Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry.
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.
Pelletier
Sarah
S
Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, Utrecht, The Netherlands.
Schuurman
Karianne G
KG
Berkers
Celia R
CR
Ovaa
Huib
H
Heck
Albert J R
AJ
Raijmakers
Reinout
R
D000818:Animals; D008099:Liver / Q000737:chemistry / Q000378:metabolism; D013058:Mass Spectrometry / Q000379:methods*; D051379:Mice; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D009928:Organ Specificity; D046988:Proteasome Endopeptidase Complex / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D021122:Protein Subunits / Q000032:analysis; D013154:Spleen / Q000737:chemistry / Q000378:metabolism; D014018:Tissue Distribution
D009097:Multienzyme Complexes; D021122:Protein Subunits; D046988:Proteasome Endopeptidase Complex