Biochemical and morphological modifications in rabbit Achilles tendon during maturation and ageing.

1. Achilles tendons of foetal, newborn, adult and old rabbits were examined by electron microscopy after staining by conventional methods or with the periodate/silver/methenamine technique. 2. The mean diameter of collagen fibrils increased with age whereas silver/methenamine-positivity became less evident. 3. Biochemical analyses showed a great decrease of the concentration of glycoproteins and galactosamine-containing glycosaminoglycans. 4. Collagen content increased with maturation and ageing of the tissue. 5. The extent of glycosylation of collagen hydroxylysine residues was also age-dependent; the total amount of hydroxylysyl glycosides rapidly decreased in the last days of prenatal life and in the first months after birth, corresponding to the rapid growth in collagen fibre diameter. 6. The hydroxylysyl diglycoside concentration decreased more markedly than that of the monoglycoside, thus indicating a possible gradual removal of the monosaccharide units. A role for the extent of glycosylation of tropocollagen molecules in fibre organization was suggested.