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신장 허혈 재관류 손상에 미치는 Ethyl Pyruvate의 효과
정구용(Ku-Yong Chung),정규영(Gyu Young Jeong),안형준(Hyung Joon Ahn),주만기(Man Ki Ju),장혜경(Hye Kyung Chang),이우정(Woo Jung Lee),한평림(Pyung-Lim Han),김유선(Yu Seun Kim) 대한외과학회 2007 Annals of Surgical Treatment and Research(ASRT) Vol.72 No.5
Purpose: Reactive oxygen species (ROS) significantly contribute to ischemia-reperfusion injury, and are also associated with the gradual loss of renal function and renal failure following renal transplantation. Pyruvate is an endogenous antioxidant, but its use as a therapeutic agent for treating conditions mediated by oxidative stress is limited due to its poor stability in solution. However, ethyl pyruvate (EP), a soluble pyruvate derivative, has far greater stability than pyruvate; thus, may serve as a practical pyruvate precursor. Therefore, the ability of EP in the prevention of renal ischemia- reperfusion injury was assessed. Methods: Sprague-Dawley rats (n=54) were subjected to 40 minutes of renal warm ischemia. The animals were divided into three groups: the sham group without warm ischemia (n=18), the EP group (n=18, EP given before ischemia), and the ischemic control (n=18). The serum levels of creatinine and TNF-α were measured 1, 3 and 5 days after induction of ischemia. The expression of high mobility group box-1 (HMGB-1), a delayed inflammatory mediator, was also assessed by Western blot of renal specimens. Results: In the EP group, late improvements in the serum levels of creatinine and TNF-α were observed in comparison with the ischemic control. Based on this delayed effect, the expression of HMGB-1 was assessed in renal tissue. The HMGB-1 expression increased over time during the ischemia process, but EP suppressed this expression 3 and 5 days after renal ischemia-reperfusion injury. Conclusion: These results have demonstrated, for the first time, that EP ameliorates renal ischemia-reperfusion injury. EP attenuates the renal ischemia-reperfusion injury, at least in part, by suppressing the expression of HMGB-1, a late mediator of delayed inflammation.
이자효소 분비에 관여하는 세포 내 조절 단백에 대한 연구
정구용(Ku Yong Chung),최재원(Jae Won Choi),최홍순(Hong Soon Choi),김경환(Kyung Hwan Kim) 대한약리학회 1996 대한약리학잡지 Vol.32 No.2
CCK and cholinergic agonist stimulate enzyme release from the pancreatic acini via G-protein-mediated activation of phospholipase C, In contrast secretin and related peptides increase the level of cAMP and activate cAMP-dependent protein kinase. Camostat, a synthetic protease inhibitor, causes pancreatic hypertrophy and hyperplasia by increasing the CCK release. In this study, the secretagogue-induced changes of intracellular proteins were examined in the dispersed pancreatic acini of rats with or without camostat treatment. Camostat(FOY-305, 200 mg/kg, p.o.) was given for 4 days twice daily and the dispersed acini were prepared at 12 bouts after last treatment. The profiles of Intracellular phosphoproteins were analyzed by two-dimensional gel electrophoresis after incubating the acini with <sup>32</sup>P. The amylase release from the dispersed acini was measured. The pancreatic weight was increased to 126% of control, while amylase activity per mg acinar protein decreased to 41% of control, The maximum response of amylase release from dispersed acini to CCK-8 or carbachol was markedly decreased(65% or 46% of control, respectively). The group of intracellular proteins(24 kD, pI 4.5 ~ 8.5) was increased in quantity by camostat. CCK-8 or secretin increased phosphorylation of a protein(34 kD, pI 4.7) in camostat-treated as well as control rats. CCK-8 increased tyrosine phosphoryiation in the acini of control rats. However, in camostat-treated rats, the basal level of tyrosine phosphorylation was increased and it was rather decreased by CCK-8. Secretin had no effect on the level of tyrosine phosphorylation in acini. These results indicate that both phospholipase C and adenylate cyclase induce phosphorylation of an intracellular acinar protein(34 kD, pI 4.7) and camostat treaFtment increases the basal level of tyrosine phosphorylation in acinar cells. And these results suggest that not only serine/threonine protein kinase but also protein tyrosine kinase/phosphatase are involved in the process of CCK receptor mediated stimulation-secrelion coupling.