promoter. Cells transfected with an AR‑overexpressing plasmid exhibited increased expression levels of the PMCA4 protein.