ArticleThe Journal of biological chemistry2014
The recognition of collagen and triple-helical toolkit peptides by MMP-13: sequence specificity for binding and cleavage.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Reversing detrimental effects of OA-related terminal maturation in high-throughput in vitro and biomimetic ex vivo human models.Arthritis research & therapy · 2026Article
- Matrix Metalloproteinase-13 Is an Unfavorable Prognostic Factor in Chordoma by Digesting Growth Inhibitory Collagens.Cancer medicine · 2026Article
- Structural basis for collagen recognition by theeLife · 2025Article
- The Coordinated Interplay Between MMP13 and Pro-Migratory MMPs in Collective Cell Migration of Zebrafish Keratocytes.International journal of molecular sciences · 2025Article
- Multiomic and electrophysiologic analyses reveal that an inherited MRC2 variant causes fibroblast dysfunction and increased atrial fibrillation susceptibility.American journal of physiology. Heart and circulatory physiology · 2025Article
- siRNA conjugate with high albumin affinity and degradation resistance for delivery and treatment of arthritis in mice and guinea pigs.Nature biomedical engineering · 2025Article
- Unveiling Matrix Metalloproteinase 13's Dynamic Role in Breast Cancer: A Link to Physical Changes and Prognostic Modulation.International journal of molecular sciences · 2025Review
- Gold Nanoparticles as a Tool to Detect Biomarkers in Osteoarthritis: New Insights.Indian journal of microbiology · 2025Article
- Effects of adipose allograft matrix on viability of humeral head cartilage and rotator cuff tendon.BMC musculoskeletal disorders · 2025Article
- ER procollagen storage defect without coupled unfolded protein response drives precocious arthritis.Life science alliance · 2024Article
- Circ_ST6GAL1-mediated competing endogenous RNA network regulates TGF-β1-stimulated matrix Metalloproteinase-13 expression via Runx2 acetylation in osteoblasts.Non-coding RNA research · 2024Article
- Mapping the Binding Sites of MMPs on Types II and III Collagens Using Triple-Helical Peptide Toolkits.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Transcriptome Profiling of Osteoblasts in a Medaka (Frontiers in cell and developmental biology · 2022Article
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- Peptides and Peptidomimetics as Inhibitors of Enzymes Involved in Fibrillar Collagen Degradation.Materials (Basel, Switzerland) · 2021Review
- Calcyclin (S100A6) Attenuates Inflammatory Response and Mediates Apoptosis of Chondrocytes in Osteoarthritis via the PI3K/AKT Pathway.Orthopaedic surgery · 2021Article
- Overview of MMP-13 as a Promising Target for the Treatment of Osteoarthritis.International journal of molecular sciences · 2021Review
- Multimerin 1 supports platelet function in vivo and binds to specific GPAGPOGPX motifs in fibrillar collagens that enhance platelet adhesion.Journal of thrombosis and haemostasis : JTH · 2021Article
- Impact of Digestive Inflammatory Environment and Genipin Crosslinking on Immunomodulatory Capacity of Injectable Musculoskeletal Tissue Scaffold.International journal of molecular sciences · 2021Article
- Leptin Induced TLR4 Expression via the JAK2-STAT3 Pathway in Obesity-Related Osteoarthritis.Oxidative medicine and cellular longevity · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Remodeling of collagen by matrix metalloproteinases (MMPs) is crucial to tissue homeostasis and repair. MMP-13 is a collagenase with a substrate preference for collagen II over collagens I and III. It recognizes a specific, well-known site in the tropocollagen molecule where its binding locally perturbs the triple helix, allowing the catalytic domain of the active enzyme to cleave the collagen α chains sequentially, at Gly(775)-Leu(776) in collagen II. However, the specific residues upon which collagen recognition depends within and surrounding this locus have not been systematically mapped. Using our triple-helical peptide Collagen Toolkit libraries in solid-phase binding assays, we found that MMP-13 shows little affinity for Collagen Toolkit III, but binds selectively to two triple-helical peptides of Toolkit II. We have identified the residues required for the adhesion of both proMMP-13 and MMP-13 to one of these, Toolkit peptide II-44, which contains the canonical collagenase cleavage site. MMP-13 was unable to bind to a linear peptide of the same sequence as II-44. We also discovered a second binding site near the N terminus of collagen II (starting at helix residue 127) in Toolkit peptide II-8. The pattern of binding of the free hemopexin domain of MMP-13 was similar to that of the full-length enzyme, but the free catalytic subunit bound none of our peptides. The susceptibility of Toolkit peptides to proteolysis in solution was independent of the very specific recognition of immobilized peptides by MMP-13; the enzyme proved able to cleave a range of dissolved collagen peptides.
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Registered trials
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