Heat Shock Proteins and Autophagy in Rats with Cerulein-Induced Acute Pancreatitis
Gut and Liver
;
: 513-520, 2011.
Article
in English
| WPRIM
| ID: wpr-56813
ABSTRACT
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.METHODS:
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 microg/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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pancreatitis
/
Autophagy
/
Trypsinogen
/
Ceruletide
/
Water
/
Cathepsin B
/
Microscopy, Electron
/
Blotting, Western
/
Hot Temperature
/
Heat-Shock Proteins
Limits:
Animals
Language:
English
Journal:
Gut and Liver
Year:
2011
Type:
Article
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