Glycation Decreases the Stability of the Triple-Helical Strands of Fibrous Collagen against Proteolytic Degradation by Pepsin in a Specific Temperature Range.

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When fibrous collagen of rat tail tendons was glycated by incubation with ribose, it became highly insoluble in dilute acetic acid and resistant to pepsin digestion at 5°C, since it was cross-linked by advanced glycation end products. Extensively glycated fibrous collagen was found to be much less stable than non-glycated control fibrous collagen against pepsin digestion at 30°C. Under conditions where nearly all of the glycated fibrous collagen was degraded into small peptides by pepsin, approximately 45% of the control collagen was left as large polypeptides having nearly the whole length of its triple-helical region. A soluble collagen, which consisted primarily of the triple-helical region of monomeric collagen, was found to be glycated as efficiently as the fibrous collagen on incubation with ribose at 30°C, while the rate of cross-linking of the soluble collagen was very low, suggesting that the triple-helical strands do not undergo intramolecular cross-linking and that most of the cross-links produced in the glycated fibrous collagen are intermolecular ones. The glycated soluble collagen was as stable as the control collagen against pepsin digestion at 30°C. These results indicate that the triple-helical strands of glycated fibrous collagen are much less stable than those of the non-glycated form against proteolytic digestion by pepsin at a temperature close to but below their melting point. Sugar-derived intermolecular cross-links are supposed to underly the decreased stability of the triple-helical strands.
社団法人日本生化学会の論文

Glycation Decreases the Stability of the Triple-Helical Strands of Fibrous Collagen against Proteolytic Degradation by Pepsin in a Specific Temperature Range.

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