Lack of Cyclophilin B in Osteogenesis Imperfecta with Normal Collagen Folding

Overview

Journal N Engl J Med

Specialty General Medicine

Date 2010 Jan 22

PMID 20089953

Citations 77

Authors

Aileen M Barnes

Erin M Carter

Wayne A Cabral

MaryAnn Weis

Weizhong Chang

Elena Makareeva

Sergey Leikin

Charles N Rotimi

David R Eyre

Cathleen L Raggio

Joan C Marini

Affiliations

Soon will be listed here.

Abstract

Osteogenesis imperfecta is a heritable disorder that causes bone fragility. Mutations in type I collagen result in autosomal dominant osteogenesis imperfecta, whereas mutations in either of two components of the collagen prolyl 3-hydroxylation complex (cartilage-associated protein [CRTAP] and prolyl 3-hydroxylase 1 [P3H1]) cause autosomal recessive osteogenesis imperfecta with rhizomelia (shortening of proximal segments of upper and lower limbs) and delayed collagen folding. We identified two siblings who had recessive osteogenesis imperfecta without rhizomelia. They had a homozygous start-codon mutation in the peptidyl-prolyl isomerase B gene (PPIB), which results in a lack of cyclophilin B (CyPB), the third component of the complex. The proband's collagen had normal collagen folding and normal prolyl 3-hydroxylation, suggesting that CyPB is not the exclusive peptidyl-prolyl cis-trans isomerase that catalyzes the rate-limiting step in collagen folding, as is currently thought.

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