A method to determine the kinetics of multiple proteins in human infants with respiratory distress syndrome

Michael S. Bereman*, Daniela M. Tomazela, Hillary S. Heins, Manuela Simonato, Paola E. Cogo, Aaron Hamvas, Bruce W. Patterson, F. Sessions Cole, Michael J. MacCoss

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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- 2H 3] 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).

Original languageEnglish (US)
Pages (from-to)2397-2402
Number of pages6
JournalAnalytical and Bioanalytical Chemistry
Volume403
Issue number8
DOIs
StatePublished - Jun 2012

Keywords

  • Protein kinetics
  • Protein metabolism
  • Protein turnover
  • Respiratory distress syndrome
  • SRM
  • Selected reaction monitoring

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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