OSTEOGENESIS IMPERFECTA CONGENITA - EVIDENCE FOR A GENERALIZED MOLECULAR DISORDER OF COLLAGEN

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  • 1 January 1977
    • journal article
    • research article
    • Vol. 36  (5) , 501-508
Abstract
Collagen from bone (femur and calvarium), rib cartilage, skin, tendon, sclera and cornea was isolated and purified from a decreased 4 day old infant with osteogenesis imperfecta congenita. Amino acid analysis indicated that the content of hydroxylysine was doubled in bone collagen and increased by 55% in cartilage as compared with age-matched normal tissues. The levels of covalently bound glucose and galactose were proportionately increased in both collagens. Collagen purified from other tissues revealed smaller increases in lysyl hydroxylation. At least 1 form of osteogenesis imperfecta congenita is apparently associated with a molecular alteration of collagen involving hydroxylysine and this alteration is particularly marked in collagens obtained from calcifying tissues.