scholarly journals Up-Regulation of Urotensin II and Its Receptor Contributes to Human Hepatocellular Carcinoma Growth via Activation of the PKC, ERK1/2, and p38 MAPK Signaling Pathways

Molecules ◽  
2014 ◽  
Vol 19 (12) ◽  
pp. 20768-20779 ◽  
Author(s):  
Xiao-Tong Yu ◽  
Peng-Yan Wang ◽  
Zheng-Ming Shi ◽  
Kun Dong ◽  
Ping Feng ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Signaling Pathways ◽  
P38 Mapk ◽  
Mapk Signaling ◽  
Human Hepatocellular Carcinoma ◽  
Urotensin Ii ◽  
Mapk Signaling Pathways

scholarly journals DUSP28 contributes to human hepatocellular carcinoma via regulation of the p38 MAPK signaling

2014 ◽  
Vol 45 (6) ◽  
pp. 2596-2604 ◽  
Author(s):  
DONG WANG ◽  
SHENG HAN ◽  
RUI PENG ◽  
CHENYU JIAO ◽  
XING WANG ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
P38 Mapk ◽  
Mapk Signaling ◽  
Human Hepatocellular Carcinoma

MAPK signaling pathways are needed for survival of H9c2 cardiac myoblasts under extracellular alkalosis

2008 ◽  
Vol 295 (3) ◽  
pp. H1319-H1329 ◽  
Author(s):  
Konstantina Stathopoulou ◽  
Isidoros Beis ◽  
Catherine Gaitanaki
Keyword(s):  
Signaling Pathways ◽  
P38 Mapk ◽  
Cardiac Myocyte ◽  
Consensus Sequence ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Dependent Manner ◽  
Selective Inhibitors ◽  
Cardiac Myoblasts ◽  
Mapk Signaling Pathways

pH is one of the most important physiological parameters, with its changes affecting the function of vital organs like the heart. However, the effects of alkalosis on the regulation of cardiac myocyte function have not been extensively investigated. Therefore, we decided to study whether the mitogen-activated protein kinase (MAPK) signaling pathways [c-Jun NH2-terminal kinases (JNKs), extracellular signal-regulated kinases (ERKs), and p38 MAPK] are activated by alkalosis induced with Tris-Tyrode buffer at two pH values, 8.5 and 9.5, in H9c2 rat cardiac myoblasts. These buffers also induced intracellular alkalinization comparable to that induced by 1 mM NH4Cl. The three MAPKs examined presented differential phosphorylation patterns that depended on the severity and the duration of the stimulus. Inhibition of Na+/H+ exchanger (NHE)1 by its inhibitor HOE-642 prevented alkalinization and partially attenuated the alkalosis (pH 8.5)-induced activation of these kinases. The same stimulus also promoted c-Jun phosphorylation and enhanced the binding at oligonucleotides bearing the activator protein-1 (AP-1) consensus sequence, all in a JNK-dependent manner. Additionally, mitogen- and stress-activated kinase 1 (MSK1) was transiently phosphorylated by alkalosis (pH 8.5), and this was abolished by the selective inhibitors of either p38 MAPK or ERK pathways. JNKs also mediated Bcl-2 phosphorylation in response to incubation with the alkaline medium (pH 8.5), while selective inhibitors of the three MAPKs diminished cell viability under these conditions. All these data suggest that alkalosis activates MAPKs in H9c2 cells and these kinases, in turn, modify proteins that regulate gene transcription and cell survival.

Sign in / Sign up

Export Citation Format

Share Document