Deoxynivalenol Impairs Porcine Intestinal Barrier Function and Decreases the Protein Expression of Claudin-4 through a Mitogen-Activated Protein Kinase-Dependent Mechanism

Platyphyllenone is a type of diarylheptanoid that exhibits anti-inflammatory and chemoprotective effects. However, its effect on oral cancer remains unclear. In this study, we investigated whether platyphyllenone can promote apoptosis and autophagy in SCC-9 and SCC-47 cells. We found that it dose-dependently promoted the cleavage of PARP; caspase-3, -8, and -9 protein expression; and also led to cell cycle arrest at the G2/M phase. Platyphyllenone up-regulated LC3-II and p62 protein expression in both SCC-9 and SCC-47 cell lines, implying that it can induce autophagy. Furthermore, the results demonstrated that platyphyllenone significantly decreased p-AKT and increased p-JNK1/2 mitogen-activated protein kinase (MAPK) signaling pathway in a dose-dependent manner. The specific inhibitors of p-JNK1/2 also reduced platyphyllenone-induced cleavage of PARP, caspase-3, and caspase -8, LC3-II and p62 protein expression. These findings are the first to demonstrate that platyphyllenone can induce both autophagy and apoptosis in oral cancers, and it is expected to provide a therapeutic option as a chemopreventive agent against oral cancer proliferation.

Download Full-text

Activation of signaling pathways and regulatory mechanisms of mRNA translation following myocardial ischemia-reperfusion

Journal of Applied Physiology ◽

10.1152/japplphysiol.01122.2005 ◽

2006 ◽

Vol 101 (2) ◽

pp. 576-582 ◽

Cited By ~ 14

Author(s):

Stephen J. Crozier ◽

Xueqian Zhang ◽

Jufang Wang ◽

Joseph Cheung ◽

Scot R. Kimball ◽

...

Keyword(s):

Protein Kinase ◽

Myocardial Ischemia ◽

Protein Expression ◽

Signaling Pathways ◽

Mrna Translation ◽

Mitogen Activated Protein Kinase ◽

Regulatory Mechanisms ◽

Ischemia And Reperfusion ◽

Myocardial Ischemia And Reperfusion ◽

Mitogen Activated Protein

Protein expression in the heart is altered following periods of myocardial ischemia. The changes in protein expression are associated with increased cell size that can be maladaptive. There is little information regarding the regulation of protein expression through the process of mRNA translation during ischemia and reperfusion in the heart. Therefore, the purpose of this study was to identify changes in signaling pathways and downstream regulatory mechanisms of mRNA translation in an in vivo model of myocardial ischemia and reperfusion. Hearts were collected from rats whose left main coronary arteries had either been occluded for 25 min or reversibly occluded for 25 min and subsequently reperfused for 15 min. Following reperfusion, both the phosphoinositide 3-kinase and mitogen-activated protein kinase pathways were activated, as evidenced by increased phosphorylation of Akt (PKB), extracellular signal-regulated kinase 1/2, and p38 mitogen-activated protein kinase. Activation of Akt stimulated signaling through the protein kinase mammalian target of rapamycin, as evidenced by increased phosphorylation of two of its effectors, the ribosomal protein S6 kinase and the eukaryotic initiation factor eIF4E binding protein 1. Ischemia and reperfusion also resulted in increased phosphorylation of eIF2 and eIF2B. These changes in protein phosphorylation suggest that control of mRNA translation following ischemia and reperfusion is modulated through a number of signaling pathways and regulatory mechanisms.

Download Full-text

Interleukin 17A Promotes Pneumococcal Clearance by Recruiting Neutrophils and Inducing Apoptosis through a p38 Mitogen-Activated Protein Kinase-Dependent Mechanism in Acute Otitis Media

Infection and Immunity ◽

10.1128/iai.00006-14 ◽

2014 ◽

Vol 82 (6) ◽

pp. 2368-2377 ◽

Cited By ~ 25

Author(s):

W. Wang ◽

A. Zhou ◽

X. Zhang ◽

Y. Xiang ◽

Y. Huang ◽

...

Keyword(s):

Protein Kinase ◽

Otitis Media ◽

Acute Otitis Media ◽

Mitogen Activated Protein Kinase ◽

Interleukin 17A ◽

Mitogen Activated Protein ◽

Dependent Mechanism

Download Full-text

P38 MAPK Pharmacological Inhibitor SB203580 Alleviates Total Parenteral Nutrition-Induced Loss of Intestinal Barrier Function but Promotes Hepatocyte Lipoapoptosis

Cellular Physiology and Biochemistry ◽

10.1159/000457933 ◽

2017 ◽

Vol 41 (2) ◽

pp. 623-634 ◽

Cited By ~ 9

Author(s):

Yong-Tao Xiao ◽

Wei-Hui Yan ◽

Yi Cao ◽

Jun-Kai Yan ◽

Wei Cai

Keyword(s):

Parenteral Nutrition ◽

Palmitic Acid ◽

Total Parenteral Nutrition ◽

P38 Mapk ◽

Barrier Function ◽

Intestinal Barrier ◽

Mitogen Activated Protein Kinase ◽

Intestinal Barrier Function ◽

P38 Mapk Inhibitor ◽

Mapk Inhibitor

Background & Aims: Our previous studies have provided evidence that p38 mitogen-activated protein kinase (MAPK) is involved in total parenteral nutrition (TPN)-associated complications, but its exact effects and mechanisms have not been fully understood. This study aimed to evaluate the roles of p38 MAPK inhibitor SB203580 in the TPN-induced loss of intestinal barrier function and liver disease. Methods: A rodent model of TPN was used to analyze the roles of SB203580 in TPN-associated complications.Intestinal barrier function was evaluated by transepithelial electrical resistance (TER) and paracellular permeability in Caco-2 cells. The palmitic acid (PA) was used to induce hepatic lipoapoptosis in vitro. The lipoapoptosis was detected using Caspase-3/7 and lipid staining. Results: In the present study, we showed that SB203580 treatment significantly suppressed TPN-mediated intestinal permeability in rats. SB203580 treatment significantly inhibited IL-1β-induced an increase in tight junction permeability of Caco-2 cells via repressing the p38/ATF-2 signaling. Unexpectedly, SB203580 treatment enhanced hepatic lipoapoptosis in the model of TPN. Palmitic acid (PA)-induced hepatic lipoapoptosis in human liver cells was significantly augmented by the SB203580 treatment. Conclusions: We demonstrate that the p38 MAPK inhibitor SB203508 ameliorates intestinal barrier function but promotes hepatic lipoapoptosis in model of TPN.

Download Full-text