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Musculoskeletal Injuries and Conditions: From Pathophysiology to Novel Therapeutic Approaches

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (31 July 2025) | Viewed by 618

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Guest Editor
Center for Shockwave Medicine and Tissue Engineering, Kaohsiung Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Kaohsiung 833, Taiwan
Interests: shockwave medicine; translational research; cell therapy; regeneration medicine
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Special Issue Information

Dear Colleagues,

This Special Issue aims to focus on the pathophysiology, diagnosis, and treatment of musculoskeletal injuries and conditions affecting the joints, cartilage, bones, tendons, and ligaments. We welcome the submission of original research and reviews that explore molecular mechanisms, inflammation, tissue degeneration, fibrosis, and biomechanical alterations. Submissions addressing innovative diagnostic tools, regenerative medicine, molecular and cellular therapies, tissue engineering, and translational research are highly encouraged. Studies on preclinical models, biomarkers, and cutting-edge imaging techniques to elucidate the molecular mechanism of diseases are also of interest. By highlighting multidisciplinary approaches, this Special Issue aims to bridge the gap between diseases and molecular mechanisms, driving progress in the formation, prevention, management, and treatment of musculoskeletal conditions. Researchers are invited to contribute to this Special Issue to help advance this dynamic field.

Dr. Jai-Hong Cheng
Guest Editor

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Keywords

  • musculoskeletal disorder
  • pathophysiology
  • diagnosis
  • biomarkers
  • regenerative medicine

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Published Papers (1 paper)

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19 pages, 2024 KB  
Article
Immunoglobulin G Subclass-Specific Glycosylation Changes in Rheumatoid Arthritis
by Dániel Szabó, Balázs Gyebrovszki, Eszter Szarka, Felícia Auer, Bernadette Rojkovich, György Nagy, András Telekes, Károly Vékey, László Drahos, András Ács and Gabriella Sármay
Int. J. Mol. Sci. 2025, 26(19), 9626; https://doi.org/10.3390/ijms26199626 - 2 Oct 2025
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Abstract
Rheumatoid arthritis (RA) is the most common inflammatory polyarthritis. In addition, 60–80% of patients express anti-citrullinated protein antibodies (ACPAs), which serve as a diagnostic marker for RA. The effector functions of these autoantibodies can be heavily affected by the N-glycosylation of their Fc [...] Read more.
Rheumatoid arthritis (RA) is the most common inflammatory polyarthritis. In addition, 60–80% of patients express anti-citrullinated protein antibodies (ACPAs), which serve as a diagnostic marker for RA. The effector functions of these autoantibodies can be heavily affected by the N-glycosylation of their Fc region. Here we present a comparison of the Fc N-glycosylation of ACPA IgG to that of non-ACPA IgG from the same patients, and of healthy controls, in an IgG isoform-specific manner. We isolated ACPA and normal serum IgG, digested by trypsin, and separated the resulting peptide mixture by a reversed-phase nanoLC coupled to a Bruker Maxis II Q-TOF, and determined the relative abundance of glycoforms. The paired analysis of galactosylation and sialylation of the IgG subclasses of ACPA and non-ACPA IgG has shown a significant, moderate negative correlation with the inflammatory markers, the level of C-reactive protein (CRP) and erythrocyte sedimentation rate (ESR), as well as with rheuma-factor (RF), but not with the disease activity score (DAS) or cyclic citrullinated peptide specific antibodies (anti-CCP). However, we detected a significant negative correlation between glycosylation and DAS in the non-ACPA IgG fractions. Furthermore, the isoform-specific analysis revealed additional insight into the changes of the glycosylation features of IgG in RA: changes in the frequencies of the bisecting GlcNAc unit between sample groups could be explained by only the IgG1 isoform; while invariance in fucosylation is the result of the superposition of two isoforms with opposite changes. These results highlight the importance of analyzing immunoglobulin glycosylation in an isoform-specific manner. Full article
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