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Characterization of trivalently crosslinked C-terminal telopeptide of type I collagen (CTX) species in human plasma and serum using high resolution mass spectrometry
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  • Justine Demeuse,
  • William Determe,
  • Elodie Grifnée,
  • Philippe Massonnet,
  • Matthieu Schoumacher,
  • Loreen Huyghebaert,
  • Thomas Dubrowski,
  • Stéphanie Peeters,
  • Caroline Le Goff,
  • Etienne Cavalier
Justine Demeuse
University of Liege

Corresponding Author:[email protected]

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William Determe
University of Liege
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Elodie Grifnée
Central University Hospital of Liege
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Philippe Massonnet
Central University Hospital of Liege
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Matthieu Schoumacher
University of Liege
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Loreen Huyghebaert
Central University Hospital of Liege
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Thomas Dubrowski
Central University Hospital of Liege
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Stéphanie Peeters
Central University Hospital of Liege
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Caroline Le Goff
Central University Hospital of Liege
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Etienne Cavalier
Central University Hospital of Liege
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Abstract

With an aging population, there has been significant progress in the discovery and measurement of bone turnover biomarkers since the 2000s, especially for monitoring skeletal diseases like osteoporosis. Multiple markers derived from type I collagen, such as CTX, NTX, PINP, and ICTP, have been developed. Extensive efforts have been devoted to characterizing these molecules; however, their complex crosslinked structures have posed significant analytical challenges, and to date, these biomarkers remain poorly characterized. Previous attempts at characterization involved gel-based separation methods and MALDI-TOF analysis on collagen peptides directly extracted from bone. However, using bone powder, while rich in collagen, does not represent the true structure of the peptides in the biofluids. In this study, our goal was to characterize plasma and serum CTX for subsequent LC-MS/MS method development. We extracted and characterized type I collagen peptides directly from human plasma and serum using a proteomics workflow that integrates preparative liquid chromatography, affinity chromatography, and high-resolution mass spectrometry. Subsequently, we successfully identified numerous CTX species, providing valuable insights into the characterization of these crucial biomarkers.
Submitted to PROTEOMICS
10 Mar 2024Review(s) Completed, Editorial Evaluation Pending
05 Jun 2024Reviewer(s) Assigned
20 Sep 2024Review(s) Completed, Editorial Evaluation Pending
20 Sep 2024Editorial Decision: Revise Minor
30 Sep 2024Review(s) Completed, Editorial Evaluation Pending
30 Sep 20242nd Revision Received
11 Oct 2024Editorial Decision: Accept