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Palmfeldt J, Vang S, Stenbroen V, et al. Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress. Proteome Sci. 2009;7:20doi: 10.1186/1477-5956-7-20.
Palmfeldt, J., Vang, S., Stenbroen, V., Pedersen, C. B., Christensen, J. H., Bross, P., & Gregersen, N. (2009). Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress. Proteome science, 720. https://doi.org/10.1186/1477-5956-7-20
Palmfeldt, Johan, et al. "Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress." Proteome science vol. 7 (2009): 20. doi: https://doi.org/10.1186/1477-5956-7-20
Palmfeldt J, Vang S, Stenbroen V, Pedersen CB, Christensen JH, Bross P, Gregersen N. Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress. Proteome Sci. 2009 May 28;7:20. doi: 10.1186/1477-5956-7-20. PMID: 19476632; PMCID: PMC2695441.
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Proteome Sci. 2009 May 28;7:20. doi: 10.1186/1477-5956-7-20.

Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress.

Proteome science

Johan Palmfeldt, Søren Vang, Vibeke Stenbroen, Christina B Pedersen, Jane H Christensen, Peter Bross, Niels Gregersen

Affiliations

  1. Institute of Clinical Medicine, Aarhus University Hospital, University of Aarhus, Denmark. [email protected]

PMID: 19476632 PMCID: PMC2695441 DOI: 10.1186/1477-5956-7-20

Abstract

BACKGROUND: Mitochondrial proteins are central to various metabolic activities and are key regulators of apoptosis. Disturbance of mitochondrial proteins is therefore often associated with disease. Large scale protein data are required to capture the mitochondrial protein levels and mass spectrometry based proteomics is suitable for generating such data. To study the relative quantities of mitochondrial proteins in cells from cultivated human skin fibroblasts we applied a proteomic method based on nanoLC-MS/MS analysis of iTRAQ-labeled peptides.

RESULTS: When fibroblast cultures were exposed to mild metabolic stress - by cultivation in galactose medium- the amount of mitochondria appeared to be maintained whereas the levels of individual proteins were altered. Proteins of respiratory chain complex I and IV were increased together with NAD+-dependent isocitrate dehydrogenase of the citric acid cycle illustrating cellular strategies to cope with altered energy metabolism. Furthermore, quantitative protein data, with a median standard error below 6%, were obtained for the following mitochondrial pathways: fatty acid oxidation, citric acid cycle, respiratory chain, antioxidant systems, amino acid metabolism, mitochondrial translation, protein quality control, mitochondrial morphology and apoptosis.

CONCLUSION: The robust analytical platform in combination with a well-defined compendium of mitochondrial proteins allowed quantification of single proteins as well as mapping of entire pathways. This enabled characterization of the interplay between metabolism and stress response in human cells exposed to mild stress.

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