Aging, and crosslinking in mammalian collagen
- 1 March 1977
- journal article
- Published by Taylor & Francis in Experimental Aging Research
- Vol. 3 (2) , 87-105
- https://doi.org/10.1080/03610737708257091
Abstract
The amount and type of borohydride-reducible crosslinks in collagen have been examined as a function of animal age. In a variety of bovine, canine and human tissues the level of redicible crosslinks decreases with time and the ratios of individual compounds change. There is both tissue and species specificity in the extent of these changes. A decrease in the level of reducible crosslinks correlates with the cessation of growth. Loss of reducible crosslinks does not imply a small total number of crosslinks since physical changes with age imply the opposite. We conclude that reducible crosslinks are converted to a stable nonreducible state and the persistence of low levels of reducible crosslinks may be indicative of a low level of turnover in the tissue. Changes in ratios of reducible crosslinks are of doubtful functioal significance and may simply reflect variation in post-translational modification of lysine residues.Keywords
This publication has 28 references indexed in Scilit:
- Isolation of a Crosslinked Cyanogen‐Bromide Peptide from Insoluble Rabbit Collagen Tissue Differences in Hydroxylation and Glycosylation of the CrosslinkEuropean Journal of Biochemistry, 1976
- A Stabilised Tris(Hydroxymethyl)Aminomethane Adduct in Reduced CollagenConnective Tissue Research, 1976
- Aging of Human Bone and Articular Cartilage CollagenGerontology, 1976
- Collagen crosslinking: Isolation of hydroxyaldol-histidine, a naturally-occurring crosslinkBiochemical and Biophysical Research Communications, 1975
- Age-related changes in aldehyde location on rat tail tendon collagenBiochemical and Biophysical Research Communications, 1975
- Isolation and characterization of glycosyl derivatives of the reducible cross‐links in collagensFEBS Letters, 1974
- The stability of collagen cross-links when derived from hydroxylysyl residuesBiochemical and Biophysical Research Communications, 1973
- Analysis of a crosslinked peptide from calf bone collagen: Evidence that hydroxylysyl glycoside participates in the crosslinkBiochemical and Biophysical Research Communications, 1973
- Cross-linking and aging in rat tendon collagenExperimental Gerontology, 1973
- The nature of crosslinking in collagens from mineralized tissuesBiochemical and Biophysical Research Communications, 1971