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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 VIIIX 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...

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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...

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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...

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ba0005op14 | Pre-Clinical | ECTS2016

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Willaert Andy , Ghistelinck Charlotte , Witten P Eckhard , Huysseune Ann , Simoens Pascal , Symoens Sofie , Malfait Fransiska , De Muynck Amelie , De Paepe Anne , Kwon Ronald Y , Weiss Mary Ann , Eyre David E , Coucke Paul

see P483....

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ba0005p483 | Paediatric bone disease | ECTS2016

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Willaert Andy , Ghistelinck Charlotte , Witten P Eckhard , Huysseune Ann , Simoens Pascal , Symoens Sofie , Malfait Fransiska , De Muynck Amelie , De Paepe Anne , Kwon Ronald Y , Weiss Mary Ann , Eyre David E , Coucke Paul

Bruck syndrome, a disorder caused by bi-allelic mutations in either PLOD2 or FKBP10, is characterized by flexion contractures and bone fractures and shows strong clinical overlap with the brittle bone disease Osteogenesis Imperfecta. PLOD2 encodes the Lysyl hydroxylase 2 (LH2) enzyme, which is responsible for the hydroxylation of lysine residues in the type-I collagen telopeptides. This hydroxylation directs cross-linking of the collagen fibrils in t...

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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 ...

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Bone Abstracts

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

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

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

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

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

BiosciAbstracts