Abstract
Monitoring protein dynamics, compared to measuring static protein expression profiles taken with snapshot evaluations, have recently been the focus of proteomics studies examining tissue or blood samples where time course changes occur. Using deuterium oxide (2H2O) to label amino acids is a useful method to monitor protein turnover rates. The synthesis rate for individual proteins is calculated from the rate of 2H incorporation into specific proteins analyzed by high resolution MS. In this issue, Wang and colleagues measured the plasma protein turnover dynamics in healthy humans by in vivo 2H2O labeling [Wang, D. et al., Proteomics Clin. Appl. 2014, 8, 610-619]. The authors developed and validated a safe and accessible 2H2O administration protocol to record the turnover dynamics of 542 plasma proteins using MS. Their study demonstrates a promising new way to evaluate plasma protein dynamics in clinical trials where such knowledge could help for prognosis and evaluating treatment efficacy.
Original language | English (US) |
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Pages (from-to) | 477-479 |
Number of pages | 3 |
Journal | Proteomics - Clinical Applications |
Volume | 8 |
Issue number | 7-8 |
DOIs |
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State | Published - Aug 2014 |
Externally published | Yes |
Keywords
- Deuterium oxide
- MS
- Matrix metalloproteinase
- Protein
ASJC Scopus subject areas
- Clinical Biochemistry