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| Content Provider | Springer Nature Link |
|---|---|
| Author | Aslan, Mutay |
| Copyright Year | 2010 |
| Abstract | To link the phenomena of inflammatory-induced increases in protein nitrotyrosine (NO2Tyr) derivatives to protein dysfunction and consequent pathological conditions, the evaluation of discrete NO2Tyr modifications on specific proteins must be undertaken. Mass spectrometric (MS) proteomics-based strategies allow for the identification of all individual proteins that are nitrated by separating tissue homogenates using 2D gel electrophoresis, detecting the nitrated proteins using an anti-NO2Tyr antibody, and then identifying the peptides generated during an in-gel proteolytic digest using matrix-assisted laser desorption ionization/time-of-flight (MALDI-TOF) MS. Actin, one of the most abundant proteins in eukaryotic cells, constitutes 5% or more of cell protein and serves with other cytoskeletal proteins as a critical target for nitration-induced functional impairment. Herein, examples of actin nitration detected under physiological conditions in various models of human disease or in clinically derived tissues are given and the impact that this post-translational protein modification can have on cell and organ function is discussed. |
| Starting Page | 65 |
| Ending Page | 74 |
| Page Count | 10 |
| File Format | |
| ISSN | 09394451 |
| Journal | Amino Acids |
| Volume Number | 42 |
| Issue Number | 1 |
| e-ISSN | 14382199 |
| Language | English |
| Publisher | Springer Vienna |
| Publisher Date | 2010-05-18 |
| Publisher Place | Vienna |
| Access Restriction | Subscribed |
| Subject Keyword | Nitrotyrosine Actin Reactive nitrogen species Reactive oxygen species Protein structure and function Biochemical Engineering Biochemistry Analytical Chemistry Neurobiology Proteomics Life Sciences |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Biochemistry Clinical Biochemistry |
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