PMID- 27350002
OWN - NLM
STAT- MEDLINE
DCOM- 20170925
LR  - 20180104
IS  - 1535-3907 (Electronic)
IS  - 1535-3893 (Linking)
VI  - 15
IP  - 8
DP  - 2016 Aug 5
TI  - Redox Sensitivities of Global Cellular Cysteine Residues under Reductive and 
      Oxidative Stress.
PG  - 2548-59
LID - 10.1021/acs.jproteome.6b00087 [doi]
AB  - The protein cysteine residue is one of the amino acids most susceptible to 
      oxidative modifications, frequently caused by oxidative stress. Several 
      applications have enabled cysteine-targeted proteomics analysis with simultaneous 
      detection and quantitation. In this study, we employed a quantitative approach 
      using a set of iodoacetyl-based cysteine reactive isobaric tags (iodoTMT) and 
      evaluated the transient cellular oxidation ratio of free and reversibly modified 
      cysteine thiols under DTT and hydrogen peroxide (H2O2) treatments. DTT treatment 
      (1 mM for 5 min) reduced most cysteine thiols, irrespective of their cellular 
      localizations. It also caused some unique oxidative shifts, including for 
      peroxiredoxin 2 (PRDX2), uroporphyrinogen decarboxylase (UROD), and thioredoxin 
      (TXN), proteins reportedly affected by cellular reactive oxygen species 
      production. Modest H2O2 treatment (50 muM for 5 min) did not cause global 
      oxidations but instead had apparently reductive effects. Moreover, with H2O2, 
      significant oxidative shifts were observed only in redox active proteins, like 
      PRDX2, peroxiredoxin 1 (PRDX1), TXN, and glyceraldehyde 3-phosphate dehydrogenase 
      (GAPDH). Overall, our quantitative data illustrated both H2O2- and 
      reduction-mediated cellular responses, whereby while redox homeostasis is 
      maintained, highly reactive thiols can potentiate the specific, rapid cellular 
      signaling to counteract acute redox stress.
FAU - Araki, Kazutaka
AU  - Araki K
AD  - Molecular Profiling Research Center for Drug Discovery, National Institute of 
      Advanced Industrial Science and Technology , Tokyo 135-0064, Japan.
FAU - Kusano, Hidewo
AU  - Kusano H
AD  - Molecular Profiling Research Center for Drug Discovery, National Institute of 
      Advanced Industrial Science and Technology , Tokyo 135-0064, Japan.
FAU - Sasaki, Naoyuki
AU  - Sasaki N
AD  - Robotic Biology Institute, Inc. , Tokyo 135-0064, Japan.
FAU - Tanaka, Riko
AU  - Tanaka R
AD  - Molecular Profiling Research Center for Drug Discovery, National Institute of 
      Advanced Industrial Science and Technology , Tokyo 135-0064, Japan.
FAU - Hatta, Tomohisa
AU  - Hatta T
AD  - Robotic Biology Institute, Inc. , Tokyo 135-0064, Japan.
FAU - Fukui, Kazuhiko
AU  - Fukui K
AD  - Molecular Profiling Research Center for Drug Discovery, National Institute of 
      Advanced Industrial Science and Technology , Tokyo 135-0064, Japan.
FAU - Natsume, Tohru
AU  - Natsume T
AD  - Molecular Profiling Research Center for Drug Discovery, National Institute of 
      Advanced Industrial Science and Technology , Tokyo 135-0064, Japan.
AD  - Robotic Biology Institute, Inc. , Tokyo 135-0064, Japan.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20160715
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (Sulfhydryl Compounds)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Cells, Cultured
MH  - Cysteine/*metabolism
MH  - *Homeostasis
MH  - Humans
MH  - *Oxidation-Reduction
MH  - *Oxidative Stress
MH  - Proteomics
MH  - Sulfhydryl Compounds/metabolism
OTO - NOTNLM
OT  - cysteine
OT  - oxidation
OT  - proteomics
OT  - quantification
OT  - redox
EDAT- 2016/06/29 06:00
MHDA- 2017/09/26 06:00
CRDT- 2016/06/29 06:00
PHST- 2016/06/29 06:00 [entrez]
PHST- 2016/06/29 06:00 [pubmed]
PHST- 2017/09/26 06:00 [medline]
AID - 10.1021/acs.jproteome.6b00087 [doi]
PST - ppublish
SO  - J Proteome Res. 2016 Aug 5;15(8):2548-59. doi: 10.1021/acs.jproteome.6b00087. 
      Epub 2016 Jul 15.