Affiliation: | 1. Genos Glycoscience Research Laboratory, Zagreb, Croatia;2. PolyOmica, Het Vlaggeschip 61, 5237 PA ‘s-Hertogenbosch, The Netherlands;3. The Glycomics and Glycoproteomics Group, Center for Proteomics and Metabolomics, Leiden University Medical Center, The Netherlands;4. Department of Twin Research and Genetic Epidemiology, King''s College London, London, UK;5. NIHR Biomedical Research Centre at Guy''s and St Thomas'' Foundation Trust, London SE1 9RT, UK;6. Pain Therapy Service, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy;7. SIMPAR Group, Italy;8. Anesthesia, Intensive Care and Pain Service, Parma Hospital, Parma, Italy;9. Department of Medicine and Surgery, University of Parma, Parma, Italy;10. Carolinas Pain Institute, Winston Salem, NC, USA;11. St. Catherine Specialty Hospital, Zabok/Zagreb, Croatia;12. J J Strossmayer University of Osijek, School of Medicine, Osijek, Croatia;13. University of Split, School of Medicine, Split, Croatia;14. Eberly College of Science, The Pennsylvania State University, University Park, USA;15. Children''s Hospital Srebrnjak, Zagreb, Croatia;p. Department of Anesthesiology and Multidisciplinary Pain Center, Ziekenhuis Oost-Limburg, Genk, Belgium;q. Anesthesia and Intensive Care Service - IRCCS MultiMedica Hospital, Sesto San Giovanni, Milano, Italy;r. University of Zagreb, Faculty of Pharmacy and Biochemistry, Zagreb, Croatia |
Abstract: | BackgroundLow back pain (LBP) is the symptom of a group of syndromes with heterogeneous underlying mechanisms and molecular pathologies, making treatment selection and patient prognosis very challenging. Moreover, symptoms and prognosis of LBP are influenced by age, gender, occupation, habits, and psychological factors. LBP may be characterized by an underlying inflammatory process. Previous studies indicated a connection between inflammatory response and total plasma N-glycosylation. We wanted to identify potential changes in total plasma N-glycosylation pattern connected with chronic low back pain (CLBP), which could give an insight into the pathogenic mechanisms of the disease.MethodsPlasma samples of 1128 CLBP patients and 760 healthy controls were collected in clinical centers in Italy, Belgium and Croatia and used for N-glycosylation profiling by hydrophilic interaction ultra-performance liquid chromatography (HILIC-UPLC) after N-glycans release, fluorescent labeling and clean-up. Observed N-glycosylation profiles have been compared with a cohort of 126 patients with acute inflammation that underwent abdominal surgery.ResultsWe have found a statistically significant increase in the relative amount of high-branched (tri-antennary and tetra-antennary) N-glycan structures on CLBP patients' plasma glycoproteins compared to healthy controls. Furthermore, relative amounts of disialylated and trisialylated glycan structures were increased, while high-mannose and glycans containing bisecting N-acetylglucosamine decreased in CLBP.ConclusionsObserved changes in CLBP on the plasma N-glycome level are consistent with N-glycosylation changes usually seen in chronic inflammation.General significanceTo our knowledge, this is a first large clinical study on CLBP patients and plasma N-glycome providing a new glycomics perspective on potential disease pathology. |