Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones.
Tissue from two patients with osteogenesis imperfecta suffering from a hyperplastic callus was studied. Although collagen type I from the compact bone and the skin and fibroblast cultures of these patients showed normal lysyl hydroxylation, collagen types I, II, III and V from the callus tissue were markedly overhydroxylated. Furthermore, the overhydroxylation of lysine residues covered almost equally the entire alpha 1 (I) collagen chain, as demonstrated by the analysis of individual CNBr-derived peptides. In addition, collagen type I was isolated from femoral compact bone of 33 individuals who died between the 16th week of gestational age and 22 years. Lysyl hydroxylation rapidly decreased in both collagen alpha 1 (I) and alpha 2 (I) chains during fetal development, and only little in the postnatal period. The transient increase in lysyl hydroxylation and the involvement of various collagen types in callus tissue argue for a regulatory mechanism that may operate in bone repair and during fetal development.
Lehmann
H W
HW
Institut für Medizinische Molekularbiologie, Lübeck, Federal Republic of Germany.
Bodo
M
M
Frohn
C
C
Nerlich
A
A
Rimek
D
D
Notbohm
H
H
Müller
P K
PK
D000293:Adolescent; D000328:Adult; D000596:Amino Acids / Q000032:analysis; D001842:Bone and Bones / Q000196:embryology / Q000378:metabolism*; D002146:Bony Callus / Q000378:metabolism* / Q000473:pathology; D002942:Circular Dichroism; D003094:Collagen / Q000378:metabolism; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006900:Hydroxylation; D006965:Hyperplasia; D008297:Male; D011392:Proline / Q000378:metabolism; D012867:Skin / Q000378:metabolism
D000596:Amino Acids; D003094:Collagen; D011392:Proline; D003488:Cyanogen Bromide