ArticleScientific reports2018
COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Analysis of cranial tenocyte heterogeneity reveals a role for Wnt signaling in tendon attachments.Development (Cambridge, England) · 2026Article
- COMP Is a Biomarker of Cartilage Destruction, Extracellular Matrix and Vascular Remodeling and Tissue Repair.International journal of molecular sciences · 2025Review
- Expression of thrombospondin-4 in the infrapatellar fat pad and synovial fluid - potential contribution to osteoarthritis pain.Arthritis research & therapy · 2025Article
- Evaluation and refinement of all-atom force fields for reproducing collagen structure and dynamics.Biophysical journal · 2025Article
- Thrombospondins: Conserved mediators and modulators of metazoan extracellular matrix.International journal of experimental pathology · 2024Review
- Pathophysiological roles of thrombospondin-4 in disease development.Seminars in cell & developmental biology · 2024Review
- Generation of Matrix Degradation Products Using an In Vitro MMP Cleavage Assay.International journal of molecular sciences · 2022Article
- Collagen's primary structure determines collagen:HSP47 complex stoichiometry.The Journal of biological chemistry · 2021Article
- COMP and TSP-4: Functional Roles in Articular Cartilage and Relevance in Osteoarthritis.International journal of molecular sciences · 2021Article
- Incidental Finding of Elevated Serum Cartilage Oligomeric Matrix Protein (sCOMP) in Knee Osteoarthritis Patient with Undiagnosed Colon Cancer: A Case Report.International medical case reports journal · 2021Article
- Alterations in proteome of human sclera associated with primary open-angle glaucoma involve proteins participating in regulation of the extracellular matrix.Molecular vision · 2020Article
- Reversible Covalent End-Capping of Collagen Model Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Thrombospondin 1 and Its Diverse Roles as a Regulator of Extracellular Matrix in Fibrotic Disease.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Review
- The Expression of Thrombospondin-4 Correlates with Disease Severity in Osteoarthritic Knee Cartilage.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
COMP (cartilage oligomeric matrix protein) is a member of the thrombospondin family and forms homopentamers as well as mixed heterooligomers with its closely related family member TSP-4. COMP is long known to bind to collagens and to influence collagen fibril formation. Recent work indicates that already intracellular interaction with collagen is important for collagen secretion. However, the exact binding site of COMP on the collagen triple helix has not been described up to now. In this study we have identified a GXKGHR motif on the collagen II helix to bind to COMP, using a recombinantly expressed collagen II peptide library. This binding sequence is conserved throughout evolution and we demonstrate that TSP-4 binds to the same sequence. The identified binding motif overlaps with the recognition sites of many other collagen-binding partners (e.g. PEDF, Heparin) and also spans the lysine residues, which form collagen cross-links. COMP might thereby protect collagen helices from premature modification and cross-linking. Interestingly, this motif is only found in classical fibrillar collagens, although COMP is known to also bind other types. This might indicate that COMP has a unique interface for fibrillar collagens, thus making it an interesting target for the development of antifibrotic drugs.
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Registered trials
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