Collagen crosslinking and cartilage glycosaminoglycan composition in normal and scoliotic chickens

Abstract

The amounts of lysine-derived crosslinks in collagens from tendon, intervertebral, disc, and bone and changes in the composition of sternal cartilage glycosaminoglycans were estimated in two lines of chickens, a control-isogenic line and a line that develops scoliosis. In the scoliotic line, scoliosis first appears at 3–4 weeks and progressively increases in severity and incidence so that 90% of the birds experss the lesion by week 10. We have reported previously that cartilage, tendon, and bone collagens from scoliotic birds are more soluble than corresponding collagens from normal birds. Herein, collagen crosslinking and altered proteoglycan metabolism are examined as possible mechanisms for the differences in collagen solubility. At 1 week of age there were fewer reducible crosslinking amino acids (hydroxylysinonorleucine, dihydroxylysinonorleucine, and lysinonorleucine) in collagens from sternal vartilage and tendon in the scoliotic line than in the isogenic line. However, by week 3 and at weeks 5 or 7 values were similar in both groups. The amounts of hydroxypyridinium in vertebral bone and intervertebral disc collagen were also similar in both groups of birds. Consequently, differences in collagen crosslinking do not appear to be a persistent developmental effect underlying the expression of scoliosis in the model. However, differences were observed in cartilage proteoglycans and glycosaminoglycans from the scoliotic line that were not present in cartilage from the isogenic line. The average molecular weight of the uronide-containing glycosaminoglycans was 30% less in the scoliotic line than in the isogenic line, i.e., 12000 compared to 18000. The size distribution of cartilage proteoglycans from the scoliotic line also differed from that of proteglycans from the isogenic line. An overly sulfated chondroitin also appeared to be a minor component of the glycosaminoglycans in cartilage from the scoliotic line. This chondroitin was not observed in cartilage from the isogenic line of chickens.