10.1021/pr050377+.s001
Christian Hunzinger
Christian
Hunzinger
Wojciech Wozny
Wojciech
Wozny
Gerhard P. Schwall
Gerhard P.
Schwall
Slobodan Poznanović
Slobodan
Poznanović
Werner Stegmann
Werner
Stegmann
Helmut Zengerling
Helmut
Zengerling
Rainer Schoepf
Rainer
Schoepf
Karlfried Groebe
Karlfried
Groebe
Michael A. Cahill
Michael
A. Cahill
Heinz D. Osiewacz
Heinz
D. Osiewacz
Nora Jägemann
Nora
Jägemann
Monika Bloch
Monika
Bloch
Norbert A. Dencher
Norbert A.
Dencher
Frank Krause
Frank
Krause
André Schrattenholz
André
Schrattenholz
Comparative Profiling of the Mammalian Mitochondrial Proteome:
Multiple Aconitase-2 Isoforms Including <i>N</i>-formylkynurenine
Modifications as Part of a Protein Biomarker Signature for Reactive
Oxidative Species
American Chemical Society
2006
formylkynurenine Modifications
oligomeric states
heart mitochondria
membrane proteins
resolution IEF
ROS
mitochondrial preparations
Reactive Oxidative Species
Comparative Profiling
formylkynurenine modifications
Protein Biomarker Signature
mitochondrial proteins
protein spots
cell death
protein redundancy
2006-03-03 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Comparative_Profiling_of_the_Mammalian_Mitochondrial_Proteome_Multiple_Aconitase_2_Isoforms_Including_i_N_i_formylkynurenine_Modifications_as_Part_of_a_Protein_Biomarker_Signature_for_Reactive_Oxidative_Species/3372634
The activity of mitochondria induces, as a byproduct, a variety of post-translational modifications in
associated proteins, which have functional downstream consequences for processes such as apoptosis,
autophagy, and plasticity; e.g., reactive oxygen species (ROS), which induce <i>N</i>-formyl-kynurenine from
oxidized tryptophans in certain mitochondrial proteins which are localized in close spatial proximity to
their source. This type of fast molecular changes has profound influence on cell death and survival
with implications in a number of pathologies. The quantitative and differential analysis of bovine heart
mitochondria by four 2D-PAGE methods, including 2D-PAGE with high-resolution IEF as first dimension,
revealed that due to limited resolution, those methods employing blue native-, tricine-urea-, and 16-BAC-PAGE as the first dimension are less applicable for the differential quantitative analysis of redundant
protein spots which might give insight into post-translational modifications that are relevant in age-
and stress-related changes. Moreover, 2D-PAGE with high resolution IEF was able to resolve a
surprisingly large number of membrane proteins from mitochondrial preparations. For aconitase-2,
an enzyme playing an important role in mitochondrial aging, a more thorough molecular analysis of
all separable isoforms was performed, leading to the identification of two particular <i>N</i>-formylkynurenine
modifications. Next to protein redundancy, native protein−protein interactions, with the potential of
relating certain post-translational modification patterns to distinct oligomeric states, e.g., oxidative
phosphorylation super complexes, might provide novel and (patho-) physiologically relevant information. Among proteins identified, 14 new proteins (GenBank entries), previously not associated with
mitochondria, were found.
Keywords: mitochondria • proteomics • two-dimensional polyacrylamide gel electrophoresis • IEF-SDS-PAGE •
blue native-SDS-PAGE • tricine-urea-SDS-PAGE • 16-BAC-SDS-PAGE • quantitative differential protein expression •
membrane proteins • reactive oxygen species • aconitase-2 • <i>N</i>-formylkynurenine • post-translational modifications