Biomaterial Database

Osteogenesis imperfecta: biochemical studies of bone collagen. 1977

K Fujii, and M L Tanzer

The biochemical properties of tibial bone collagen, obtained from patients with osteogenesis imperfecta, were studied by investigating amino acid composition, subunit composition and crosslink formation. Direct comparison of this bone was made with normal bone, age and sex matched, which had been removed from the tibiae of individuals within 48 hours after accidental death. The amino acid compositions of OI and normal bone collagen were almost identical and the pepsin solubilized collagen fraction as well as the CNBr peptides of insoluble bone collagen were very similar, indicating that no differences in collagen genetic type occurred in OI compared to normal. The crosslink contents and the specific radioactivities of the insoluble collagens were determined following NaB3H4 reduction. The specific radioactivity values of OI bone collagen were found to average 50 per cent higher than normal collagen. Analyses of OI collagen showed abundant formation of the major reducible aldehydes and crosslinks. Compared to the controls there were much higher proportions of the reduced aldehyde, dihydroxynorleucine and the reduced crosslink, dihydroxylysinonorleucine. These results may indicate delayed maturation of crosslinking in OI bone collagen and may reflect diminished stability of such collagen during bone development.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D010013	Osteogenesis Imperfecta	COLLAGEN DISEASES characterized by brittle, osteoporotic, and easily fractured bones. It may also present with blue sclerae, loose joints, and imperfect dentin formation. Most types are autosomal dominant and are associated with mutations in COLLAGEN TYPE I.	Fragilitas Ossium,Lobstein Disease,Brittle Bone Disease,Lobstein's Disease,Osteogenesis Imperfecta Tarda,Osteogenesis Imperfecta with Blue Sclerae,Osteogenesis Imperfecta, Type 1,Osteogenesis Imperfecta, Type I,Disease, Lobstein,Disease, Lobstein's,Lobsteins Disease,Ossiums, Fragilitas,Osteogenesis Imperfecta Tardas
D001842	Bone and Bones	A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principal cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.	Bone Tissue,Bone and Bone,Bone,Bones,Bones and Bone,Bones and Bone Tissue,Bony Apophyses,Bony Apophysis,Condyle,Apophyses, Bony,Apophysis, Bony,Bone Tissues,Condyles,Tissue, Bone,Tissues, Bone
D002648	Child	A person 6 to 12 years of age. An individual 2 to 5 years old is CHILD, PRESCHOOL.	Children
D003094	Collagen	A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).	Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D005260	Female		Females
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000293	Adolescent	A person 13 to 18 years of age.	Adolescence,Youth,Adolescents,Adolescents, Female,Adolescents, Male,Teenagers,Teens,Adolescent, Female,Adolescent, Male,Female Adolescent,Female Adolescents,Male Adolescent,Male Adolescents,Teen,Teenager,Youths
D000447	Aldehydes	Organic compounds containing a carbonyl group in the form -CHO.	Aldehyde
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino