ArticleThe Journal of biological chemistry2012
Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 113 citations in OpenAlex.
- Matrix metalloproteinase-mediated degradation governs angioarchitecture within poly(ethylene Glycol) hydrogels.Acta biomaterialia · 2026Article
- Reversing ABCB1-Mediated Multidrug Resistance in Colorectal Cancer: electroacupuncture shows therapeutic potentialJournal of pharmacopuncture · 2026Article
- Antagonistic SMAD2/3 control of TIMP-1, VEGF-A, and hypoxia signaling in myofibroblasts shapes histotype-specific angiogenesis in lung cancer.Cell death & disease · 2026Article
- MMPs at Work: Deciphering Their Role in the Cellular Mechanisms of Orthodontic Tooth Movement.International journal of molecular sciences · 2026Review
- Review
- Bioinformatics mining and experimental validation of prognostic biomarkers in colorectal cancer.Discover oncology · 2025Article
- Tissue inhibitor of metalloproteinase 1 promotes ferroptosis and suppresses prostate cancer metastasis.The Journal of biological chemistry · 2025Article
- Matrix metalloproteinase-driven epithelial-mesenchymal transition: implications in health and disease.Journal of translational medicine · 2025Review
- In silico research of coagulation- and fibrinolysis-related genes for predicting prognosis of clear cell renal cell carcinoma.Translational andrology and urology · 2025Article
- Nano-Drug Delivery Systems Targeting MMPs: A Promising Treatment for Gliomas.International journal of nanomedicine · 2025Review
- Engineered TIMP2 with narrow MMP-9 specificity is an effective inhibitor of invasion and proliferation of triple-negative breast cancer cells.The Journal of biological chemistry · 2024Article
- Bioinformatics analysis-based mining of potential markers for inflammatory bowel disease and their immune relevance.Translational cancer research · 2024Article
- Identification and experimental verification of a biomarker by combining the unfolded protein response with the immune cells in colon cancer.BMC cancer · 2024Article
- Article
- Tissue Inhibitors of Metalloproteinase 1 (TIMP-1) and 3 (TIMP-3) as New Markers of Acute Kidney Injury After Massive Burns.Medical science monitor : international medical journal of experimental and clinical research · 2024Article
- Correlation of Experimental and Calculated Inhibition Constants of Protease Inhibitor Complexes.International journal of molecular sciences · 2024Article
- Article
- Cell mediated ECM-degradation as an emerging tool for anti-fibrotic strategy.Cell regeneration (London, England) · 2023Review
- Designed Loop Extension Followed by Combinatorial Screening Confers High Specificity to a Broad Matrix MetalloproteinaseInhibitor.Journal of molecular biology · 2023Article
- Estimation of hub genes and exploration of multi-omics level alterations in the landscape of lung adenocarcinoma.American journal of translational research · 2023Article
14 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Matrix metalloproteinase 10 (MMP-10, stromelysin-2) is a secreted metalloproteinase with functions in skeletal development, wound healing, and vascular remodeling; its overexpression is also implicated in lung tumorigenesis and tumor progression. To understand the regulation of MMP-10 by tissue inhibitors of metalloproteinases (TIMPs), we have assessed equilibrium inhibition constants (K(i)) of putative physiological inhibitors TIMP-1 and TIMP-2 for the active catalytic domain of human MMP-10 (MMP-10cd) using multiple kinetic approaches. We find that TIMP-1 inhibits the MMP-10cd with a K(i) of 1.1 × 10(-9) M; this interaction is 10-fold weaker than the inhibition of the similar MMP-3 (stromelysin-1) catalytic domain (MMP-3cd) by TIMP-1. TIMP-2 inhibits the MMP-10cd with a K(i) of 5.8 × 10(-9) M, which is again 10-fold weaker than the inhibition of MMP-3cd by this inhibitor (K(i) = 5.5 × 10(-10) M). We solved the x-ray crystal structure of TIMP-1 bound to the MMP-10cd at 1.9 Å resolution; the structure was solved by molecular replacement and refined with an R-factor of 0.215 (R(free) = 0.266). Comparing our structure of MMP-10cd·TIMP-1 with the previously solved structure of MMP-3cd·TIMP-1 (Protein Data Bank entry 1UEA), we see substantial differences at the binding interface that provide insight into the differential binding of stromelysin family members to TIMP-1. This structural information may ultimately assist in the design of more selective TIMP-based inhibitors tailored for specificity toward individual members of the stromelysin family, with potential therapeutic applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.