PMID- 30367882
OWN - NLM
STAT- MEDLINE
DCOM- 20191108
LR  - 20191108
IS  - 1096-0309 (Electronic)
IS  - 0003-2697 (Linking)
VI  - 564-565
DP  - 2019 Jan 1
TI  - Characterization of residue-specific glutathionylation of CSF proteins in 
      multiple sclerosis - A MS-based approach.
PG  - 108-115
LID - S0003-2697(18)30942-4 [pii]
LID - 10.1016/j.ab.2018.10.015 [doi]
AB  - Reduction of a disulfide linkage between cysteine residues in proteins, a 
      standard step in the preanalytical preparation of samples in conventional 
      proteomics approach, presents a challenge to characterize S-glutathionylation of 
      proteins. S-glutathionylation of proteins has been reported in medical conditions 
      associated with high oxidative stress. In the present study, we attempted to 
      characterize glutathionylation of CSF proteins in patients with multiple 
      sclerosis which is associated with high oxidative stress. Using the 
      nano-LC/ESI-MS platform, we adopted a modified proteomics approach and a targeted 
      database search to investigate glutathionylation at the residue level of CSF 
      proteins. Compared to patients with Intracranial hypertension, the following CSF 
      proteins: Extracellular Superoxide dismutase (ECSOD) at Cys195, alpha1-antitrypsin 
      (A1AT) at Cys232, Phospholipid transfer protein (PLTP) at Cys318, 
      Alpha-2-HS-glycoprotein at Cys340, Ectonucleotide pyrophosphate (ENPP-2) at 
      Cys773, Gelsolin at Cys304, Interleukin-18 (IL-18) at Cys38 and Ig heavy chain V 
      III region POM at Cys22 were found to be glutathionylated in patients with 
      multiple sclerosis during a relapse. ECSOD, A1AT, and PLTP were observed to be 
      glutathionylated at the functionally important cysteine residues. In conclusion, 
      in the present study using a modified proteomics approach we have identified and 
      characterized glutathionylation of CSF proteins in patients with multiple 
      sclerosis.
CI  - Copyright (c) 2018 Elsevier Inc. All rights reserved.
FAU - Srivastava, Deepsikha
AU  - Srivastava D
AD  - Division of Molecular Medicine, Clinical Proteomics Unit, St. John's Research 
      Institute, St. John's National Academy of Health Sciences, Bangalore, 560034, 
      India.
FAU - Kukkuta Sarma, Gosala Raja
AU  - Kukkuta Sarma GR
AD  - Department of Neurology, St. John's Hospital, St. John's National Academy of 
      Health Sciences, Bangalore, 560034, India.
FAU - Dsouza, Delon Snehal
AU  - Dsouza DS
AD  - Department of Neurology, St. John's Hospital, St. John's National Academy of 
      Health Sciences, Bangalore, 560034, India.
FAU - Muralidharan, Monita
AU  - Muralidharan M
AD  - Division of Molecular Medicine, Clinical Proteomics Unit, St. John's Research 
      Institute, St. John's National Academy of Health Sciences, Bangalore, 560034, 
      India.
FAU - Srinivasan, Krishnamachari
AU  - Srinivasan K
AD  - Department of Psychiatry, St. John's Medical College and Hospital, St. John's 
      National Academy of Health Sciences, Bangalore, 560034, India.
FAU - Mandal, Amit Kumar
AU  - Mandal AK
AD  - Division of Molecular Medicine, Clinical Proteomics Unit, St. John's Research 
      Institute, St. John's National Academy of Health Sciences, Bangalore, 560034, 
      India. Electronic address: amit@sjri.res.in.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20181024
PL  - United States
TA  - Anal Biochem
JT  - Analytical biochemistry
JID - 0370535
RN  - GAN16C9B8O (Glutathione)
SB  - IM
MH  - Chromatography, Liquid
MH  - Glutathione/cerebrospinal fluid
MH  - Humans
MH  - Multiple Sclerosis/cerebrospinal fluid/*metabolism
MH  - Oxidative Stress/physiology
MH  - Protein Processing, Post-Translational
MH  - Proteomics/*methods
MH  - Spectrometry, Mass, Electrospray Ionization/*methods
OTO - NOTNLM
OT  - Cerebrospinal fluid
OT  - Glutathione
OT  - Multiple sclerosis
OT  - Oxidative stress
OT  - Proteomics
OT  - Targeted database
EDAT- 2018/10/28 06:00
MHDA- 2019/11/09 06:00
CRDT- 2018/10/28 06:00
PHST- 2018/09/04 00:00 [received]
PHST- 2018/10/12 00:00 [revised]
PHST- 2018/10/14 00:00 [accepted]
PHST- 2018/10/28 06:00 [pubmed]
PHST- 2019/11/09 06:00 [medline]
PHST- 2018/10/28 06:00 [entrez]
AID - S0003-2697(18)30942-4 [pii]
AID - 10.1016/j.ab.2018.10.015 [doi]
PST - ppublish
SO  - Anal Biochem. 2019 Jan 1;564-565:108-115. doi: 10.1016/j.ab.2018.10.015. Epub 
      2018 Oct 24.