Searchable abstracts of presentations at key conferences on calcified tissues

ba0001pp501 | Other diseases of bone and mineral metabolism | ECTS2013

Abnormal type I collagen glycosylation pattern and cross-linking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta

Cabral Wayne , Perdivara Irina , MaryAnn Weis , Terajima Masahiko , Blissett Angela , Chang Weizhong , Makareeva Elena , Leikin Sergey , Eyre David , Yamauchi Mitsuo

Introduction: Recessive osteogenesis imperfecta (OI) is caused by mutations in genes encoding proteins involved in post-translational interactions with type I collagen. Types VII–IX OI involve defects in the collagen prolyl 3-hydroxylation complex, which modifies α1(I)Pro986. PPIB encodes CyPB, a complex component with PPIase activity and the major isomerase facilitating collagen folding. We investigated the role of CyPB in collagen post-translational modifications a...