IBM-type inclusions in a patient with slow-channel syndrome caused by a mutation in the AChR epsilon subunit
| Autor: | Barbara Ryniewicz, Xing Ming Shen, Andrew G. Engel, Anna Fidziańska |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Adult
Pathology medicine.medical_specialty Patch-Clamp Techniques DNA Mutational Analysis Molecular Sequence Data Receptors Nicotinic Biology Transfection medicine.disease_cause Inclusion bodies Cell Line Membrane Potentials Myositis Inclusion Body Radioligand Assay Microscopy Electron Transmission Iodine Isotopes Internal medicine medicine Humans Muscle Skeletal Receptor Genetics (clinical) Myositis Acetylcholine receptor Myasthenic Syndromes Congenital Mutation Dose-Response Relationship Drug Skeletal muscle Valine Congenital myasthenic syndrome Bungarotoxins medicine.disease Acetylcholine Endocrinology medicine.anatomical_structure Neurology Pediatrics Perinatology and Child Health Female Neurology (clinical) Inclusion body myositis Protein Binding |
| Zdroj: | Neuromuscular Disorders. 15:753-759 |
| ISSN: | 0960-8966 |
| DOI: | 10.1016/j.nmd.2005.07.009 |
| Popis: | We report a patient with a slow-channel congenital myasthenic syndrome who carries a novel slow-channel mutation in the epsilon subunit of the acetylcholine receptor and has tubulofilamentous inclusion bodies, in skeletal muscle of the type observed in hereditary and sporadic inclusion body myositis. Ultrastructural analysis of a muscle specimen obtained at the age of 9 years showed an endplate myopathy typical of the slow-channel syndrome. Twenty years later, a second muscle specimen again showed the endplate myopathy as well numerous nuclear and cytoplasmic tubulofilamentous inclusion bodies. Molecular genetic studies revealed a novel valine to phenylalanine mutation (epsilonV259F) in the M2 domain of the acetylcholine receptor. Coexistence of the slow-channel syndrome with a feature of IBM has not been observed before. |
| Databáze: | OpenAIRE |
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