Abstract
We report a method to measure in vivo turnover of four proteins from sequential tracheal aspirates obtained from human newborn infants with respiratory distress syndrome using targeted proteomics. We detected enrichment for all targeted proteins approximately 3 h from the start of infusion of [5,5,5-2H3] leucine, secretion times that varied from 1.2 to 2.5 h, and half lives that ranged between 10 and 21 h. Complement factor B, a component of the alternative pathway of complement activation, had an approximately twofold-longer half-life than the other three proteins. In addition, the kinetics of mature and carboxy-terminal tryptic peptides from the same protein (surfactant protein B) were not statistically different (p = 0.49).
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Acknowledgments
The authors acknowledge financial support from the National Institutes of Health (R01 HL082747 F.S.C., A.H.) and R01 DK069386 (M.J.M.). M.S.B. acknowledges support from the Genome Training Grant (T32 HG000035).
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Published in the special issue Young Investigators in Analytical and Bioanalytical Science with guest editors S. Daunert, J. Bettmer, T. Hasegawa, Q. Wang and Y. Wei.
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Bereman, M.S., Tomazela, D.M., Heins, H.S. et al. A method to determine the kinetics of multiple proteins in human infants with respiratory distress syndrome. Anal Bioanal Chem 403, 2397–2402 (2012). https://doi.org/10.1007/s00216-012-5953-3
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DOI: https://doi.org/10.1007/s00216-012-5953-3