Difference between revisions of "Miller 2006 FEBS Lett"
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{{Publication | {{Publication | ||
|title=Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nürnberger S, Bahrami | |title=Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nürnberger S, Bahrami Sl, Redl H, Kozlov AV (2006) Proteome analysis of rat liver mitochondria reveals a possible compensatory response to endotoxic shock. FEBS Lett 580:1257-62. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/16442530 PMID: 16442530] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/16442530 PMID: 16442530] | ||
|authors=Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nuernberger S, Bahrami | |authors=Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nuernberger S, Bahrami Sl, Redl H, Kozlov AV | ||
|year=2006 | |year=2006 | ||
|journal=FEBS | |journal=FEBS Lett | ||
|abstract=Organ failure induced by endotoxic shock has recently been associated with affected mitochondrial function. In this study, effects of ''in vivo'' lipopolysaccharide-challenge on protein patterns of rat liver mitochondria in treated animals versus controls were studied by two-dimensional electrophoresis (differential image gel electrophoresis). Significant upregulation was found for ATP-synthase α chain and superoxide dismutase [Mn]. Our data suggest that endotoxic shock mediated changes in the mitochondrial proteome contribute to a compensatory reaction (adaptation to endotoxic shock) rather than to a mechanism of cell damage. | |abstract=Organ failure induced by endotoxic shock has recently been associated with affected mitochondrial function. In this study, effects of ''in vivo'' lipopolysaccharide-challenge on protein patterns of rat liver mitochondria in treated animals versus controls were studied by two-dimensional electrophoresis (differential image gel electrophoresis). Significant upregulation was found for ATP-synthase α chain and superoxide dismutase [Mn]. Our data suggest that endotoxic shock mediated changes in the mitochondrial proteome contribute to a compensatory reaction (adaptation to endotoxic shock) rather than to a mechanism of cell damage. | ||
|keywords=Mitochondria, Proteomics, Lipopolysaccharide, Endotoxic shock, ATP-synthase, Superoxide dismutase | |keywords=Mitochondria, Proteomics, Lipopolysaccharide, Endotoxic shock, ATP-synthase, Superoxide dismutase | ||
|mipnetlab= | |mipnetlab=AT Vienna Kozlov AV | ||
|discipline=Biomedicine | |discipline=Biomedicine | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Rat | |organism=Rat | ||
|tissues=Liver | |tissues=Liver | ||
|injuries=Mitochondrial disease | |||
|couplingstates=OXPHOS | |couplingstates=OXPHOS | ||
|instruments=Oxygraph-2k | |||
|discipline=Biomedicine | |discipline=Biomedicine | ||
}} | }} |
Latest revision as of 14:26, 3 June 2015
Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nürnberger S, Bahrami Sl, Redl H, Kozlov AV (2006) Proteome analysis of rat liver mitochondria reveals a possible compensatory response to endotoxic shock. FEBS Lett 580:1257-62. |
Miller I, Gemeiner M, Gesslbauer B, Kungl A, Piskernik C, Haindl S, Nuernberger S, Bahrami Sl, Redl H, Kozlov AV (2006) FEBS Lett
Abstract: Organ failure induced by endotoxic shock has recently been associated with affected mitochondrial function. In this study, effects of in vivo lipopolysaccharide-challenge on protein patterns of rat liver mitochondria in treated animals versus controls were studied by two-dimensional electrophoresis (differential image gel electrophoresis). Significant upregulation was found for ATP-synthase α chain and superoxide dismutase [Mn]. Our data suggest that endotoxic shock mediated changes in the mitochondrial proteome contribute to a compensatory reaction (adaptation to endotoxic shock) rather than to a mechanism of cell damage. • Keywords: Mitochondria, Proteomics, Lipopolysaccharide, Endotoxic shock, ATP-synthase, Superoxide dismutase
• O2k-Network Lab: AT Vienna Kozlov AV
Labels:
Stress:Mitochondrial disease Organism: Rat Tissue;cell: Liver
Coupling state: OXPHOS
HRR: Oxygraph-2k