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KMID : 1188320110050040513
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Gut and Liver
2011 Volume.5 No. 4 p.513 ~ p.520
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Heat Shock Proteins and Autophagy in Rats with Cerulein-Induced Acute Pancreatitis
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Kim Jin-Nam
Lee Hong-Sik
Ryu Soo-Hyung
Kim You-Sun
Moon Jeong-Seop
Kim Chang-Duck
Chang In-Youb
Yoon Sang-Pill
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Abstract
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Background/Aims:Heat shock proteins (HSPs) protect rats from cerulein-induced acute pancreatitis (AP) by preventing the subcellular redistribution of cathepsin B and the activation of trypsinogen. Autophagy plays a critical role in the secretion of digestive enzymes and triggering of cerulein-induced AP via the colocalization of trypsinogen and lysosomes. Therefore, using a rat cerulein-induced AP model, we investigated whether HSPs prevent AP by regulating autophagy.
Method:Twelve hours after fed standard laboratory chow and water, the experimental groups (cerulein, water-immersion [WI]-cerulein and heat-shock [HS]-cerulein) and the control groups (control, WI, and HS) received one intraperitoneal injection of cerulein (50 μg/kg) or saline, respectively. All of the rats were sacrificed at 6 hours after injection. The severity of the AP was assessed based on the serum amylase level and the histological and electron microscopy findings. Western blotting was also performed for HSP60/70 and LC3B-II.
Results:WI and HS induced HSP60 and HSP70, respectively. The induced HSP60/70 effectively prevented the development of cerulein-induced AP. Autophagy developed in the rats with cerulein-induced AP and was documented by the expression of LC3-II and electron microscopy findings. The WI-stressed rats and HS-treated rats did not develop cerulein-induced autophagy.
Conclusions:HSPs exert protective effects against cerulein-induced AP in rats by inhibiting autophagy.
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KEYWORD
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Acute pancreatitis, Autophagy, Heat shock protein
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