ArticleActa neuropathologica1995
Tau protein immunoreactivity in muscle fibers with rimmed vacuoles differs from that in regenerating muscle fibers.
Article in Acta neuropathologica, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 14 citations in OpenAlex.
- The Interactions of Tau, RNA, and Stress Granules in Neurodegenerative Disease: A Comprehensive Review.Cells · 2026Review
- MAPT mutations in amyotrophic lateral sclerosis: clinical, neuropathological and functional insights.Journal of neurology · 2025Article
- A Combinatorial MAP Code Dictates Polarized Microtubule Transport.Developmental cell · 2020Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To determine whether tau protein found in muscle fibers with rimmed vacuoles and in regenerating fibers was phosphorylated, we examined eight muscle biopsy samples containing rimmed vacuoles (from five patients with distal myopathy with rimmed vacuole formation and three patients with inclusion body myositis) and three muscle biopsy samples from patients with Duchenne muscular dystrophy containing numerous regenerating fibers. Although both rimmed vacuolated and regenerating fibers had increased immunoreactivity against tubulin and tau protein, tau protein in the former was more highly phosphorylated than that in the latter. While very few microtubules in muscle fibers with rimmed vacuoles were recognizable by electron microscopy, regenerating fibers, especially immature ones, contained numerous microtubules. Since tau protein found in vacuolated fibers is hyperphosphorylated, it can be considered to have reduced ability to bind tubulin molecules. Thus, the tau protein cannot stabilize microtubules, resulting in their depolymerization even in the presence of tubulin molecules.
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