Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 50Advanced Glycation End Products researchCollagen: Extraction and CharacterizationPotato Plant Research

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

Sajithlal, G.B., Chithra, Pandarinathan, Chandrakasan, Gowri·1999·Molecular and Cellular Biochemistry
DOI 10.1023/a:1006988719374
Open this paper in CoChat — free account

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.

Overview

Integrity signals

Registry

Crossref · 10.1023/a:1006988719374

Cites

27 of 27 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Research works printed but not linked: 2

  1. Brownlee M, Vlassara H, Cerami A: The pathogenic role of nonenzymatic glycosylation in diabetic complications. In: MJC Crabbe (ed.). Diabetic complications: Scientific and clinical aspects. London; Churchill Livingston, 1987, p 94
  2. Schnider SL, Kohn RR: Effects of age and diabetes mellitus on the solubility of collagen from human skin tracheal cartilage and duramater. Exp Gerontol 17: 185–194, 1982 · DOI

Cited by

See all 50

Related

See all

Metadata

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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.