ArticleThe Journal of cell biology1985
The presence of two skeletal muscle alpha-actinins correlates with troponin-tropomyosin expression and Z-line width.
Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 48 citations in OpenAlex.
- Motor dysfunction iniScience · 2022Article
- Article
- Electron microscopy and x-ray diffraction evidence for two Z-band structural states.Biophysical journal · 2011Article
- A nebulin ruler does not dictate thin filament lengths.Biophysical journal · 2009Article
- Architecture of the thin filament-Z-line junction: lessons from nebulette and nebulin homologies.Journal of muscle research and cell motility · 2000Article
- Intermediate filament proteins increase during chronic stimulation of skeletal muscle.Journal of muscle research and cell motility · 1995Article
- Compliance of thin filaments in skinned fibers of rabbit skeletal muscle.Biophysical journal · 1995Article
- Structurally different Drosophila striated muscles utilize distinct variants of Z-band-associated proteins.Journal of muscle research and cell motility · 1991Article
- Z-band proteins in the flight muscle and leg muscle of the honeybee.Journal of muscle research and cell motility · 1990Article
- Alpha-actinin synthesis can be modulated by antisense probes and is autoregulated in non-muscle cells.The EMBO journal · 1989Article
- Three myosin heavy chain isoforms in type 2 skeletal muscle fibres.Journal of muscle research and cell motility · 1989Article
- Detection of a specific isoform of alpha-actinin with antisera directed against dystrophin.The Journal of cell biology · 1989Article
- The extent of amino-terminal heterogeneity in rabbit fast skeletal muscle troponin T.Journal of muscle research and cell motility · 1987Article
- Patterns of troponin T expression in mammalian fast, slow and promiscuous muscle fibres.Journal of muscle research and cell motility · 1987Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Two species of alpha-actinin from rabbit fast skeletal muscles were identified with a monospecific antisera. Designated alpha-actinin1f and alpha-actinin2f, their distribution in muscles does not correlate with histochemically defined fast fiber type. Rather, the presence of each correlates with Z-line width and with the expression of different thin filament Ca2+-regulatory complexes. alpha-Actinin1f is expressed with troponin T 1f-alpha beta tropomyosin, and alpha-actinin2f with troponin T 2f-alpha 2 tropomyosin. CNBr peptide maps show that the fast alpha-actinin species differ in primary structure. In contrast, the slow alpha-actinin is indistinguishable from alpha-actinin1f. Further evidence for the similarity of alpha-actinin1f and slow alpha-actinin comes from electron microscopic studies which show that fibers that express these species exhibit thick Z-lines. So, unlike other contractile proteins, the multiple forms of alpha-actinin do not reflect the distinction between fast- and slow-twitch muscles.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.