@article{Houtente BrinkeDenisetal.2013,
  author    = {Houten, Sander M. and te Brinke, Heleen and Denis, Simone and Ruiter, Jos Pn and Knegt, Alida C. and Klerk, Johannis Bc de and Augoustides-Savvopoulou, Persephone and H{\"a}berle, Johannes and Baumgartner, Matthias R. and Co{\c{s}}kun, Turgay and Zschocke, Johannes and Sass, J{\"o}rn Oliver and Poll-The, Bwee Tien and Wanders, Ronald Ja and Duran, Marinus},
  title     = {Genetic basis of hyperlysinemia},
  journal   = {Orphanet Journal of Rare Diseases},
  volume    = {8},
  issn      = {1750-1172},
  doi       = {10.1186/1750-1172-8-57},
  institution = {Institut f{\"u}r funktionale Gen-Analytik (IFGA)},
  year      = {2013},
  abstract  = {BACKGROUND Hyperlysinemia is an autosomal recessive inborn error of L-lysine degradation. To date only one causal mutation in the AASS gene encoding α-aminoadipic semialdehyde synthase has been reported. We aimed to better define the genetic basis of hyperlysinemia. METHODS We collected the clinical, biochemical and molecular data in a cohort of 8 hyperlysinemia patients with distinct neurological features. RESULTS We found novel causal mutations in AASS in all affected individuals, including 4 missense mutations, 2 deletions and 1 duplication. In two patients originating from one family, the hyperlysinemia was caused by a contiguous gene deletion syndrome affecting AASS and PTPRZ1. CONCLUSIONS Hyperlysinemia is caused by mutations in AASS. As hyperlysinemia is generally considered a benign metabolic variant, the more severe neurological disease course in two patients with a contiguous deletion syndrome may be explained by the additional loss of PTPRZ1. Our findings illustrate the importance of detailed biochemical and genetic studies in any hyperlysinemia patient.},
  language  = {en}
}