@article{HoutenteBrinkeDenisetal.2013,
  author    = {Sander M. Houten and Heleen te Brinke and Simone Denis and Jos Pn Ruiter and Alida C. Knegt and Johannis Bc de Klerk and Persephone Augoustides-Savvopoulou and Johannes H{\"a}berle and Matthias R. Baumgartner and Turgay Coşkun and Johannes Zschocke and J{\"o}rn Oliver Sass and Bwee Tien Poll-The and Ronald Ja Wanders and Marinus Duran},
  title     = {Genetic basis of hyperlysinemia},
  series   = {Orphanet Journal of Rare Diseases},
  volume    = {8},
  publisher = {BioMed Central},
  issn      = {1750-1172},
  doi       = {10.1186/1750-1172-8-57},
  pages     = {57},
  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}
}