TY  - JOUR
U1  - Zeitschriftenartikel, wissenschaftlich - begutachtet (reviewed)
A1  - Houten, Sander M.
A1  - te Brinke, Heleen
A1  - Denis, Simone
A1  - Ruiter, Jos Pn
A1  - Knegt, Alida C.
A1  - Klerk, Johannis Bc de
A1  - Augoustides-Savvopoulou, Persephone
A1  - Häberle, Johannes
A1  - Baumgartner, Matthias R.
A1  - Coşkun, Turgay
A1  - Zschocke, Johannes
A1  - Sass, Jörn Oliver
A1  - Poll-The, Bwee Tien
A1  - Wanders, Ronald Ja
A1  - Duran, Marinus
T1  - Genetic basis of hyperlysinemia
JF  - Orphanet Journal of Rare Diseases
N2  - 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.
SN  - 1750-1172
SS  - 1750-1172
U6  - https://doi.org/10.1186/1750-1172-8-57
DO  - https://doi.org/10.1186/1750-1172-8-57
PM  - 23570448
N1  - © 2013 Houten et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.
VL  - 8
SP  - 57
PB  - BioMed Central
ER  -