[HTML][HTML] Cyclophilin-B modulates collagen cross-linking by differentially affecting lysine hydroxylation in the helical and telopeptidyl domains of tendon type I collagen
M Terajima, Y Taga, Y Chen, WA Cabral… - Journal of Biological …, 2016 - ASBMB
Covalent intermolecular cross-linking provides collagen fibrils with stability. The cross-
linking chemistry is tissue-specific and determined primarily by the state of lysine
hydroxylation at specific sites. A recent study on cyclophilin B (CypB) null mice, a model of
recessive osteogenesis imperfecta, demonstrated that lysine hydroxylation at the helical
cross-linking site of bone type I collagen was diminished in these animals (Cabral, WA,
Perdivara, I., Weis, M., Terajima, M., Blissett, AR, Chang, W., Perosky, JE, Makareeva, EN …
linking chemistry is tissue-specific and determined primarily by the state of lysine
hydroxylation at specific sites. A recent study on cyclophilin B (CypB) null mice, a model of
recessive osteogenesis imperfecta, demonstrated that lysine hydroxylation at the helical
cross-linking site of bone type I collagen was diminished in these animals (Cabral, WA,
Perdivara, I., Weis, M., Terajima, M., Blissett, AR, Chang, W., Perosky, JE, Makareeva, EN …