Chemistry of collagen cross-linking: biochemical changes in collagen during the partial mineralization of turkey leg tendon.
With age, the proximal sections of turkey leg tendons become calcified, and this phenomenon has led to their use as a model for collagen mineralization. Mineralizing turkey leg tendon was used in this study to characterize further the composition and cross-linking of collagen in calcified tissues. The cross-link profiles of mineralizing collagen are significantly different from those of other collagenous matrices with characteristically low amounts of hydroxylysyl-pyridinoline and the presence of lysyl-pyridinoline and pyrrolic cross-links. However, the presence of the immature cross-link precursors previously reported in calcifying tissues was not supported in the present study, and was found to be due to the decalcification procedure using EDTA. Analysis of tendons from young birds demonstrated differences in the cross-link profile which indicated a higher level of hydroxylation of specific triple-helical lysines involved in cross-linking of the proximal tendon. This may be related to later calcification, suggesting that this part of the tendon is predestined to be calcified. The minimal changes in lysyl hydroxylation in both regions of the tendon with age were in contrast with the large changes in the cross-link profile, indicating differential hydroxylation of the helical and telopeptide lysine residues. Changes with age in the collagen matrix, its turnover and thermal properties in both the proximal and distal sections of the tendon clearly demonstrate that a new and modified matrix is formed throughout the tendon, and that a different type of matrix is formed at each site.
Knott
L
L
Division of Molecular and Cellular Biology, University of Bristol, Langford, U.K.
Tarlton
J F
JF
Bailey
A J
AJ
D000367:Age Factors; D000818:Animals; D002113:Calcification, Physiologic; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism*; D003432:Cross-Linking Reagents; D004586:Electrophoresis / Q000379:methods; D005780:Gelatin / Q000378:metabolism; D018093:Gelatinases / Q000032:analysis; D006901:Hydroxylysine / Q000032:analysis; D020778:Matrix Metalloproteinase 2; D008666:Metalloendopeptidases / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D011499:Protein Processing, Post-Translational; D011758:Pyrroles / Q000737:chemistry; D013710:Tendons / Q000502:physiology*; D014422:Turkeys
D003432:Cross-Linking Reagents; D011758:Pyrroles; D006901:Hydroxylysine; D005780:Gelatin; D003094:Collagen; D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2