Identification, clinical manifestation and structural mechanisms of mutations in AMPK associated cardiac glycogen storage disease.


Journal

EBioMedicine
ISSN: 2352-3964
Titre abrégé: EBioMedicine
Pays: Netherlands
ID NLM: 101647039

Informations de publication

Date de publication:
Apr 2020
Historique:
received: 11 09 2019
revised: 08 02 2020
accepted: 03 03 2020
pubmed: 8 4 2020
medline: 26 1 2021
entrez: 8 4 2020
Statut: ppublish

Résumé

Although 21 causative mutations have been associated with PRKAG2 syndrome, our understanding of the syndrome remains incomplete. The aim of this project is to further investigate its unique genetic background, clinical manifestations, and underlying structural changes. We recruited 885 hypertrophic cardiomyopathy (HCM) probands and their families internationally. Targeted next-generation sequencing of sudden cardiac death (SCD) genes was performed. The role of the identified variants was assessed using histological techniques and computational modeling. Twelve PRKAG2 syndrome kindreds harboring 5 distinct variants were identified. The clinical penetrance of 25 carriers was 100.0%. Twenty-two family members died of SCD or heart failure (HF). All probands developed bradycardia (HRmin, 36.3 ± 9.8 bpm) and cardiac conduction defects, and 33% had evidence of atrial fibrillation/paroxysmal supraventricular tachycardia (PSVT) and 67% had ventricular preexcitation, respectively. Some carriers presented with apical hypertrophy, hypertension, hyperlipidemia, and renal insufficiency. Histological study revealed reduced AMPK activity and major cardiac channels in the heart tissue with K485E mutation. Computational modelling suggests that K485E disrupts the salt bridge connecting the β and γ subunits of AMPK, R302Q/P decreases the binding affinity for ATP, T400N and H401D alter the orientation of H383 and R531 residues, thus altering nucleotide binding, and N488I and L341S lead to structural instability in the Bateman domain, which disrupts the intramolecular regulation. Including 4 families with 3 new mutations, we describe a cohort of 12 kindreds with PRKAG2 syndrome with novel pathogenic mechanisms by computational modelling. Severe clinical cardiac phenotypes may be developed, including HF, requiring close follow-up.

Sections du résumé

BACKGROUND BACKGROUND
Although 21 causative mutations have been associated with PRKAG2 syndrome, our understanding of the syndrome remains incomplete. The aim of this project is to further investigate its unique genetic background, clinical manifestations, and underlying structural changes.
METHODS METHODS
We recruited 885 hypertrophic cardiomyopathy (HCM) probands and their families internationally. Targeted next-generation sequencing of sudden cardiac death (SCD) genes was performed. The role of the identified variants was assessed using histological techniques and computational modeling.
FINDINGS RESULTS
Twelve PRKAG2 syndrome kindreds harboring 5 distinct variants were identified. The clinical penetrance of 25 carriers was 100.0%. Twenty-two family members died of SCD or heart failure (HF). All probands developed bradycardia (HRmin, 36.3 ± 9.8 bpm) and cardiac conduction defects, and 33% had evidence of atrial fibrillation/paroxysmal supraventricular tachycardia (PSVT) and 67% had ventricular preexcitation, respectively. Some carriers presented with apical hypertrophy, hypertension, hyperlipidemia, and renal insufficiency. Histological study revealed reduced AMPK activity and major cardiac channels in the heart tissue with K485E mutation. Computational modelling suggests that K485E disrupts the salt bridge connecting the β and γ subunits of AMPK, R302Q/P decreases the binding affinity for ATP, T400N and H401D alter the orientation of H383 and R531 residues, thus altering nucleotide binding, and N488I and L341S lead to structural instability in the Bateman domain, which disrupts the intramolecular regulation.
INTERPRETATION CONCLUSIONS
Including 4 families with 3 new mutations, we describe a cohort of 12 kindreds with PRKAG2 syndrome with novel pathogenic mechanisms by computational modelling. Severe clinical cardiac phenotypes may be developed, including HF, requiring close follow-up.

Identifiants

pubmed: 32259713
pii: S2352-3964(20)30098-0
doi: 10.1016/j.ebiom.2020.102723
pmc: PMC7132172
pii:
doi:

Substances chimiques

Adenosine Triphosphate 8L70Q75FXE
PRKAG2 protein, human EC 2.7.11.1
AMP-Activated Protein Kinases EC 2.7.11.31

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

102723

Subventions

Organisme : NHLBI NIH HHS
ID : R01 HL047678
Pays : United States
Organisme : NHLBI NIH HHS
ID : R56 HL138103
Pays : United States

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors report no relationships that could be construed as a conflict of interest.

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Auteurs

Dan Hu (D)

Department of Cardiology and Cardiovascular Research Institute, Renmin Hospital of Wuhan University, 238 Jiefang Road, Wuhan 430060, China; Hubei Key Laboratory of Cardiology, Wuhan 430060, China. Electronic address: rm002646@whu.edu.cn.

Dong Hu (D)

Center for Stem Cell Research and Application, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.

Liwen Liu (L)

Department of Ultrasound, Xijing Hospital, Fourth Military Medical University, Xi'an, China.

Daniel Barr (D)

Department of Chemistry, University of Mary, 7500 University Drive, Bismarck, ND, USA.

Yang Liu (Y)

Guangdong Cardiovascular Institute, Guangdong General Hospital, Guangdong Academy of Medical Sciences, 106 Zhongshan Er Road, Guangzhou 510080, China.

Norma Balderrabano-Saucedo (N)

Department of Cardiology, Children Hospital of Mexico Federico Gómez, México, D.F., México.

Bo Wang (B)

Department of Ultrasound, Xijing Hospital, Fourth Military Medical University, Xi'an, China.

Feng Zhu (F)

Clinic Center of Human Gene Research, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, China; Department of Cardiology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, China.

Yumei Xue (Y)

Guangdong Cardiovascular Institute, Guangdong General Hospital, Guangdong Academy of Medical Sciences, 106 Zhongshan Er Road, Guangzhou 510080, China.

Shulin Wu (S)

Guangdong Cardiovascular Institute, Guangdong General Hospital, Guangdong Academy of Medical Sciences, 106 Zhongshan Er Road, Guangzhou 510080, China.

BaoLiang Song (B)

College of Life Sciences, Wuhan University, Wuhan, China.

Heather McManus (H)

Department of Chemistry and Biochemistry, Utica College, Utica, NY, USA.

Katherine Murphy (K)

Department of Chemistry, University of Mary, 7500 University Drive, Bismarck, ND, USA.

Katherine Loes (K)

Department of Chemistry, University of Mary, 7500 University Drive, Bismarck, ND, USA.

Arnon Adler (A)

Department of Physiology and the Peter Munk Cardiovascular Molecular Medicine Laboratory, Toronto General Hospital, University of Toronto, Toronto, ON, Canada.

Lorenzo Monserrat (L)

Health in Code SL, A Coruña, Spain.

Charles Antzelevitch (C)

Lankenau Institute for Medical Research, Wynnewood, PA, USA; Lankenau Heart Institute, Sidney Kimmel College of Medicine, Thomas Jefferson University, USA.

Michael H Gollob (MH)

Department of Physiology and the Peter Munk Cardiovascular Molecular Medicine Laboratory, Toronto General Hospital, University of Toronto, Toronto, ON, Canada.

Perry M Elliott (PM)

University College London and St. Bartholomew's Hospital, London, United Kingdom.

Hector Barajas-Martinez (H)

Lankenau Institute for Medical Research, Wynnewood, PA, USA; Lankenau Heart Institute, Sidney Kimmel College of Medicine, Thomas Jefferson University, USA.

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Classifications MeSH