The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
An in vitro study on the role of metal catalyzed oxidation in glyeation and crosslinking of collagen
Abstract
The present investigation was carried out to understand the effect of metal catalyzed oxidation on glycation and crosslinking of collagen. Tail tendons obtained from rats weighing 200-225 g were incubated with glucose (250 mM) and increasing concentrations of copper ions (5, 25, 50 and 100 microM) under physiological conditions of temperature and pH. Early glycation, crosslinking and late glycation (fluorescence) of collagen samples were analyzed periodically. Early glycation was estimated by phenol sulfuric acid method, and the crosslinking was assessed by pepsin and cyanogen bromide digestion. A concentration-dependent effect of metal ions on the rate of glycation and crosslinking of collagen was observed. Tendon collagen incubated with glucose and 100 microM copper ions showed 80% reduction in pepsin digestion within seven days, indicating extensive crosslinking, whereas collagen incubated with glucose alone for the same period showed only 7% reduction. The presence of metal ions in the incubation medium accelerated the development of Maillard reaction fluorescence on collagen, and the increase was dependent on the concentration of metal ions used. The metal chelator diethylene triamine penta-acetate significantly prevented the increase in collagen crosslinking by glucose and copper ions. Free radical scavengers benzoate and mannitol effectively prevented the increased crosslinking and browning of collagen by glucose. The results indicate that the metal catalyzed oxidation reactions play a major role in the crosslinking of collagen by glucose. It is also suggested that the prevention of increased oxidative stress in diabetes may prevent the accelerated advanced glycation and crosslinking of collagen.
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“Several crucial wound healing mechanisms rely on copper for proper function [19,20]. These include the regulation of key growth factors such as VEGF and angiogenin, which drive angiogenesis during the proliferation phase [21,22,23,24,25]; the production of collagen (types I, II, and V) and elastin fibers by dermal fibroblasts, which are essential for tissue formation in the proliferation and remod”
From The Journey of Copper-Impregnated Dressings in Wound Healing: From a Medical Hypothesis to Clinical Practice (2025) · cites this paper as [31]
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Cited by
Copper, oxidative stress, and human health
Uriu‐Adams, J. Y., & Keen, C. L. (2005) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2005.07.015 · Cited by 998
Novel advances in inhibiting advanced glycation end product formation using natural compounds
Song, Q., Liu, J., Dong, L., Wang, X., & Zhang, X. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111750 · Cited by 272
Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
Møller, I. M., Rogowska-Wrzesińska, A., & Rao, R. S. P. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.004 · Cited by 242
Oxidative damage to extracellular matrix and its role in human pathologies
Rees, M. D., Kennett, E. C., Whitelock, J. M., & Davies, M. J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.016 · Cited by 209
Using Copper to Improve the Well-Being of the Skin
Borkow, G. (2015) · Current Chemical Biology · doi:10.2174/2212796809666150227223857 · Cited by 149
Metadata
- Authors
- Sajithlal, G. B., Chithra, P., & Chandrakasan, G.
- Affiliations
- Central Leather Research Institute (IN)
- Venue
- Molecular and Cellular Biochemistry
- Published
- 1999-04
- Volume
- 194
- Issue
- 1-2
- Pages
- 257-263
- ISSN
- 0300-8177 (ISSN-L)
- 1573-4919
- OpenAlex
- W256455925
- Cited by
- 50
- References
- 27
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 0.24
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Molecular and Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Keywords
- collagen glycation, collagen cross-linking, metal-catalyzed oxidation, copper ions, Maillard reaction, advanced glycation end products, radical scavengers, benzoate, mannitol, oxidative stress, diabetes mellitus, tendon collagen, glucose
- MeSH terms
- Animals, Catalysis, Collagen, Electrophoresis, Polyacrylamide Gel, Glucose, Male, Metals, Oxidation-Reduction, Peptide Mapping, Free Radical Scavengers, Glycation End Products, Advanced, Rats, Wistar, Hydroxyl Radical, Rats
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