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J Med Genet 42:e43 doi:10.1136/jmg.2004.029967
  • Electronic letters

Mutations in FLNB cause boomerang dysplasia

  1. L S Bicknell1,
  2. T Morgan1,
  3. L Bonafé2,
  4. M W Wessels3,
  5. M G Bialer4,
  6. P J Willems5,
  7. D H Cohn6,
  8. D Krakow7,
  9. S P Robertson1
  1. 1Department of Paediatrics and Child Health, University of Otago, Dunedin, New Zealand
  2. 2Division of Molecular Paediatrics, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland
  3. 3Department of Clinical Genetics, Erasmus University and University Hospital, Rotterdam, The Netherlands
  4. 4Department of Pediatrics, Schneider Children’s Hospital at North Shore/NYU Medical Center, Manhasset, NY, USA
  5. 5Gendia, Antwerp, Belgium
  6. 6Department of Human Genetics, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA
  7. 7Department of Obstetrics and Gynecology, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA
  1. Correspondence to:
 Professor S Robertson
 Department of Paediatrics and Child Health, Dunedin School of Medicine, PO Box 913, Dunedin, New Zealand; stephen.robertsonstonebow.otago.ac.nz
  • Received 12 December 2004
  • Accepted 18 February 2005
  • Revised 7 February 2005

Abstract

Boomerang dysplasia (BD) is a perinatal lethal osteochondrodysplasia, characterised by absence or underossification of the limb bones and vertebrae. The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that we have recently shown to be associated with mutations in FLNB, the gene encoding the actin binding cytoskeletal protein, filamin B. We report the identification of mutations in FLNB in two unrelated individuals with boomerang dysplasia. The resultant substitutions, L171R and S235P, lie within the calponin homology 2 region of the actin binding domain of filamin B and occur at sites that are evolutionarily well conserved. These findings expand the phenotypic spectrum resulting from mutations in FLNB and underline the central role this protein plays during skeletogenesis in humans.

Footnotes

  • S Robertson is supported by the Child Health Research Foundation of New Zealand.

  • Competing interests: none declared