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Global analysis of protein folding thermodynamics for disease state characterization.

Publication ,  Journal Article
Adhikari, J; West, GM; Fitzgerald, MC
Published in: Journal of proteome research
May 2015

Current methods for the large-scale characterization of disease states generally rely on the analysis of gene and/or protein expression levels. These existing methods fail to detect proteins with disease-related functions and unaltered expression levels. Here we describe the large-scale use of thermodynamic measurements of protein folding and stability for the characterization of disease states. Using the Stable Isotope Labeling with Amino Acids in Cell Culture and Stability of Proteins from Rates of Oxidation (SILAC-SPROX) technique, we assayed ∼800 proteins for protein folding and stability changes in three different cell culture models of breast cancer including the MCF-10A, MCF-7, and MDA-MB-231 cell lines. The thermodynamic stability profiles generated here created distinct molecular markers to differentiate the three cell lines, and a significant fraction (∼45%) of the differentially stabilized proteins did not have altered expression levels. Thus, the differential thermodynamic profiling strategy reported here created novel molecular signatures of breast cancer and provided additional insight into the molecular basis of the disease. Our results establish the utility of protein folding and stability measurements for the study of disease processes, and they suggest that such measurements may be useful for biomarker discovery in disease.

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Published In

Journal of proteome research

DOI

EISSN

1535-3907

ISSN

1535-3893

Publication Date

May 2015

Volume

14

Issue

5

Start / End Page

2287 / 2297

Related Subject Headings

  • Thermodynamics
  • Proteomics
  • Proteome
  • Protein Stability
  • Protein Folding
  • Oxidation-Reduction
  • Neoplasm Proteins
  • Molecular Sequence Annotation
  • Isotope Labeling
  • Humans
 

Citation

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Chicago
ICMJE
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Adhikari, J., West, G. M., & Fitzgerald, M. C. (2015). Global analysis of protein folding thermodynamics for disease state characterization. Journal of Proteome Research, 14(5), 2287–2297. https://doi.org/10.1021/acs.jproteome.5b00057
Adhikari, Jagat, Graham M. West, and Michael C. Fitzgerald. “Global analysis of protein folding thermodynamics for disease state characterization.Journal of Proteome Research 14, no. 5 (May 2015): 2287–97. https://doi.org/10.1021/acs.jproteome.5b00057.
Adhikari J, West GM, Fitzgerald MC. Global analysis of protein folding thermodynamics for disease state characterization. Journal of proteome research. 2015 May;14(5):2287–97.
Adhikari, Jagat, et al. “Global analysis of protein folding thermodynamics for disease state characterization.Journal of Proteome Research, vol. 14, no. 5, May 2015, pp. 2287–97. Epmc, doi:10.1021/acs.jproteome.5b00057.
Adhikari J, West GM, Fitzgerald MC. Global analysis of protein folding thermodynamics for disease state characterization. Journal of proteome research. 2015 May;14(5):2287–2297.
Journal cover image

Published In

Journal of proteome research

DOI

EISSN

1535-3907

ISSN

1535-3893

Publication Date

May 2015

Volume

14

Issue

5

Start / End Page

2287 / 2297

Related Subject Headings

  • Thermodynamics
  • Proteomics
  • Proteome
  • Protein Stability
  • Protein Folding
  • Oxidation-Reduction
  • Neoplasm Proteins
  • Molecular Sequence Annotation
  • Isotope Labeling
  • Humans