Estradiol Has a Direct Impact on the Exocrine Pancreas as Demonstrated by Enzyme and Vigilin Expression

Hilgendorf, Inken; Gellersen, Oliver; Emmrich, Jörg; Mikkat, Ulrike; Rohwedel, Jürgen; Krammer, Heinz-Jürgen; Müller, Peter; Kruse, Charli

doi:10.1159/000055788

Cited by 13 publications

(15 citation statements)

References 24 publications

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“…Figure 4 shows that in primary human fibroblasts, collagen synthesis was down-regulated during cultivation paralleled by a decrease in vigilin levels. In addition to collagen, the expression of several other secretory proteins has been shown to follow a similar pattern (table 1) [9,18,33,34,[40][41][42][43][44]. Whereas this demonstrated a correlation between the expression of vigilin and secretory proteins, we then investigated a similar relationship between vigilin and intracellular proteins.…”

Section: Discussionmentioning

confidence: 87%

The multi-KH protein vigilin associates with free and membrane-bound ribosomes

Kruse

Willkomm

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et al. 2003

Cellular and Molecular Life Sciences (CMLS)

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The-multi-KH domain protein vigilin has been identified by ex vivo experiments as both a tRNA- and/or mRNA-binding protein. We show here that in vitro under conditions previously shown to allow tRNA binding, recombinant vigilin also binds to selected mRNA species and ribosomal RNA. An in vivo link of vigilin to mRNA and rRNA was elucidated by several approaches. (i) Coexpression/costimulation of vigilin was found with many other proteins independently of whether their mRNA was translated on free or membrane-bound ribosomes. (ii) A close codistribution of vigilin with free ribosomes was seen in the cytoplasm while nucleoli were a major organelle of vigilin accumulation in the nucleus. (iii) Furthermore, free and membrane-bound ribosomes can be enriched for vigilin which suggests that this binding does not depend on the class of mRNA translated. Therefore, we suggest that vigilin does not distinguish between free or membrane-bound ribosomes but is generally necessary for the localization of mRNAs to actively translating ribosomes.

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Section: Discussionmentioning

confidence: 87%

The multi-KH protein vigilin associates with free and membrane-bound ribosomes

Kruse

Willkomm

Gebken

et al. 2003

Cellular and Molecular Life Sciences (CMLS)

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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: 71%

“…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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“…Vigilin is part of a ribonucleoprotein complex [18,19], which plays an important role in t-RNA trafficking [20] and is preferentially expressed in cells with increased protein synthesis, e.g. in pancreatic acinar cells after stimulation by food intake [21] or after estradiol stimulation of isolated pancreatic acini [22]. The input of tRNA into the translational machinery seems to depend on the presence of sufficient amounts of the vigilin containing tRNA-protein complex [20].…”

Section: Introductionmentioning

confidence: 99%