A New Glycogen Storage Disease Caused by a Dominant PYGM Mutation.

Szczegóły
Abstrakt

Tytuł:: A New Glycogen Storage Disease Caused by a Dominant PYGM Mutation.
Autorzy:: Echaniz-Laguna A; Department of Neurology, APHP, CHU de Bicêtre, Le Kremlin Bicêtre, France.; French National Reference Center for Rare Neuropathies (NNERF), Le Kremlin Bicêtre, France.; Inserm U1195 & Paris-Saclay University, Le Kremlin Bicêtre, France.
Lornage X; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.
Laforêt P; Department of Neurology, Raymond Poincaré Hospital, Centre de Référence de Pathologie Neuromusculaire Nord-Est-Ile-de-France, Garches, France.; Service de Neurologie, U1179 UVSQ-INSERM Handicap Neuromusculaire: Physiologie, Biothérapie et Pharmacologie appliquées, UFR Simone Veil-Santé, Université Versailles-Saint-Quentin-en-Yvelines, Garches, France.
Orngreen MC; Copenhagen Neuromuscular Center, University of Copenhagen, Rigshospitalet, Copenhagen, Denmark.
Edelweiss E; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.
Brochier G; Neuromuscular Morphology Unit, Myology Institute, GHU Pitié-Salpêtrière, Paris, France.; Centre de Référence de Pathologie Neuromusculaire Paris-Est, Institut de Myologie, GHU Pitié-Salpêtrière, Assistance Publique-Hôpitaux de Paris, Paris, France.
Bui MT; Neuromuscular Morphology Unit, Myology Institute, GHU Pitié-Salpêtrière, Paris, France.
Silva-Rojas R; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.
Birck C; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.; Structural Biology & Genomics Platform, IGBMC, Illkirch, France.
Lannes B; Department of Pathology, Strasbourg University Hospital, Strasbourg, France.
Romero NB; Neuromuscular Morphology Unit, Myology Institute, GHU Pitié-Salpêtrière, Paris, France.; Centre de Référence de Pathologie Neuromusculaire Paris-Est, Institut de Myologie, GHU Pitié-Salpêtrière, Assistance Publique-Hôpitaux de Paris, Paris, France.; Université Sorbonne, UPMC Paris 06 University, Inserm UMRS974, CNRS FRE3617, Center for Research in Myology, GH Pitié-Salpêtrière, Paris, France.
Vissing J; Copenhagen Neuromuscular Center, University of Copenhagen, Rigshospitalet, Copenhagen, Denmark.
Laporte J; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.
Böhm J; Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.; INSERM U1258, Illkirch, France.; CNRS UMR7104, Illkirch, France.; Strasbourg University, Illkirch, France.
Źródło:: Annals of neurology [Ann Neurol] 2020 Aug; Vol. 88 (2), pp. 274-282. Date of Electronic Publication: 2020 Jun 03.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: New York, NY : Wiley-Liss
Original Publication: Boston, Little, Brown.
MeSH Terms:: Glycogen Phosphorylase, Muscle Form/*genetics
Glycogen Storage Disease/*diagnosis
Glycogen Storage Disease/*genetics
Mutation/*genetics
Adult ; Female ; Humans ; Male ; Middle Aged ; Pedigree
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Substance Nomenclature:: EC 2.4.1.- (Glycogen Phosphorylase, Muscle Form)
Entry Date(s):: Date Created: 20200510 Date Completed: 20201209 Latest Revision: 20201214
Update Code:: 20240105
DOI:: 10.1002/ana.25771
PMID:: 32386344
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Objective: Glycogen storage diseases (GSDs) are severe human disorders resulting from abnormal glucose metabolism, and all previously described GSDs segregate as autosomal recessive or X-linked traits. In this study, we aimed to molecularly characterize the first family with a dominant GSD.
Methods: We describe a dominant GSD family with 13 affected members presenting with adult-onset muscle weakness, and we provide clinical, metabolic, histological, and ultrastructural data. We performed exome sequencing to uncover the causative gene, and functional experiments in the cell model and on recombinant proteins to investigate the pathogenic effect of the identified mutation.
Results: We identified a heterozygous missense mutation in PYGM segregating with the disease in the family. PYGM codes for myophosphorylase, the enzyme catalyzing the initial step of glycogen breakdown. Enzymatic tests revealed that the PYGM mutation impairs the AMP-independent myophosphorylase activity, whereas the AMP-dependent activity was preserved. Further functional investigations demonstrated an altered conformation and aggregation of mutant myophosphorylase, and the concurrent accumulation of the intermediate filament desmin in the myofibers of the patients.
Interpretation: Overall, this study describes the first example of a dominant glycogen storage disease in humans, and elucidates the underlying pathomechanisms by deciphering the sequence of events from the PYGM mutation to the accumulation of glycogen in the muscle fibers. ANN NEUROL 2020;88:274-282.
(© 2020 American Neurological Association.)

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