[PKC-dependent activation of P44/42 MAPKs and HSP70 in signal transduction pathways during hepatocyte ischemic preconditioning].
OBJECTIVE
To investigate the significance of PKC, P44/42 MAPKs and HSP70 signal transduction in IP.


METHODS
Through an in vivo rat liver IP model, PKC inhibitor, activator and MEK inhibitor were utilized to analyze the phosphorylation of PKC and P44/42 MAPKs. HSP expression, AST/ALT concentration, cellular structure and ultrastructure were also observed. All the data were statistically analyzed.


RESULTS
Compared with the control without IP, the phosphorylation of PKC was significantly increased in IP treated models and PKC activated group (P < 0.01) and P44/42 MAPKs and the expression of HSP were also obviously increased. In contrast, opposite changes were found in PKC or MEK inhibited groups, the phosphorylation PKC was decreased in PKC inhibited group (P < 0.01).


CONCLUSIONS
The model has shown that PKC activation plays a pivotal role in the activation of P44/42 MAPKs pathway that participates in the preservation of liver cells. At the same time, HSP expression is regulated by signals in P44/42 MAPKs pathway.
Gao
Yi
Y
Department of transplantation surgery, Zhujiang Hospital, The first Military Medical University, Guangzhou, 510282, China.
Wang
Yu
Y
Shan
Yu-qiang
YQ
Pan
Ming-xin
MX
D000818:Animals; D004789:Enzyme Activation; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D022781:Hepatocytes; D019194:Ischemic Preconditioning; D008099:Liver / Q000098:blood supply*; D008297:Male; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism; D048052:Mitogen-Activated Protein Kinase 3 / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley
D018840:HSP70 Heat-Shock Proteins; D011493:Protein Kinase C; D019950:Mitogen-Activated Protein Kinase 1; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases