Osteogenesis imperfecta congenita: evidence for a generalized molecular disorder of collagen.

Abstract

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.

• Authors: R L Trelstad, D Rubin, J Gross
• Journal: Laboratory investigation; a journal of technical methods and pathology (Lab Invest) Vol. 36 Issue 5 Pg. 501-8 (May 1977) ISSN: 0023-6837 [Print] United States
• PMID: 865078 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Amino Acids
• Hydroxylysine
• Collagen
• Glucose
• Galactose

Topics

• Amino Acids (analysis)
• Bone and Bones (analysis)
• Cartilage (analysis)
• Cells, Cultured
• Collagen (analysis)
• Cornea (analysis)
• Female
• Fibroblasts (analysis)
• Galactose (analysis)
• Glucose (analysis)
• Humans
• Hydroxylysine (analysis)
• Infant, Newborn
• Osteogenesis Imperfecta (congenital, metabolism)
• Sclera (analysis)
• Skin (analysis)
• Tendons (analysis)