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...

ba0003cc3 | (1) | ECTS2014

Absence of ER cation channel TMEM38B/TRIC-B causes recessive osteogenesis imperfecta by dysregulation of collagen post-translational modification

Cabral Wayne , Makareeva Elena , Ishikawa Masaki , Barnes Aileen , MaryAnn Weis , Lacbawan Felicitas , Eyre David , Yamada Yoshihiko , Leikin Sergey , Marini Joan

Recessive osteogenesis imperfecta (OI) is caused by mutations in genes encoding proteins involved in post-translational interactions with type I collagen. A founder mutation in a new gene responsible for recessive OI has recently been reported in Bedouins from Israel and Saudi Arabia, who have a homozygous deletion of TMEM38B exon 4 and surrounding intronic sequence. TMEM38B encodes TRIC-B, an integral ER membrane monovalent cation channel involved in Ca...

ba0006oc22 | (1) | ICCBH2017

Type I collagen C-propeptide cleavage deficiency increases bone mineralization and alters bone cell differentiation

Barnes Aileen , Perosky Joseph , Blouin Stephane , Rajpar M. Helen , Khoury Basma , Weis MaryAnn , Klaushofer Klaus , Roschger Paul , Eyre David , Fratzl-Zelman Nadja , Kozloff Kenneth , Marini Joan

High Bone Mass (HBM) osteogenesis imperfecta (OI) is caused by dominant mutations in the C-propeptide cleavage site of COL1A1 or COL1A2, characterized by bone hypermineralization. To elucidate the role of C-propeptide processing in bone mineralization and development, we generated heterozygous HBM mice with both residues (Ala-Asp) of the COL1A1 cleavage site substituted (Thr-Asn) to prevent processing by BMP1. Two, 6- and 12-month WT and HBM bones were examin...

ba0005lb9 | (1) | ECTS2016

First X-linked form of osteogenesis imperfecta, caused by mutations in MBTPS2, demonstrates a fundamental role for regulated intramembrane proteolysis in normal bone formation

Lindert Uschi , Cabral Wayne , Ausavarat Surasawadee , Tongkobpetch Siraprapa , Ludin Katja , Barnes Aileen , Yeetong Patra , Weis Maryann , Krabichler Birgit , Makareeva Elena , Janecke Andreas , Leikin Sergey , Rothlisberger Benno , Rohrback Marianne , Kennerknecht Ingo , Eyre David , Suphapeetiporn Kanya , Giunta Cecilia , Marini Joan , Shotelersuk Vorasuk

Osteogenesis imperfecta (OI) is a heritable bone dysplasia with collagen-related defects. Dominantly inherited OI is caused by structural defects in type I collagen or IFITM5, while recessive forms are caused by deficiency of proteins that interact with collagen for modification, folding or cross-linking. We have identified the first X-linked form of OI, caused by a defect in regulated intramembrane proteolysis (RIP). One type of RIP involves sequential cleavage of regulatory ...