Collagen heterogeneity within different growth regions of long bones of rachitic and non-rachitic chicks.
The different anatomical regions involved in osteogenesis in the chick long bone have been examined for heterogeneities in collagen structure that might relate to the mechanism of ossification. Experimentally induced lathyrism was employed to enhance collagen solubility, and vitamin D deficiency to allow accumulation of osteoid, the precursor of bone matrix. The extractable lathyritic collagens of the cartilaginous and osseous regions of growing long bones from rachitic and non-rachitic chicks were examined for alpha-chain type and amino acid composition. In both groups of animals the growth plate and cartilaginous regions of the epiphysis gave collagen molecules of the constitution [alpha1(II)](3), whereas the ossifying regions contained [alpha1(I)](2) alpha2. The degree of hydroxylation of the lysine moieties was increased by approximately 50% in the alpha1(I)-chain and alpha2-chain of rachitic bone collagen. Since uncalcified osteoid is greatly enriched in rachitic bone, it is concluded that the collagen of osteoid has the configuration [alpha1(I)](2) alpha2, similar to that of bone matrix, but has an elevated hydroxylysine content. The possible relationship of this difference to the mechanism of calcification is discussed.
D000596:Amino Acids / Q000032:analysis; D000629:Aminopropionitrile; D000818:Animals; D001842:Bone and Bones / Q000032:analysis; D002113:Calcification, Physiologic; D002645:Chickens; D002845:Chromatography; D003094:Collagen / Q000378:metabolism*; D004838:Epiphyses / Q000032:analysis; D006900:Hydroxylation; D007842:Lathyrism / Q000378:metabolism; D008239:Lysine; D010012:Osteogenesis; D012279:Rickets / Q000378:metabolism*
D000596:Amino Acids; D000629:Aminopropionitrile; D003094:Collagen; D008239:Lysine