Abstract
Cultured muscle fibers (CMF) from a patient with inclusion-body myositis (IBM) and cardiac amyloidosis associated with the transthyretin (TTR) Val122Ile mutation contained aspects of the IBM phenotype: vacuolation, congophilic inclusions, and clusters of immunocolocalizing amyloid beta-peptide (Abeta) and TTR accumulations. These abnormalities are never present in normal human CMF. These perturbations were greatly increased after Abeta precursor protein gene transfer. The TTR mutation may be a genetic predisposition factor for the patient's IBM.
Publication types
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Case Reports
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aged
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Amino Acid Substitution*
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Amyloid / chemistry*
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Amyloid beta-Peptides / analysis*
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Amyloid beta-Peptides / biosynthesis
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Amyloid beta-Protein Precursor / genetics
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Cell Death
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Cells, Cultured / chemistry
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Coloring Agents
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Congo Red
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DNA, Complementary / genetics
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Genes, Dominant
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Genetic Predisposition to Disease
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Humans
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Immunohistochemistry
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Lysosomes / ultrastructure
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Male
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Microscopy, Fluorescence
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Muscle, Skeletal / chemistry
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Muscle, Skeletal / pathology
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Mutation, Missense*
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Myositis, Inclusion Body / genetics*
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Myositis, Inclusion Body / metabolism
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Myositis, Inclusion Body / pathology
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Prealbumin / analysis
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Prealbumin / genetics*
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Recombinant Fusion Proteins / biosynthesis
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Vacuoles / ultrastructure
Substances
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Amyloid
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Amyloid beta-Peptides
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Amyloid beta-Protein Precursor
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Coloring Agents
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DNA, Complementary
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Prealbumin
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Recombinant Fusion Proteins
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Congo Red