Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding Academic Article uri icon

Overview

MeSH Major

  • Codon, Initiator
  • Cyclophilins
  • Mutation
  • Osteogenesis Imperfecta

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.

publication date

  • February 11, 2010

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3156560

Digital Object Identifier (DOI)

  • 10.1056/NEJMoa0907705

PubMed ID

  • 20089953

Additional Document Info

start page

  • 521

end page

  • 8

volume

  • 362

number

  • 6