Induction of heat shock proteins fails to produce protection against trypsin-induced acute pancreatitis in rats

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Heat shock proteins (HSPs) are necessary in the synthesis, degradation, folding, transport, and translocation of different proteins. It is well known that the increased expression of HSPs may have a protective effect against cerulein-induced pancreatitis in rats or against choline-deficient ethionine-supplemented diet model pancreatitis in mice. The aim of this study was to investigate the potential effects of HSP preinduction by cold or hot water immersion on trypsin-induced acute pancreatitis in rats. Trypsin was injected into the interlobular tissue of the duodenal part of the pancreas at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were sacrificed by exsanguination through the abdominal aorta 6 h after the trypsin injection. The serum amylase activity, the tumor necrosis factor-α, interleukin-1, and interleukin-6 levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured. A biopsy for histology was taken. Hot water immersion significantly elevated the HSP72 expression, while cold water immersion significantly increased the HSP60 expression. Cold water immersion pretreatment ameliorated the pancreatic edema in trypsin-induced pancreatitis, however this was not due to the HSP60. Hot water immersion pretreatment did not have any effect on the measured parameters in trypsin-induced pancreatitis. The findings suggest that the induction of HSP60 or HSP72 are not enough to protect rats against the early phase of this localized necrohemorrhagic pancreatitis model.

Original languageEnglish
Pages (from-to)89-97
Number of pages9
JournalClinical and Experimental Medicine
Volume2
Issue number2
Publication statusPublished - 2002

Fingerprint

Heat-Shock Proteins
Pancreatitis
Trypsin
Immersion
Rats
Water
Amylases
Ethionine
Trypsinogen
Ceruletide
Histology
Biopsy
Exsanguination
Nutrition
Choline
Lipase
Interleukin-1
Abdominal Aorta
Protein Transport
Interleukin-6

Keywords

  • HSP60
  • HSP72
  • Pancreatitis
  • Sodium taurocholate
  • Water immersion

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Clinical Biochemistry

Cite this

@article{aa08c75b405b4ac0a5323cbbc8e1b40b,
title = "Induction of heat shock proteins fails to produce protection against trypsin-induced acute pancreatitis in rats",
abstract = "Heat shock proteins (HSPs) are necessary in the synthesis, degradation, folding, transport, and translocation of different proteins. It is well known that the increased expression of HSPs may have a protective effect against cerulein-induced pancreatitis in rats or against choline-deficient ethionine-supplemented diet model pancreatitis in mice. The aim of this study was to investigate the potential effects of HSP preinduction by cold or hot water immersion on trypsin-induced acute pancreatitis in rats. Trypsin was injected into the interlobular tissue of the duodenal part of the pancreas at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were sacrificed by exsanguination through the abdominal aorta 6 h after the trypsin injection. The serum amylase activity, the tumor necrosis factor-α, interleukin-1, and interleukin-6 levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured. A biopsy for histology was taken. Hot water immersion significantly elevated the HSP72 expression, while cold water immersion significantly increased the HSP60 expression. Cold water immersion pretreatment ameliorated the pancreatic edema in trypsin-induced pancreatitis, however this was not due to the HSP60. Hot water immersion pretreatment did not have any effect on the measured parameters in trypsin-induced pancreatitis. The findings suggest that the induction of HSP60 or HSP72 are not enough to protect rats against the early phase of this localized necrohemorrhagic pancreatitis model.",
keywords = "HSP60, HSP72, Pancreatitis, Sodium taurocholate, Water immersion",
author = "Z. Rakonczay and T. Tak{\'a}cs and B. Iv{\'a}nyi and Y. M{\'a}ndi and G. P{\'a}pai and I. Boros and I. Varga and K. Jost and J. Lonovics",
year = "2002",
language = "English",
volume = "2",
pages = "89--97",
journal = "Zeitschrift für Die Gesamte Experimentelle Medizin",
issn = "1591-8890",
publisher = "Springer Verlag",
number = "2",

}

TY - JOUR

T1 - Induction of heat shock proteins fails to produce protection against trypsin-induced acute pancreatitis in rats

AU - Rakonczay, Z.

AU - Takács, T.

AU - Iványi, B.

AU - Mándi, Y.

AU - Pápai, G.

AU - Boros, I.

AU - Varga, I.

AU - Jost, K.

AU - Lonovics, J.

PY - 2002

Y1 - 2002

N2 - Heat shock proteins (HSPs) are necessary in the synthesis, degradation, folding, transport, and translocation of different proteins. It is well known that the increased expression of HSPs may have a protective effect against cerulein-induced pancreatitis in rats or against choline-deficient ethionine-supplemented diet model pancreatitis in mice. The aim of this study was to investigate the potential effects of HSP preinduction by cold or hot water immersion on trypsin-induced acute pancreatitis in rats. Trypsin was injected into the interlobular tissue of the duodenal part of the pancreas at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were sacrificed by exsanguination through the abdominal aorta 6 h after the trypsin injection. The serum amylase activity, the tumor necrosis factor-α, interleukin-1, and interleukin-6 levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured. A biopsy for histology was taken. Hot water immersion significantly elevated the HSP72 expression, while cold water immersion significantly increased the HSP60 expression. Cold water immersion pretreatment ameliorated the pancreatic edema in trypsin-induced pancreatitis, however this was not due to the HSP60. Hot water immersion pretreatment did not have any effect on the measured parameters in trypsin-induced pancreatitis. The findings suggest that the induction of HSP60 or HSP72 are not enough to protect rats against the early phase of this localized necrohemorrhagic pancreatitis model.

AB - Heat shock proteins (HSPs) are necessary in the synthesis, degradation, folding, transport, and translocation of different proteins. It is well known that the increased expression of HSPs may have a protective effect against cerulein-induced pancreatitis in rats or against choline-deficient ethionine-supplemented diet model pancreatitis in mice. The aim of this study was to investigate the potential effects of HSP preinduction by cold or hot water immersion on trypsin-induced acute pancreatitis in rats. Trypsin was injected into the interlobular tissue of the duodenal part of the pancreas at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were sacrificed by exsanguination through the abdominal aorta 6 h after the trypsin injection. The serum amylase activity, the tumor necrosis factor-α, interleukin-1, and interleukin-6 levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured. A biopsy for histology was taken. Hot water immersion significantly elevated the HSP72 expression, while cold water immersion significantly increased the HSP60 expression. Cold water immersion pretreatment ameliorated the pancreatic edema in trypsin-induced pancreatitis, however this was not due to the HSP60. Hot water immersion pretreatment did not have any effect on the measured parameters in trypsin-induced pancreatitis. The findings suggest that the induction of HSP60 or HSP72 are not enough to protect rats against the early phase of this localized necrohemorrhagic pancreatitis model.

KW - HSP60

KW - HSP72

KW - Pancreatitis

KW - Sodium taurocholate

KW - Water immersion

UR - http://www.scopus.com/inward/record.url?scp=0036351105&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036351105&partnerID=8YFLogxK

M3 - Article

VL - 2

SP - 89

EP - 97

JO - Zeitschrift für Die Gesamte Experimentelle Medizin

JF - Zeitschrift für Die Gesamte Experimentelle Medizin

SN - 1591-8890

IS - 2

ER -