ArticleThe Journal of biological chemistry2011
Exosite interactions impact matrix metalloproteinase collagen specificities.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Dysregulation of autophagy during photoaging reduce oxidative stress and inflammatory damage caused by UV.Frontiers in pharmacology · 2025Review
- Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease.International journal of molecular sciences · 2023Review
- Crustacean Proteases and Their Application in Debridement.Tropical life sciences research · 2020Article
- Anti-fibrotic Actions of Equine Interleukin-10 on Transforming Growth Factor-Beta1-Stimulated Dermal Fibroblasts Isolated From Limbs of Horses.Frontiers in veterinary science · 2020Article
- Structural studies of the MMP-3 interaction with triple-helical collagen introduce new roles for the enzyme in tissue remodelling.Scientific reports · 2019Article
- Anti‑photoaging effect of fermented agricultural by‑products on ultraviolet B‑irradiated hairless mouse skin.International journal of molecular medicine · 2019Article
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates.Chemical communications (Cambridge, England) · 2018Article
- Therapeutic Potential of Matrix Metalloproteinase Inhibition in Breast Cancer.Journal of cellular biochemistry · 2017Review
- Second Generation Triple-Helical Peptide Inhibitors of Matrix Metalloproteinases.Journal of medicinal chemistry · 2017Article
- Matrix Metalloproteinases in Myocardial Infarction and Heart Failure.Progress in molecular biology and translational science · 2017Review
- Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.Scientific reports · 2016Article
- Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Frontiers in bioscience (Landmark edition) · 2015Review
- Collagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical Substrates.Biochemistry · 2015Article
- Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analogues.Chembiochem : a European journal of chemical biology · 2015Article
- Transient collagen triple helix binding to a key metalloproteinase in invasion and development.Structure (London, England : 1993) · 2015Article
- The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.The Journal of biological chemistry · 2014Article
- Biophysical studies of matrix metalloproteinase/triple-helix complexes.Advances in protein chemistry and structural biology · 2014Review
- Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- The synthesis and application of Fmoc-Lys(5-Fam) building blocks.Biopolymers · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
Members of the matrix metalloproteinase (MMP) family selectively cleave collagens in vivo. However, the substrate structural determinants that facilitate interaction with specific MMPs are not well defined. We hypothesized that type I-III collagen sequences located N- or C-terminal to the physiological cleavage site mediate substrate selectivity among MMP-1, MMP-2, MMP-8, MMP-13, and MMP-14/membrane-type 1 (MT1)-MMP. The enzyme kinetics for hydrolysis of three fluorogenic triple-helical peptides (fTHPs) was evaluated herein. The first fTHP contained consensus residues 769-783 from type I-III collagens, the second inserted α1(II) collagen residues 763-768 N-terminal to the consensus sequence, and the third inserted α1(II) collagen residues 784-792 C-terminal to the consensus sequence. Our analyses showed that insertion of the C-terminal residues significantly increased k(cat)/K(m) and k(cat) for MMP-1. MMP-13 showed the opposite behavior with a decreased k(cat)/K(m) and k(cat) and a greatly improved K(m) in response to the C-terminal residues. Insertion of the N-terminal residues enhanced k(cat)/K(m) and k(cat) for MMP-8 and MT1-MMP. For MMP-2, the C-terminal residues enhanced K(m) and dramatically decreased k(cat), resulting in a decrease in the overall activity. These changes in activities and kinetic parameters represented the collagen preferences of MMP-8, MMP-13, and MT1-MMP well. Thus, interactions with secondary binding sites (exosites) helped direct the specificity of these enzymes. However, MMP-1 collagen preferences were not recapitulated by the fTHP studies. The preference of MMP-1 for type III collagen appears to be primarily based on the flexibility of the hydrolysis site of type III collagen compared with types I and II. Further characterization of exosite determinants that govern interactions of MMPs with collagenous substrates should aid the development of pharmacotherapeutics that target individual MMPs.
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