Glycation cross-links inhibit matrix metalloproteinase-2 activation in vascular smooth muscle cells cultured on collagen lattice
Open accessAbstract
Aims/hypothesis Extracellular matrix glycation has been proposed to contribute to the arterial stiffness observed in aging and diabetes. We examined whether matrix protein glycation regulates the proleolytic process through the manipulation of matrix metalloproteinases (MMPs) activation, using collagen fibrils model.Methods Vascular smooth muscle cells were cultured on control or glycated collagen fibrils. Matrix metalloproteinase-2 activation and the production of tissue inhibitors of metalloproteinase (TIMPs) were measured in the conditioned medium by using gelatin zymography and immunoblotting. Membrane type 1 matrix metalloproteinase (MT1-MMP) expression was also measured in cell lysates.Results When smooth muscle cells were cultured on collagen fibrils, pro-MMP-2 processing to active form was observed in the conditioned medium in coincidence with the increased MT1-MMP expression and the suppressed TIMP-2 production. Culturing smooth muscle cells on glycated collagen fibrils inhibited MMP-2 activation and attenuated MT1-MMP expression without the alteration of TIMP-2 production compared with control fibrils, indicating the possible mechanism of the suppression of MT1-MMP expression for the inhibition of MMP-2 activation on glycated collagen fibrils. Inclusion of aminoguanidine, an inhibitor of cross-linking formation, during collagen glycation restored the MMP-2 activation, suggesting the role of cross-links on the inhibition of MMP-2 activation.Conclusion/interpretation These observations suggest that glycation-induced cross-linking formation in interstitial collagen contributes to arterial stiffness in aging and diabetes through the manipulation of matrix metalloproteinase activation along with the reduction of the susceptibility to proteolytic enzymes.
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Endothelial cell dysfunction strongly affects arterial stiffness through cellular adhesion molecules, matrix metalloproteinases and collagen molecules.
“EC dysfunction has been shown to strongly affect arterial stiffness via cellular adhesion molecules (CAMs), matrix metalloproteinases (MMPs) and collagen molecules (COLs)67–71.”
From An inflammatory aging clock (iAge) based on deep learning tracks multimorbidity, immunosenescence, frailty and cardiovascular aging (2021) · cites this paper as [70]
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- Authors
- Kuzuya, M., Asai, T., Kanda, S., Maeda, K., Cheng, X. W., & Iguchi, A.
- Affiliations
- Nagoya University (JP)
- Venue
- Diabetologia
- Published
- 2001-04-06
- Volume
- 44
- Issue
- 4
- Pages
- 433-436
- ISSN
- 0012-186X (ISSN-L)
- 1432-0428
- OpenAlex
- W2025795193
- Cited by
- 79
- References
- 8
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 2 · 2022: 3 · 2021: 3 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 1 · 2015: 3 · 2014: 7 · 2013: 3 · 2012: 4
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Diabetologia (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Keywords
- collagen cross-links, vascular smooth muscle cells, MT1-MMP, TIMP-2, arterial stiffness, diabetes mellitus, aging, aminoguanidine, collagen fibrils, proteolysis
- MeSH terms
- Cell Adhesion, Cells, Cultured, Collagen, Cross-Linking Reagents, Culture Media, Enzyme Activation, Gelatin, Glycosylation, Guanidines, Humans, Muscle, Smooth, Vascular, Extracellular Matrix Proteins, Tissue Inhibitor of Metalloproteinase-2, Matrix Metalloproteinase 2
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