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Proteomic and metabolomic responses to connexin43 silencing in primary hepatocyte cultures

Mathieu Vinken, Michaël Maes, Rachel Cavill, Dirk Valkenborg, James K Ellis, Elke Decrock UGent, Luc Leybaert UGent, An Staes UGent, Kris Gevaert UGent, André G Oliveira, et al. (2013) ARCHIVES OF TOXICOLOGY. 87(5). p.883-894
abstract
Freshly established cultures of primary hepatocytes progressively adopt a foetal-like phenotype and display increased production of connexin43. The latter is a multifaceted cellular entity with variable subcellular locations, including the mitochondrial compartment. Cx43 forms hemichannels and gap junctions that are involved in a plethora of physiological and pathological processes, such as apoptosis. The present study was conducted with the goal of shedding more light onto the role of connexin43 in primary hepatocyte cultures. Connexin43 expression was suppressed by means of RNA interference technology, and the overall outcome of this treatment on the hepatocellular proteome and metabolome was investigated using tandem mass tag-based differential protein profiling and 1H NMR spectroscopy, respectively. Global protein profiling revealed a number of targets of the connexin43 knock-down procedure, including mitochondrial proteins (heat shock protein 60, glucose-regulated protein 75, thiosulphate sulphurtransferase and adenosine triphosphate synthase) and detoxifying enzymes (glutathione S-transferase μ 2 and cytochrome P450 2C70). At the metabolomic level, connexin43 silencing caused no overt changes, though there was some evidence for a subtle increase in intracellular glycine quantities. Collectively, these data could further substantiate the established existence of a mitochondrial connexin pool and could be reconciled with the previously reported involvement of connexin43 signalling in spontaneously occurring apoptosis in primary hepatocyte cultures.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
Proteomics, Primary hepatocyte, Metabolomics, Connexin43, CELL-DEATH, APOPTOSIS, NORMALIZATION, CONTRIBUTES, CHANNELS
journal title
ARCHIVES OF TOXICOLOGY
Arch. Toxicol.
volume
87
issue
5
pages
883 - 894
Web of Science type
Article
Web of Science id
000317682700011
ISSN
1432-0738
DOI
10.1007/s00204-012-0994-0
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
3175312
handle
http://hdl.handle.net/1854/LU-3175312
date created
2013-03-26 14:52:13
date last changed
2016-12-19 15:39:25
@article{3175312,
  abstract     = {Freshly established cultures of primary hepatocytes progressively adopt a foetal-like phenotype and display increased production of connexin43. The latter is a multifaceted cellular entity with variable subcellular locations, including the mitochondrial compartment. Cx43 forms hemichannels and gap junctions that are involved in a plethora of physiological and pathological processes, such as apoptosis. The present study was conducted with the goal of shedding more light onto the role of connexin43 in primary hepatocyte cultures. Connexin43 expression was suppressed by means of RNA interference technology, and the overall outcome of this treatment on the hepatocellular proteome and metabolome was investigated using tandem mass tag-based differential protein profiling and 1H NMR spectroscopy, respectively. Global protein profiling revealed a number of targets of the connexin43 knock-down procedure, including mitochondrial proteins (heat shock protein 60, glucose-regulated protein 75, thiosulphate sulphurtransferase and adenosine triphosphate synthase) and detoxifying enzymes (glutathione S-transferase \ensuremath{\mu} 2 and cytochrome P450 2C70). At the metabolomic level, connexin43 silencing caused no overt changes, though there was some evidence for a subtle increase in intracellular glycine quantities. Collectively, these data could further substantiate the established existence of a mitochondrial connexin pool and could be reconciled with the previously reported involvement of connexin43 signalling in spontaneously occurring apoptosis in primary hepatocyte cultures.},
  author       = {Vinken, Mathieu and Maes, Micha{\"e}l and Cavill, Rachel and Valkenborg, Dirk and Ellis, James K and Decrock, Elke and Leybaert, Luc and Staes, An and Gevaert, Kris and Oliveira, Andr{\'e} G and Menezes, Gustavo B and Cogliati, Bruno and Dagli, Maria L{\'u}cia Zaidan and Ebbels, Timothy MD and Witters, Erwin and Keun, Hector C and Vanhaecke, Tamara and Rogiers, Vera},
  issn         = {1432-0738},
  journal      = {ARCHIVES OF TOXICOLOGY},
  keyword      = {Proteomics,Primary hepatocyte,Metabolomics,Connexin43,CELL-DEATH,APOPTOSIS,NORMALIZATION,CONTRIBUTES,CHANNELS},
  language     = {eng},
  number       = {5},
  pages        = {883--894},
  title        = {Proteomic and metabolomic responses to connexin43 silencing in primary hepatocyte cultures},
  url          = {http://dx.doi.org/10.1007/s00204-012-0994-0},
  volume       = {87},
  year         = {2013},
}

Chicago
Vinken, Mathieu, Michaël Maes, Rachel Cavill, Dirk Valkenborg, James K Ellis, Elke Decrock, Luc Leybaert, et al. 2013. “Proteomic and Metabolomic Responses to Connexin43 Silencing in Primary Hepatocyte Cultures.” Archives of Toxicology 87 (5): 883–894.
APA
Vinken, M., Maes, M., Cavill, R., Valkenborg, D., Ellis, J. K., Decrock, E., Leybaert, L., et al. (2013). Proteomic and metabolomic responses to connexin43 silencing in primary hepatocyte cultures. ARCHIVES OF TOXICOLOGY, 87(5), 883–894.
Vancouver
1.
Vinken M, Maes M, Cavill R, Valkenborg D, Ellis JK, Decrock E, et al. Proteomic and metabolomic responses to connexin43 silencing in primary hepatocyte cultures. ARCHIVES OF TOXICOLOGY. 2013;87(5):883–94.
MLA
Vinken, Mathieu, Michaël Maes, Rachel Cavill, et al. “Proteomic and Metabolomic Responses to Connexin43 Silencing in Primary Hepatocyte Cultures.” ARCHIVES OF TOXICOLOGY 87.5 (2013): 883–894. Print.