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Localization of the dominant non-enzymatic intermolecular cross-linking sites on fibrous collagen.

Abstract：

:Previous studies have shown that fibrous collagen undergoes intermolecular cross-linking at multiple sites of the elongated triple-helical regions among adjacent juxtaposed collagen molecules on incubation with a very high concentration of reducing sugar such as 200 mM ribose, and the similarity of the changes in its physicochemical properties to that of senescent collagen aged in vivo has been emphasized. In the present study, however, it was found that when incubated with less than 30 mM ribose, fibrous collagen underwent intermolecular cross-linking primarily between the telopeptide region of a collagen molecule and the triple-helical region of another adjacent collagen molecule, and intermolecular cross-linking between the triple-helical regions of adjacent collagen molecules was very small. Physiological significance of the previous studies thus needs to be reevaluated.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Chiue H,Yamazoye T,Matsumura S

doi

10.1016/j.bbrc.2015.04.011

subject

Has Abstract

pub_date

2015-06-05 00:00:00

pages

445-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(15)00677-4

journal_volume

461

pub_type

杂志文章

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