ArticleThe Journal of biological chemistry2020
Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 54 citations in OpenAlex.
- Enzymatic and non-enzymatic oxidation of fibrillar collagen.Redox report : communications in free radical research · 2026Review
- Proteomic signatures of equine dental tooth tissues in ageing and disease.Equine veterinary journal · 2026Article
- Age-related local versus systemic early phase wound healing dynamics following free gingival graft harvest.Journal of periodontology · 2026Article
- Serum Advanced Glycation End Products as Drivers of Poor Tendon Outcomes in Diabetes? An Emerging Hypothesis and Narrative Review.Endocrinology, diabetes & metabolism · 2026Review
- Atomic Force Microscopy Investigations of Collagen: From Single Molecules to Fibrils.Methods in molecular biology (Clifton, N.J.) · 2026Article
- In tendons, differing physiological requirements lead to distinct patterns of MMP-1 degradation.Scientific reports · 2025Article
- Short- and Medium-Term Surgical Outcomes of Tissue-Engineered Pulmonary Valve Replacement in Sheep.Tissue engineering and regenerative medicine · 2025Article
- Skeletal Muscle Aging: Enhancing Skeletal Muscle Integrity and Function as a Potential Pharmacological Approach.Pharmaceuticals (Basel, Switzerland) · 2025Review
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- The Combination of Two Small Molecules Improves Neurological Parameters and Extends the Lifespan of C3H Strain Female Mice.Brain and behavior · 2025Article
- Solid-State NMR Spectroscopy Investigation of Structural Changes of Mechanically Strained Mouse Tail Tendons.Journal of the American Chemical Society · 2025Article
- Engineered Age-Mimetic Breast Cancer Models Reveal Differential Drug Responses in Young and Aged Microenvironments.Advanced healthcare materials · 2025Article
- Poly(ADP-ribose) binding sites on collagen I fibrils for nucleating intrafibrillar bone mineral.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rapid LC-MS/MS Evaluation of Collagen and Elastin Crosslinks in Human and Mouse Lung Tissue with a Novel Bioanalytical Surrogate Matrix Approach.International journal of molecular sciences · 2024Article
- Structural determinants of tendon multiscale mechanics and their sensitivity to mechanical stimulation during development in an embryonic chick model.Acta biomaterialia · 2024Article
- Nails in older adults.Annals of medicine · 2024Review
- Cellular senescence impairs tendon extracellular matrix remodeling in response to mechanical unloading.Aging cell · 2024Article
- Engineered Age-Mimetic Breast Cancer Models Reveal Differential Drug Responses in Young and Aged Microenvironments.bioRxiv : the preprint server for biology · 2024Article
- Collagen is crucial target protein for scleral remodeling and biomechanical change in myopia progression and control.Heliyon · 2024Review
- Patellar tendon biomechanical and morphologic properties and their relationship to serum clinical variables in persons with prediabetes and type 2 diabetes.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2024Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Collagen is a structural protein whose internal cross-linking critically determines the properties and functions of connective tissue. Knowing how the cross-linking of collagen changes with age is key to understanding why the mechanical properties of tissues change over a lifetime. The current scientific consensus is that collagen cross-linking increases with age and that this increase leads to tendon stiffening. Here, we show that this view should be reconsidered. Using MS-based analyses, we demonstrated that during aging of healthy C57BL/6 mice, the overall levels of collagen cross-linking in tail tendon decreased with age. However, the levels of lysine glycation in collagen, which is not considered a cross-link, increased dramatically with age. We found that in 16-week-old diabetic db/db mice, glycation reaches levels similar to those observed in 98-week-old C57BL/6 mice, while the other cross-links typical of tendon collagen either decreased or remained the same as those observed in 20-week-old WT mice. These results, combined with findings from mechanical testing of tendons from these mice, indicate that overall collagen cross-linking in mouse tendon decreases with age. Our findings also reveal that lysine glycation appears to be an important factor that contributes to tendon stiffening with age and in diabetes.
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Registered trials
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