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Impairment of endoplasmic reticulum in liver as an early consequence of the systemic inflammatory response in rats
Author(s) -
Sylvia Nürnberger,
Ingrid Miller,
J. Catharina Duvigneau,
Edel Kavanagh,
Sanjeev Gupta,
Romana T. Hartl,
Osamu Hori,
Bernd Gesslbauer,
Afshin Samali,
Andreas J. Kungl,
Heinz Redl,
Andrey V. Kozlov
Publication year - 2012
Publication title -
ajp gastrointestinal and liver physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.644
H-Index - 169
eISSN - 1522-1547
pISSN - 0193-1857
DOI - 10.1152/ajpgi.00056.2012
Subject(s) - endoplasmic reticulum , unfolded protein response , proteome , biology , cellular stress response , cytosol , microbiology and biotechnology , intracellular , downregulation and upregulation , mitochondrion , endocrinology , biochemistry , gene , fight or flight response , enzyme
It is well known that systemic inflammatory response (SIR) often causes liver dysfunction. The aim of this study was to identify the intracellular compartment in the liver most susceptible to SIR. We analyzed morphology, ultrastructure, proteome, and expression of relevant genes in livers of rats subjected to endotoxic shock. Histological examination revealed that focal necrosis in liver was insignificant to explain liver dysfunction. Electron microscopy revealed no morphological changes in the mitochondrial structure and in the cytosol, but dilated endoplasmic reticulum (ER) cisterns were frequently observed. Apoptosis was found in white blood cells within liver tissue but not in hepatocytes. Mitochondrial, ER, and cytosolic fractions were subjected to proteome analysis by difference gel electrophoresis, and the protein spots with the highest degree of differential regulation were identified with mass spectrometry. The most pronounced proteome changes appeared in the ER, manifested as a remarkable downregulation of several proteins essential for ER functions, such as protein synthesis and transport, whereas the changes in mitochondrial and cytosolic fractions suggested a compensatory response. ER stress, as an underlying mechanism for ER impairment, was confirmed by analysis of upstream (splicing X-box-binding protein 1 mRNA) and downstream (e.g., 78-kDa glucose-regulated protein mRNA) markers, suggesting ongoing unresolved ER stress as a cause for ER dilation. Because ER is the intracellular compartment responsible for the major liver functions, our data suggest that inflammatory mediators induce unresolved ER stress, resulting in the biochemical, functional, and morphological impairment of ER that in turn causes liver dysfunction. The pathway activating ER stress in response to SIR is not known yet.

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