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

doi:10.1007/s00216-012-5953-3

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

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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 language	English
Pages (from-to)	2397-2402
Number of pages	6
Journal	Analytical and Bioanalytical Chemistry
Volume	403
Issue number	8
DOIs	https://doi.org/10.1007/s00216-012-5953-3
State	Published - Jun 2012

Keywords

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

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

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).",

keywords = "Protein kinetics, Protein metabolism, Protein turnover, Respiratory distress syndrome, SRM, Selected reaction monitoring",

author = "Bereman, {Michael S.} and Tomazela, {Daniela M.} and Heins, {Hillary S.} and Manuela Simonato and Cogo, {Paola E.} and Aaron Hamvas and Patterson, {Bruce W.} and Cole, {F. Sessions} and MacCoss, {Michael J.}",

note = "Funding Information: 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).",

year = "2012",

month = jun,

doi = "10.1007/s00216-012-5953-3",

language = "English",

volume = "403",

pages = "2397--2402",

journal = "Analytical and Bioanalytical Chemistry",

issn = "1618-2642",

number = "8",

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T1 - A method to determine the kinetics of multiple proteins in human infants with respiratory distress syndrome

AU - Bereman, Michael S.

AU - Tomazela, Daniela M.

AU - Heins, Hillary S.

AU - Simonato, Manuela

AU - Cogo, Paola E.

AU - Hamvas, Aaron

AU - Patterson, Bruce W.

AU - Cole, F. Sessions

AU - MacCoss, Michael J.

N1 - Funding Information: 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).

PY - 2012/6

Y1 - 2012/6

N2 - 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).

AB - 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).

KW - Protein kinetics

KW - Protein metabolism

KW - Protein turnover

KW - Respiratory distress syndrome

KW - SRM

KW - Selected reaction monitoring

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DO - 10.1007/s00216-012-5953-3

M3 - Article

C2 - 22526637

AN - SCOPUS:84863724947

SN - 1618-2642

VL - 403

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EP - 2402

JO - Analytical and Bioanalytical Chemistry

JF - Analytical and Bioanalytical Chemistry

IS - 8

ER -

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

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Keywords

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