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Genetic basis of hyperlysinemia. / Houten, Sander M.; te Brinke, Heleen; Denis, Simone et al.

In: Orphanet journal of rare diseases, Vol. 8, No. 1, 2013, p. 57.

Research output: Contribution to journal › Article › Academic › peer-review

Harvard

Houten, SM, te Brinke, H, Denis, S, Ruiter, JP, Knegt, AC, de Klerk, JB, Augoustides-Savvopoulou, P, Häberle, J, Baumgartner, MR, Coşkun, T, Zschocke, J, Sass, JO, Poll-The, BT, Wanders, RJ & Duran, M 2013, 'Genetic basis of hyperlysinemia', Orphanet journal of rare diseases, vol. 8, no. 1, pp. 57. https://doi.org/10.1186/1750-1172-8-57

APA

Houten, S. M., te Brinke, H., Denis, S., Ruiter, J. P., Knegt, A. C., de Klerk, J. B., Augoustides-Savvopoulou, P., Häberle, J., Baumgartner, M. R., Coşkun, T., Zschocke, J., Sass, J. O., Poll-The, B. T., Wanders, R. J., & Duran, M. (2013). Genetic basis of hyperlysinemia. Orphanet journal of rare diseases, 8(1), 57. https://doi.org/10.1186/1750-1172-8-57

Vancouver

Houten SM, te Brinke H, Denis S, Ruiter JP, Knegt AC, de Klerk JB et al. Genetic basis of hyperlysinemia. Orphanet journal of rare diseases. 2013;8(1):57. doi: 10.1186/1750-1172-8-57

Author

Houten, Sander M. ; te Brinke, Heleen ; Denis, Simone et al. / Genetic basis of hyperlysinemia. In: Orphanet journal of rare diseases. 2013 ; Vol. 8, No. 1. pp. 57.

BibTeX

@article{7c29e80307ab445d96bd8116abb43c38,
title = "Genetic basis of hyperlysinemia",
abstract = "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. We collected the clinical, biochemical and molecular data in a cohort of 8 hyperlysinemia patients with distinct neurological features. 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. 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",
author = "Houten, {Sander M.} and {te Brinke}, Heleen and Simone Denis and Ruiter, {Jos Pn} and Knegt, {Alida C.} and {de Klerk}, {Johannis Bc} and Persephone Augoustides-Savvopoulou and Johannes H{\"a}berle and Baumgartner, {Matthias R.} and Turgay Co{\c s}kun and Johannes Zschocke and Sass, {J{\"o}rn Oliver} and Poll-The, {Bwee Tien} and Wanders, {Ronald Ja} and Marinus Duran",
year = "2013",
doi = "10.1186/1750-1172-8-57",
language = "English",
volume = "8",
pages = "57",
journal = "Orphanet journal of rare diseases",
issn = "1750-1172",
publisher = "BioMed Central",
number = "1",

}

RIS

TY - JOUR

T1 - Genetic basis of hyperlysinemia

AU - Houten, Sander M.

AU - te Brinke, Heleen

AU - Denis, Simone

AU - Ruiter, Jos Pn

AU - Knegt, Alida C.

AU - de Klerk, Johannis Bc

AU - Augoustides-Savvopoulou, Persephone

AU - Häberle, Johannes

AU - Baumgartner, Matthias R.

AU - Coşkun, Turgay

AU - Zschocke, Johannes

AU - Sass, Jörn Oliver

AU - Poll-The, Bwee Tien

AU - Wanders, Ronald Ja

AU - Duran, Marinus

PY - 2013

Y1 - 2013

N2 - 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. We collected the clinical, biochemical and molecular data in a cohort of 8 hyperlysinemia patients with distinct neurological features. 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. 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

AB - 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. We collected the clinical, biochemical and molecular data in a cohort of 8 hyperlysinemia patients with distinct neurological features. 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. 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

U2 - 10.1186/1750-1172-8-57

DO - 10.1186/1750-1172-8-57

M3 - Article

C2 - 23570448

VL - 8

SP - 57

JO - Orphanet journal of rare diseases

JF - Orphanet journal of rare diseases

SN - 1750-1172

IS - 1

ER -

ID: 2099373