TY - JOUR
T1 - Histopathologic Marks of Tongue in a Mouse Model of Oculopharyngeal Muscular Dystrophy Suggest Biomechanical Defects
AU - Kordikowski Boix, Rebecca
AU - Bos, Erik
AU - Shademan, Milad
AU - Mallon, Sander
AU - van Zanen-Gerhardt, Sofie
AU - Lu-Nguyen, Ngoc
AU - Malerba, Alberto
AU - Coenen de Roo, Christina J J
AU - Raz, Vered
N1 - Copyright © 2025 American Society for Investigative Pathology. Published by Elsevier Inc. All rights reserved.
PY - 2025/4
Y1 - 2025/4
N2 - Difficulty swallowing (dysphagia) is common in the elderly population and in patients with adult-onset neuromuscular disease. In oculopharyngeal muscular dystrophy (OPMD), dysphagia is often the first symptom. OPMD is an autosomal-dominant myopathy caused by a trinucleotide-expansion mutation in the gene encoding poly(A) binding protein nuclear 1 (PABPN1). Expanded-mutant PABPN1 forms insoluble nuclear aggregates that reduce the levels of the soluble form. Clinical tongue involvement in OPMD has been documented but is poorly understood. Histopathologic analysis of the tongue in an OPMD mouse model was done by light and electron microscopy combined with RNA sequencing. PABPN1 nuclear aggregates were found at moderate levels, whereas deposition of insoluble PABPN1 in blood vessels was prominent already at 4 months of age. Muscle wasting of the tongue was age associated. RNA signatures of the OPMD tongue were enriched for mitochondrial and cytoskeletal genes. Electron microscopy revealed abnormalities in sarcomere and mitochondria organization in A17/+ mice, suggesting an energy and contractile deficit in OPMD tongue. This detailed analysis of the histopathology of the tongue in the A17/+ mouse model opens new avenues for understanding the mechanisms of dysphagia.
AB - Difficulty swallowing (dysphagia) is common in the elderly population and in patients with adult-onset neuromuscular disease. In oculopharyngeal muscular dystrophy (OPMD), dysphagia is often the first symptom. OPMD is an autosomal-dominant myopathy caused by a trinucleotide-expansion mutation in the gene encoding poly(A) binding protein nuclear 1 (PABPN1). Expanded-mutant PABPN1 forms insoluble nuclear aggregates that reduce the levels of the soluble form. Clinical tongue involvement in OPMD has been documented but is poorly understood. Histopathologic analysis of the tongue in an OPMD mouse model was done by light and electron microscopy combined with RNA sequencing. PABPN1 nuclear aggregates were found at moderate levels, whereas deposition of insoluble PABPN1 in blood vessels was prominent already at 4 months of age. Muscle wasting of the tongue was age associated. RNA signatures of the OPMD tongue were enriched for mitochondrial and cytoskeletal genes. Electron microscopy revealed abnormalities in sarcomere and mitochondria organization in A17/+ mice, suggesting an energy and contractile deficit in OPMD tongue. This detailed analysis of the histopathology of the tongue in the A17/+ mouse model opens new avenues for understanding the mechanisms of dysphagia.
KW - Animals
KW - Muscular Dystrophy, Oculopharyngeal/pathology
KW - Tongue/pathology
KW - Disease Models, Animal
KW - Mice
KW - Deglutition Disorders/pathology
KW - Poly(A)-Binding Protein I/genetics
KW - Biomechanical Phenomena
KW - Male
U2 - 10.1016/j.ajpath.2024.12.009
DO - 10.1016/j.ajpath.2024.12.009
M3 - Article
C2 - 39800052
SN - 0002-9440
VL - 195
SP - 741
EP - 753
JO - American Journal of Pathology
JF - American Journal of Pathology
IS - 4
ER -