Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry

Sarah Pelletier; Karianne G Schuurman; Celia R Berkers; Huib Ovaa; Albert J R Heck; Reinout Raijmakers

doi:10.1039/c004989a

Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry

Mol Biosyst. 2010 Aug;6(8):1450-3. doi: 10.1039/c004989a. Epub 2010 May 24.

Authors

Sarah Pelletier¹, Karianne G Schuurman, Celia R Berkers, Huib Ovaa, Albert J R Heck, Reinout Raijmakers

Affiliation

¹ Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, Utrecht, The Netherlands.

PMID: 20498902
DOI: 10.1039/c004989a

Abstract

The composition of 20S mouse proteasome complexes isolated from mice heart, kidney, liver, lung, thymus and spleen was compared using quantitative mass spectrometry. Significant variety was observed in hybrid classes of immunoproteasomes which may have implications for the use of proteasome targeted inhibitors.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Liver / chemistry
Liver / metabolism
Mass Spectrometry / methods*
Mice
Models, Biological
Multienzyme Complexes / analysis
Multienzyme Complexes / chemistry
Multienzyme Complexes / metabolism
Organ Specificity
Proteasome Endopeptidase Complex / analysis*
Proteasome Endopeptidase Complex / chemistry
Proteasome Endopeptidase Complex / metabolism*
Protein Subunits / analysis
Spleen / chemistry
Spleen / metabolism
Tissue Distribution

Substances

Multienzyme Complexes
Protein Subunits
Proteasome Endopeptidase Complex