Production of Trypsin by Cells of the Exocrine Pancreas Is Paralleled by the Expression of the KH Protein Vigilin

Kruse, Charli; Emmrich, Jörg; Rumpel, Elisabeth; Klinger, Matthias; Grünweller, Arnold; Rohwedel, Jürgen; Krammer, Heinz-Jürgen; Kühnel, Wolfgang; Müller, Peter

doi:10.1006/excr.1997.3891

Cited by 17 publications

(30 citation statements)

References 24 publications

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“…Here we hypothesised that the RNA-binding protein vigilin may play a crucial role in the onset of pancreatitis since trypsinogen is involved in the pathogenesis of pancreatitis [7,8] and we could demonstrate that trypsinogen expression coincided with vigilin expression [9,10]. In the present study the animal model of DBTC-induced chronic pancreatitis was used to test this hypothesis.…”

Section: Introductionmentioning

confidence: 72%

“…Sections were immunostained with different antibodies. Primary antisera were directed against vigilin (FP-III, dilution 1:500 in PBS containing 0.1% bovine serum albumin) from rabbits [11] or trypsin (1:200 in PBS containing 0.1% bovine serum albumin) [9]. Specimens were incubated with the primary antibody overnight at 4…”

Section: Immunohistochemical Proceduresmentioning

confidence: 99%

“…Using 7% polyacrylamide gels for vigilin and 10% polyacrylamide gels for trypsinogen detection, the presence of vigilin or trypsinogen was demonstrated by immunoblotting, using vigilin [11] or trypsinogen antibodies [9]. Preimmunization serum served as the background control.…”

Section: Electrophoresis and Immunoblotting Of Pancreatic Extractsmentioning

confidence: 99%

“…The production of trypsin(ogen) by cells of the exocrine pancreas is paralleled by the expression of the ubiquitous protein vigilin as demonstrated in vivo [9] and in vitro [10]. Vigilin is a 150 kDa protein containing 14 copies of the hnRNP K homology (KH) domain, is present in the nucleus and in the cytoplasm [11], and has apparently high affinity to RNA [12,13].…”

Section: Introductionmentioning

confidence: 99%

“…Vigilin is a 150 kDa protein containing 14 copies of the hnRNP K homology (KH) domain, is present in the nucleus and in the cytoplasm [11], and has apparently high affinity to RNA [12,13]. It is an essential protein in human cells [14] and preferentially expressed in cells with increased protein synthesis, for example in pancreatic acinar and diverse carcinoma cells [9,10]. A specific down-regulation of vigilin translation affects the synthesis of two different classes of proteins, digestive enzymes of the pancreas, as well as structural proteins such as cytokeratines [15].…”

Section: Introductionmentioning

confidence: 99%

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Enhanced vigilin and anionic trypsinogen expression in experimental chronic pancreatitis

et al. 2007

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AbstractThe 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.

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Section: Introductionmentioning

confidence: 72%

Section: Immunohistochemical Proceduresmentioning

confidence: 99%

Section: Electrophoresis and Immunoblotting Of Pancreatic Extractsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Enhanced vigilin and anionic trypsinogen expression in experimental chronic pancreatitis

et al. 2007

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A jack of all trades: the RNA‐binding protein vigilin

Cheng

Jansen

2017

WIREs RNA

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The vigilin family of proteins is evolutionarily conserved from yeast to humans and characterized by the proteins' 14 or 15 hnRNP K homology (KH) domains, typically associated with RNA-binding. Vigilin is the largest RNA-binding protein (RBP) in the KH domain-containing family and one of the largest RBP known to date. Since its identification 30 years ago, vigilin has been shown to bind over 700 mRNAs and has been associated with cancer progression and cardiovascular disease. We provide a brief historic overview of vigilin research and outline the proteins' different functions, focusing on maintenance of genome ploidy, heterochromatin formation, RNA export, as well as regulation of translation, mRNA transport, and mRNA stability. The multitude of associated functions is reflected by the large number of identified interaction partners, ranging from tRNAs, mRNAs, ribosomes and ribosome-associated proteins, to histone methyltransferases and DNA-dependent protein kinases. Most of these partners bind to vigilin's carboxyterminus, and the two most C-terminal KH domains of the protein, KH13 and KH14, represent the main mRNA-binding interface. Since the nuclear functions of vigilins in particular are not conserved, we outline a model for the basal functions of vigilins, as well as those which were acquired during the transition from unicellular organisms to metazoa. WIREs RNA 2017, 8:e1448. doi: 10.1002/wrna.1448 For further resources related to this article, please visit the WIREs website.

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