Enhanced vigilin and anionic trypsinogen expression in experimental chronic pancreatitis

• Authors: Inken Hilgendorf , Karen Aßmuth , Gisela Sparmann , Jörg Emmrich , Charli Kruse
• Languages of publication: EN

Abstracts

EN

The molecular principles that lead to chronic pancreatitis are incompletely understood. Trypsin(ogen) plays a key role in the development of pancreatitis. Since the production of trypsin(ogen) by acinary pancreatic cells is paralleled by the expression of vigilin we hypothesised that vigilin may be involved in the onset of pancreatitis. Vigilin is a ubiquitous protein and has apparently high affinity to RNA.In the present study experimental pancreatitis was induced in male rats by a single intravenous application of dibutyltin dichloride (DBTC). Sections of rat pancreas were immunostained with an affinity-purified polyclonal antiserum against vigilin or trypsin(ogen). The changes in vigilin and trypsin(ogen) protein expression were determined by immunoblotting and subsequent sequence analysis of the amino acids.Induction of pancreatitis by DBTC caused alterations in the distribution and the amount of both vigilin and trypsin(ogen) as shown by immunohistochemical and immunoblot analysis.Furthermore we could demonstrate that anionic trypsinogen expression is up-regulated in DBTC-induced chronic pancreatitis. The obtained results suggest that vigilin as well as trypsin(ogen) are involved in the pathogenesis of pancreatitis and that the long-time DBTC-induced pancreatitis is a useful model for study of chronic pancreatitis.

Keywords

EN

Pancreatitis; trypsin; vigilin

• Publisher: De Gruyter Open
• Journal: Open Medicine
• Year: 2007
• Volume: 2
• Issue: 2
• Pages: 159-167

Dates

published

1 - 6 - 2007

online

1 - 6 - 2007

Contributors

author

Inken Hilgendorf

• Division of Haematology and Oncology, Department of Medicine, Medical Faculty, University Rostock, 18057, Rostock, Germany

author

Karen Aßmuth

• Frauenhofer-Institute of Biomedical Engineering, Group of Cell Differentiation and Cell Technology at the University of Lübeck, 23538, Lübeck, Germany

author

Gisela Sparmann

• Division of Gastroenterology, Department of Medicine, Medical Faculty, University Rostock, 18057, Rostock, Germany

author

Jörg Emmrich

• Division of Gastroenterology, Department of Medicine, Medical Faculty, University Rostock, 18057, Rostock, Germany

author

Charli Kruse

• Frauenhofer-Institute of Biomedical Engineering, Group of Cell Differentiation and Cell Technology at the University of Lübeck, 23538, Lübeck, Germany

References

• [1] R.M. Mitchell, M.F. Byrne and J. Baillie: “Pancreatitis”, Lancet, Vol. 361, (2003), pp. 1447–55. http://dx.doi.org/10.1016/S0140-6736(03)13139-X[Crossref]
• [2] T. Strate, W.T. Knoefel, E. Yekebas and J.R. Izbicki: “Chronic pancreatitis: aetiology, pathogenesis, diagnosis, and treatment”, Int. J. Colorectal. Dis., Vol. 18, (2003), pp. 97–106.
• [3] R.M. Charnley: “Hereditary pancreatitis”, World. J. Gastroenterol., Vol. 9, (2003) pp. 1–4.
• [4] C. Hanck, A. Schneider and D.C. Whitcomb: “Genetic polymorphisms in alcoholic pancreatitis”, Best. Pract. Res. Clin. Gastroenterol., Vol. 17, (2003), pp. 613–623. http://dx.doi.org/10.1016/S1521-6918(03)00048-9[Crossref]
• [5] D.C. Whitcomb: “Motion-Genetic testing is useful in the diagnosis of nonhereditary pancreatic conditions: Arguments for the motion”, Can. J. Gastroenterol., Vol. 17, (2003), pp. 47–52.
• [6] G. Sparmann, J. Merkord, A. Jäschke, H. Nizze, L. Jonas, M. Löhr, S. Liebe and J. Emmrich: “Pancreatic fibrosis in experimental pancreatitis induced by dibultylin dichloride”, Gastroenterology, Vol. 112, (1997), pp. 1664–1672. http://dx.doi.org/10.1016/S0016-5085(97)70049-0[Crossref]
• [7] H. Rinderknecht: “Activation of pancreatic zymogens, normal activation, premature intrapancreatic activation, protective mechanisms against inappropriate activation”, Dig. Dis. Sci., Vol. 31, (1986), pp. 324–331. http://dx.doi.org/10.1007/BF01318124[Crossref]
• [8] Y. Tando, H. Algul, G. Schneider, C.K. Weber, H. Weidenbach, G. Adler and R.M. Schmid: “Induction of IkappaB-kinase by cholecystokinin is mediated by trypsinogen activation in rat pancreatic lobules”, Digestion, Vol. 66, (2002), pp. 237–245. http://dx.doi.org/10.1159/000068364[Crossref]
• [9] C. Kruse, J. Emmrich, E. Rumpel, M.H.F. Klinger, A. Grünweller, J. Rohwedel, H.J. Krammer, W. Kühnel and P.K. Müller: “Production of trypsin by cells of the exocrine pancreas is paralleled by the expression of the KH protein vigilin”, Exp. Cell. Res., Vol. 239, (1998), pp. 111–118. http://dx.doi.org/10.1006/excr.1997.3891[Crossref]
• [10] I. Hilgendorf, O. Gellersen, J. Emmrich, U. Mikkat, J. Rohwedel, H.J. Krammer and P.K. Müller: “Estradiol has a direct impact on the exocrine pancreas as demonstrated by enzyme and vigilin expression”, Pancreatology, Vol. 1, (2001), pp. 24–29. http://dx.doi.org/10.1159/000055788[Crossref]
• [11] S. Kügler, A. Grünweller, C. Probst, M.H.F. Klinger, P.K. Müller and C. Kruse: “Vigilin contains a functional localisation sequence and is present in both the cytoplasm and the nucleus”, FEBS Lett., Vol. 382, (1996), pp. 330–334. http://dx.doi.org/10.1016/0014-5793(96)00204-9[Crossref]
• [12] C. Kruse, A. Grünweller, H. Notbohm, S. Kügler, W.G. Purschke and P.K. Müller: “Evidence for a novel cytoplasmatic tRNA complex containing the KH-multidomain protein vigilin”, Biochem. J., Vol. 320, (1996), pp. 247–252.
• [13] C. Kruse, D.K. Willkomm, A. Grünweller, T. Vollbrandt, S. Sommer, S. Busch, T. Pfeiffer, J. Brinkman, R.K. Hartmann and P.K. Müller: “Export and transport of tRNA are coupled to a multi-protein complex”, Biochem. J., Vol. 346, (2000), pp. 107–115. http://dx.doi.org/10.1042/0264-6021:3460107[Crossref]
• [14] K.M. Goolsby and D.J. Shapiro: “RNAi-mediated depletion of the 15 KH domain protein, vigilin, induces death of dividing and non-dividing human cells but does not initially inhibit protein synthesis”, Nucleic. Acids. Res., Vol. 31, (2003), pp. 5644–5653. http://dx.doi.org/10.1093/nar/gkg768[Crossref]
• [15] A. Schuh, K. Assmuth, I. Hilgendorf, P.K. Mueller and C. Kruse: “Protein synthesis of eukaryotic cells could be decreased by antisense-DNA of the multi KH domain protein vigilin”, Int. J. Mol. Med., Vol. 12, (2003), pp. 35–43.
• [16] M. Bradford: “A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein dye binding”, Anal. Biochem., Vol. 72, (1976), pp. 248–254. http://dx.doi.org/10.1016/0003-2697(76)90527-3[Crossref]
• [17] U.K. Laemmli: “Cleavage of structural proteins during the assembly of the head of bacteriophage T4”, Nature, Vol. 227, (1970), pp. 680–685. http://dx.doi.org/10.1038/227680a0[Crossref]
• [18] W.R. Pearson and D.J. Lipman: “Improved tools for biological sequence comparison”, Proc. Natl. Acad. Sci. USA, Vol. 85, (1988), pp. 2444–2448. http://dx.doi.org/10.1073/pnas.85.8.2444[Crossref]
• [19] C. Kruse, R.K. Hartmann and P.K. Müller: “Nuclear-cytoplasmatic translocation of tRNA”, Exp. Cell. Res., Vol. 262, (2001), pp. 3–7. http://dx.doi.org/10.1006/excr.2000.5070[Crossref]
• [20] E. Colomb, O. Guy, P. Deprez, R. Michel and C. Figarella: “The two human trypsinogens: catalytic properties of the corresponding trypsins”, Biochem. Biophys. Acta., Vol. 525, (1978), pp. 186–193.
• [21] J. Schick, R. Verspohl, H. Kern and G. Scheele: “Two distinct adaptive responses in the synthesis of exocrine pancreatic enzymes inverse changes in protein and carbohydrate in the diet”, Am. J. Physiol., Vol. 247, (1984), pp. G611–616.
• [22] H. Rinderknecht, I.G. Renner and C. Carmack: “Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics and patients with pancreatitis and cancer of the pancreas”, Gut, Vol. 20, (1979), pp. 886–891.
• [23] M. Kimland, C. Russick, W.H. Marks and A. Borgstrom: “Immunoreactive anionic and cationic trypsin in human serum”, Clin. Chim. Acta., Vol. 148, (1989), pp. 31–46. http://dx.doi.org/10.1016/0009-8981(89)90254-4[Crossref]
• [24] Z. Kukor, M. Tòth and M. Sahin-Tòth: “Human anionic trypsinogen. Properties of autocatalytic activation and degradation and implications in pancreatic diseases”, Eur. J. Biochem., Vol. 270, (2003), pp. 2047–2058. http://dx.doi.org/10.1046/j.1432-1033.2003.03581.x[Crossref]

Identifiers

DOI

10.2478/s11536-007-0019-1