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N Engl J Med. 2010 Feb 11;362(6):521-8. doi: 10.1056/NEJMoa0907705. Epub 2010 Jan 20.

Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding.

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1
National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

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.

PMID:
20089953
PMCID:
PMC3156560
DOI:
10.1056/NEJMoa0907705
[Indexed for MEDLINE]
Free PMC Article
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