Heat shock protein (HSP) 70 expression reduces the severity of caerulein-induced acute pancreatitis by reducing intrapancreatic active trypsin levels

Frossard, J. L.; Saluja, Ashok; Hs, Lee; Bhagat, Lakshmi; Bhatia, Madhav; Steer, Michael L.

doi:10.1016/s0016-5085(98)81857-x

Cited by 3 publications

(2 citation statements)

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“…Prior thermal stress protects against cerulein-induced pancreatitis (8) and prevents cerulein-induced in vivo activation of trypsinogen in acinar cells (39). Whereas these phenomena are associated with thermal stress-induced HSP70 expression, thermal stress may have other effects, including induction of other HSPs, which could account for protection against pancreatitis and prevention of trypsinogen activation in vivo.…”

Section: Figurementioning

confidence: 99%

Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation

Bhagat¹,

Singh²,

Hietaranta³

et al. 2000

J. Clin. Invest.

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Section: Figurementioning

confidence: 99%

Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation

Bhagat¹,

Singh²,

Hietaranta³

et al. 2000

J. Clin. Invest.

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“…The fi rst of them is that hyperthermia can modify the interaction of cerulein with its receptors. However, in his (11) demonstrated that CCK-A receptors of pancreatic acini undergone hyperthermia keep its capability of binding the cerulein. Another suggestion is that hyperthermia might directly prevent the activation of pancreatic enzymes; however, another report showed that kinase activation activity was unaltered after heating procedure (24) ; nevertheless, this issue is controversial and other studies had demonstrated opposite results (4,13) .…”

Section: Resultsmentioning

confidence: 99%

Effect of hyperthermia on experimental acute pancreatitis

Almeida

Jukemura

Sampietre

et al. 2006

Arq. Gastroenterol.

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-Background -Recent studies indicate that hyperthermia can change infl ammatory mechanisms and protect experimental animals from deleterious effects of secretagogue-induced acute pancreatitis. Aim -To evaluate the effects of hyperthermia posttreatment on cerulein-induced acute pancreatitis in rats. Methods -Twenty animals were divided in two groups: group I (n = 10), rats with cerulein-induced acute pancreatitis undergone hyperthermia, and group II (n = 10), animals with cerulein-induced acute pancreatitis that were kept normothermic. In all groups, amylase serum levels, histologic damage, vascular permeability and pancreatic water content were assessed. Acute pancreatitis was induced by administration of two cerulein injections (20 mcg/kg). A single dose of Evans' blue dye was administered along with the second dose of cerulein. All animals also received a subcutaneous injection of saline solution. After this process, animals undergone hyperthermia were heated in a cage with two 100 W lamps. Body temperature was increased to 39.5ºC and maintained at that level for 45 minutes. Normothermia rats were kept at room temperature in a second cage. Results -Control animals had typical edema, serum amylase activity and morphologic changes of this acute pancreatitis model. Hyperthermia post-treatment ameliorated the pancreatic edema, whereas the histologic damage and the serum amylase level remained unchanged. Conclusions -The fi ndings suggest a benefi cial effect of the thermal stress on infl ammatory edema in experimental acute pancreatitis.

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Thermal stress–induced HSP70 mediates protection against intrapancreatic trypsinogen activation and acute pancreatitis in rats

Bhagat¹,

Singh²,

Song³

et al. 2002

Gastroenterology

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Heat shock protein (HSP) 70 expression reduces the severity of caerulein-induced acute pancreatitis by reducing intrapancreatic active trypsin levels

Cited by 3 publications

References 0 publications

Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation

Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation

Effect of hyperthermia on experimental acute pancreatitis

Thermal stress–induced HSP70 mediates protection against intrapancreatic trypsinogen activation and acute pancreatitis in rats

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