By Sameh Magdeldin
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Extra info for Recent Advances Proteomics Research
When the ESI trap and quadrupole instruments were tested for the accuracy and precision of isotope distribution, the ion-trap MS performed better than the SIM quadrupole MS. 5772/61776 had greater precision than MALDI-TOF MS and the accuracy of the quadrupole measurement was improved when it was operated in a profile scan mode. When applied to protein turnover studies, the high resolution of MALDI-TOF MS allows accurate quantification of 2H enrichment of tryptic peptides . The traditional proteomics methods coupled with MALDI-TOF MS-assisted isotope distribution analysis greatly ad‐ vanced protein turnover studies in a mixture of proteins.
Consistent with previous studies , we found that similar to the heart, the turnover rates of all analyzed mitochondrial brain proteins had much slower turnover rates compared to those in the liver. 0 0 10 20 30 40 50 60 0 10 Time (day) 20 30 40 50 60 Time (day) Figure 5. Comparison of half-lives of brain and heart mitochondrial proteins. To test the effect of heart failure on the stability of cardiac mitochondrial proteins, we utilized our 2H2O approach to measure mitochondrial proteome dynamics in a well-established rat model of heart failure induced by chronic transverse aortic constriction (TAC) .
This was due to bidirectional changes in the synthesis rate of different mitochondrial proteins. 5772/61776 fatty acid oxidation, electron transport chain, and ATP synthesis, while it decreased the turnover of other proteins, including pyruvate dehydrogenase subunit in IFM, but not in SSM. The study of proteome dynamics suggested that reduced respiratory capacity in IFM might be related to increased degradation of several IFM proteins involved in fatty acid oxidation and ETC. Interestingly, proteins with destabilizing N-terminal amino acids of mature proteins exhibited shorter half-lives compared to those with stabilizing N-terminal amino acids.