PMID- 20957471
OWN - NLM
STAT- MEDLINE
DCOM- 20110407
LR  - 20220408
IS  - 1618-2650 (Electronic)
IS  - 1618-2642 (Print)
IS  - 1618-2642 (Linking)
VI  - 398
IP  - 7-8
DP  - 2010 Dec
TI  - A targeted mass spectrometry-based approach for the identification and 
      characterization of proteins containing alpha-aminoadipic and gamma-glutamic semialdehyde 
      residues.
PG  - 2905-14
LID - 10.1007/s00216-010-4289-0 [doi]
AB  - The site-specific identification of alpha-aminoadipic semialdehyde (AAS) and 
      gamma-glutamic semialdehyde (GGS) residues in proteins is reported. Semialdehydic 
      protein modifications result from the metal-catalyzed oxidation of Lys or Arg and 
      Pro residues, respectively. Most of the analytical methods for the analysis of 
      protein carbonylation measure change to the global level of carbonylation and 
      fail to provide details regarding protein identity, site, and chemical nature of 
      the carbonylation. In this work, we used a targeted approach, which combines 
      chemical labeling, enrichment, and tandem mass spectrometric analysis, for the 
      site-specific identification of AAS and GGS sites in proteins. The approach is 
      applied to in vitro oxidized glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and 
      an untreated biological sample, namely cardiac mitochondrial proteins. The 
      analysis of GAPDH resulted in the site-specific identification of two AAA and 
      four GGS residues. Computational evaluation of the identified AAS and GGS sites 
      in GAPDH indicated that these sites are located in flexible regions, show high 
      solvent accessibility values, and are in proximity with possible metal ion 
      binding sites. The targeted proteomic analysis of semialdehydic modifications in 
      cardiac mitochondria yielded nine AAS modification sites which were unambiguously 
      assigned to distinct lysine residues in the following proteins: ATP/ATP 
      translocase isoforms 1 and 2, ubiquinol cytochrome-c reductase core protein 2, 
      and ATP synthase alpha-subunit.
FAU - Chavez, Juan D
AU  - Chavez JD
AD  - Department of Chemistry, Oregon State University, Corvallis, OR 97331, USA.
FAU - Bisson, William H
AU  - Bisson WH
FAU - Maier, Claudia S
AU  - Maier CS
LA  - eng
GR  - R01 AG025372-05/AG/NIA NIH HHS/United States
GR  - R01 AG025372/AG/NIA NIH HHS/United States
GR  - R01AG025372/AG/NIA NIH HHS/United States
GR  - P30ES00210/ES/NIEHS NIH HHS/United States
GR  - P30 ES000210/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20101019
PL  - Germany
TA  - Anal Bioanal Chem
JT  - Analytical and bioanalytical chemistry
JID - 101134327
RN  - 0 (Glutamates)
RN  - 0 (Mitochondrial Proteins)
RN  - 1K7B1OED4N (2-Aminoadipic Acid)
RN  - 425I4Y24YZ (allysine)
RN  - 496-92-4 (glutamic acid gamma-semialdehyde)
RN  - EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating))
SB  - IM
MH  - 2-Aminoadipic Acid/*analogs & derivatives/chemistry/isolation & purification
MH  - Animals
MH  - Chromatography, Liquid/methods
MH  - Glutamates/*chemistry/isolation & purification
MH  - Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)/*chemistry
MH  - Male
MH  - Mitochondrial Proteins/chemistry
MH  - Models, Molecular
MH  - Oxidation-Reduction
MH  - Rats
MH  - Rats, Inbred F344
MH  - Spectrometry, Mass, Electrospray Ionization/*methods
MH  - Tandem Mass Spectrometry/*methods
PMC - PMC3071856
MID - NIHMS264564
EDAT- 2010/10/20 06:00
MHDA- 2011/04/08 06:00
PMCR- 2011/12/01
CRDT- 2010/10/20 06:00
PHST- 2010/07/24 00:00 [received]
PHST- 2010/10/03 00:00 [accepted]
PHST- 2010/09/30 00:00 [revised]
PHST- 2010/10/20 06:00 [entrez]
PHST- 2010/10/20 06:00 [pubmed]
PHST- 2011/04/08 06:00 [medline]
PHST- 2011/12/01 00:00 [pmc-release]
AID - 10.1007/s00216-010-4289-0 [doi]
PST - ppublish
SO  - Anal Bioanal Chem. 2010 Dec;398(7-8):2905-14. doi: 10.1007/s00216-010-4289-0. 
      Epub 2010 Oct 19.