Related Experiment Videos
Isolation and partial characterization of collagen chains dimerized by sugar-derived cross-links
S Tanaka1, G Avigad, E F Eikenberry
1Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854.
The Journal of Biological Chemistry
|November 25, 1988
Summary
D-ribose rapidly attaches to collagen, forming cross-links faster than glucose. This process increases collagen fluorescence and resistance to degradation, mimicking age-related changes.
Area of Science:
- Biochemistry
- Biomaterials Science
- Connective Tissue Research
Background:
- Collagen is a crucial structural protein.
- Age-related changes in collagen affect tissue properties.
- Non-enzymatic glycation contributes to collagen aging.
Purpose of the Study:
- To investigate the interaction of D-ribose with collagen.
- To compare ribose-induced collagen cross-linking with glucose.
- To characterize the resulting collagen modifications and their implications for aging.
Main Methods:
- Incubation of rat tail tendon collagen with D-ribose.
- Solubilization assays to assess collagen cross-linking.
- Fluorescence spectroscopy to measure collagen modifications.
- Peptic digestion and peptide analysis (CNBr) to identify cross-linking sites.
- Isolation and characterization of collagen dimers.
Main Results:
- D-ribose rapidly cross-linked collagen, exceeding glucose's rate.
- Ribose-bound collagen showed increased fluorescence and resistance to solubilization.
- Cross-linking occurred preferentially in specific collagen peptide regions (alpha 2-CB3,5 and alpha 1-CB6).
- Pepsin digestion revealed ribose-induced dimers (beta 11, beta 12, beta 22) with fluorescence similar to aged collagen.
Conclusions:
- D-ribose is a potent agent for rapid collagen cross-linking.
- Ribose-induced cross-linking and fluorescence mimic age-related collagen alterations.
- This study provides insights into the molecular mechanisms of collagen aging and potential therapeutic targets.