gms | German Medical Science

German Congress of Orthopedic and Trauma Surgery (DKOU 2017)

24.10. - 27.10.2017, Berlin

Discovery of glycan biomarkers in serum of osteonecrosis of the femoral head

Meeting Abstract

  • presenting/speaker Peng Chen - Guangzhou University of Chinese Medicine, Guangzhou, China
  • Ting Song - Department of Chemistry, University of California Davis, Davis, United States
  • Haibin Wang - Guangzhou University of Chinese Medicine, Guangzhou, China
  • Wei He - Guangzhou University of Chinese Medicine, Guangzhou, China
  • Carlito B Lebrilla - Department of Chemistry, University of California Davis, Davis, United States

Deutscher Kongress für Orthopädie und Unfallchirurgie (DKOU 2017). Berlin, 24.-27.10.2017. Düsseldorf: German Medical Science GMS Publishing House; 2017. DocIN14-270

doi: 10.3205/17dkou034, urn:nbn:de:0183-17dkou0342

Published: October 23, 2017

© 2017 Chen et al.
This is an Open Access article distributed under the terms of the Creative Commons Attribution 4.0 License. See license information at http://creativecommons.org/licenses/by/4.0/.


Outline

Text

Objectives: We aimed to examine the serum glycosylation alteration in the development of steroid-induced 0steonecrosis of the femoral head (SONFH) and identify N-glycan as the potential biomarkers in diagnosing SONFH.

Methods: A training set containing 27 serum samples from steroid induced ONFH patients and 25 from gender and age matched controls were collected and used. Glycomic and site-specific glycosylation of immunoglobulins are examined for potential markers. LC-MS is used for the global glycomic profiling of the serum. LC-MS/MS using multiple reaction monitoring (MRM) is used for quantitating site-specific glycosylation of serum immunoglobulins.

Results: Results: The glycomic analysis yielded 14 N-glycan compositions and MRM yielded 8 glycopeptides that were altered between cases and controls with statistical significance. The increase of the non-sialylated, non-fucosylated N-glycans and decrease of the fucosylated Nglycans are associated with the development of ONFH. The best N-glycan marker candidate is N5410 (P<0.0001, AUC=0.85). An additional nine N-glycan and three glycopeptides were found to be promising candidates.

Conclusion: Glycosylation is a post-translational protein modification that appears to be affected by ONFH. The results are consistent with recent reports that specific glycosylation profiles are related to various pathological states. Further studies with a testing set will provide validation of these potential markers.