Cited by 50Advanced Glycation End Products researchCollagen: Extraction and CharacterizationPotato Plant Research

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An in vitro study on the role of metal catalyzed oxidation in glyeation and crosslinking of collagen

Sajithlal, G.B., Chithra, Pandarinathan, Chandrakasan, Gowri·1999·Molecular and Cellular Biochemistry

DOI 10.1023/a:1006988719374

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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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Authors: Sajithlal, G. B., Chithra, P., & Chandrakasan, G.
Affiliations: Central Leather Research Institute (IN)
Venue: Molecular and Cellular Biochemistry
Publisher: Springer Science and Business Media LLC
Published: 1999-04
Volume: 194
Issue: 1-2
Pages: 257-263
ISSN: 0300-8177 (ISSN-L)
1573-4919
DOI: 10.1023/a:1006988719374
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: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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An in vitro study on the role of metal catalyzed oxidation in glyeation and crosslinking of collagen

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