loading page

Non-coding sequence variants define a novel regulatory element in the first intron of the N-acetylglutamate synthase gene.
  • +9
  • Johannes Häberle,
  • Barry Moore,
  • Nantaporn Haskins,
  • Véronique Rüfenacht,
  • Dariusz Rokicki,
  • M. Estela Rubio Gozalbo,
  • Mendel Tuchman,
  • Nicola Longo,
  • Mark Yandell,
  • Ashley Andrews,
  • Nicholas AhMew,
  • Ljubica Caldovic
Johannes Häberle
University Children's Hospital, Zurich

Corresponding Author:[email protected]

Author Profile
Barry Moore
The University of Utah School of Medicine
Author Profile
Nantaporn Haskins
Children's National Medical Center
Author Profile
Véronique Rüfenacht
University Children's Hospital, Zurich
Author Profile
Dariusz Rokicki
The Children's Memorial Health Institute,
Author Profile
M. Estela Rubio Gozalbo
Maastricht University Medical Center
Author Profile
Mendel Tuchman
Children's National Medical Center
Author Profile
Nicola Longo
University of Utah
Author Profile
Mark Yandell
Univ of Utah
Author Profile
Ashley Andrews
University of Utah
Author Profile
Nicholas AhMew
Children's National Medical Center
Author Profile
Ljubica Caldovic
Children's National Medical Center
Author Profile

Abstract

N-acetylglutamate synthase deficiency (NAGSD, MIM #237310) is an autosomal recessive urea cycle disorder caused either by decreased expression of the NAGS gene or defective NAGS enzyme resulting in decreased production of N-acetylglutamate (NAG), an allosteric activator of carbamylphosphate synthetase 1 (CPS1). NAGSD is the only urea cycle disorder that can be effectively treated with a single drug, N-carbamylglutamate (NCG), a stable NAG analog, which activates CPS1 to restore ureagenesis. We describe three patients with NAGSD due to four novel sequence variants in the NAGS regulatory regions. All three patients had hyperammonemia that resolved upon treatment with NCG. Sequence variants NM_153006.2:c.-3065A>C and NM_153006.2:c-3098C>T reside in the NAGS enhancer, within known HNF1 and predicted glucocorticoid receptor binding sites, respectively. Sequence variants NM_153006.2:c.426+326G>A and NM_153006.2:c.427-218A>C reside in the first intron of NAGS and define a novel NAGS regulatory element that binds retinoic X receptor α. Reporter gene assays in HepG2 and HuH-7 cells demonstrated that all four substitutions could result in reduced expression of NAGS. These findings show that analyzing non-coding regions of NAGS and other urea cycle genes can reveal molecular causes of disease and identify novel regulators of ureagenesis.
19 Apr 2021Submitted to Human Mutation
21 Apr 2021Submission Checks Completed
21 Apr 2021Assigned to Editor
02 May 2021Reviewer(s) Assigned
20 May 2021Review(s) Completed, Editorial Evaluation Pending
25 May 2021Editorial Decision: Revise Minor
26 Jul 20211st Revision Received
21 Aug 2021Submission Checks Completed
21 Aug 2021Assigned to Editor
21 Aug 2021Reviewer(s) Assigned
02 Sep 2021Review(s) Completed, Editorial Evaluation Pending
08 Sep 2021Editorial Decision: Accept