Abstract
Background: HIV-associated neurocognitive disorders (HAND) has been associated with the up-regulation of various oxidative stress pathways. Previous studies have linked the neuronal damage observed in individuals diagnosed with HAND to increased nitrotyrosine modification of neuronal proteins. Materials and methods: Tyrosine nitration alters protein structure and function, affects biological half-life, and potentially prevents the phosphorylation of key tyrosine residues involved in signal transduction pathways. Therefore, in this study we employed proteomics-based experimental approaches to investigate nitrotyrosine-modified proteins in pooled cerebrospinal fluid (CSF) of individuals diagnosed with HAND. To identify specific nitrotyrosine-modified proteins in the CSF of individuals diagnosed with HAND, affinity purification and high-performance tandem mass spectrometry are utilized in a "bottom-up" proteomics approach. Results: From tandem mass spectrometric analysis, we identified major proteins that underwent nitration as a result of nitro-oxidative stress in the CSF of individuals diagnosed with HAND. We also utilized analytical and biochemical techniques to characterize the expression and modification site of in vivo nitrated lipocalin-type prostaglandin-D synthase in HAND CSF.
Original language | English (US) |
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Pages (from-to) | 29-41 |
Number of pages | 13 |
Journal | Clinical Proteomics |
Volume | 6 |
Issue number | 1-2 |
DOIs | |
State | Published - Jun 2010 |
Keywords
- BSA
- CSF
- HAND
- HIV
- Oxidative stress
- Tyrosine nitration
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Clinical Biochemistry