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pubmed:abstractText |
Collagen from bone (femur and calvarium), rib cartilage, skin, tendon, sclera, and cornea has been isolated and purified from a deceased 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 that of 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. These data suggest that at least one form of osteogenesis imperfecta congenita is associated with a molecular alteration of collagen involving hydroxy-lysine and that this alteration is particualrly marked in collagens obtained from calcifying tissues.
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