ArticlePloS one2013
The C-type lectin of the aggrecan G3 domain activates complement.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Structure and Function of Ocular Proteoglycans: Essential Proteins for Vision.International journal of molecular sciences · 2026Review
- COMP Is a Biomarker of Cartilage Destruction, Extracellular Matrix and Vascular Remodeling and Tissue Repair.International journal of molecular sciences · 2025Review
- Review
- The potential role of synovial cells in the progression and treatment of osteoarthritis.Exploration (Beijing, China) · 2023Review
- Proteomic Analysis of Synovial Fibroblasts and Articular Chondrocytes Co-Cultures Reveals Valuable VIP-Modulated Inflammatory and Degradative Proteins in Osteoarthritis.International journal of molecular sciences · 2021Article
- Review
- Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis.Experientia supplementum (2012) · 2021Article
- Review
- ADAMTS-9 in Mouse Cartilage Has Aggrecanase Activity That Is Distinct from ADAMTS-4 and ADAMTS-5.International journal of molecular sciences · 2019Article
- The cartilage-specific lectin C-type lectin domain family 3 member A (CLEC3A) enhances tissue plasminogen activator-mediated plasminogen activation.The Journal of biological chemistry · 2018Article
- Osteoarthritis and the Complement Cascade.Clinical medicine insights. Arthritis and musculoskeletal disorders · 2018Review
- Immune Contributions to Osteoarthritis.Current osteoporosis reports · 2017Review
- The complement system as a potential therapeutic target in rheumatic disease.Nature reviews. Rheumatology · 2017Review
- The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis.Arthritis research & therapy · 2016Article
- Emerging targets in osteoarthritis therapy.Current opinion in pharmacology · 2015Review
- Extracellular matrix regulation of inflammation in the healthy and injured spinal cord.Experimental neurology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Excessive complement activation contributes to joint diseases such as rheumatoid arthritis and osteoarthritis during which cartilage proteins are fragmented and released into the synovial fluid. Some of these proteins and fragments activate complement, which may sustain inflammation. The G3 domain of large cartilage proteoglycan aggrecan interacts with other extracellular matrix proteins, fibulins and tenascins, via its C-type lectin domain (CLD) and has important functions in matrix organization. Fragments containing G3 domain are released during normal aggrecan turnover, but increasingly so in disease. We now show that the aggrecan CLD part of the G3 domain activates the classical and to a lesser extent the alternative pathway of complement, via binding of C1q and C3, respectively. The complement control protein (CCP) domain adjacent to the CLD showed no effect on complement initiation. The binding of C1q to G3 depended on ionic interactions and was decreased in D2267N mutant G3. However, the observed complement activation was attenuated due to binding of complement inhibitor factor H to CLD and CCP domains. This was most apparent at the level of deposition of terminal complement components. Taken together our observations indicate aggrecan CLD as one factor involved in the sustained inflammation of the joint.
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