ArticleJournal of muscle research and cell motility1999
Exchange of alpha-actinin in isolated rigor myofibrils.
Article in Journal of muscle research and cell motility, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- α-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly.Molecular biology of the cell · 2012Article
- Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrils.Biophysical journal · 2009Article
- Properties of easily releasable myofilaments: are they the first step in myofibrillar protein turnover?American journal of physiology. Cell physiology · 2009Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the current study, the process of alpha-actinin binding to the myofibrillar Z-line was investigated to determine its mechanism. Pretreatment of rigor myofibrils with unlabeled alpha-actinin did not prevent or slow the incorporation of fluorescein skeletal alpha-actinin into myofibrils suggesting that incorporation was not the filling of empty binding sites but rather an exchange reaction. Further support for this was obtained using quantitative measures of labeled alpha-actinin incorporation and measures of total myofibrillar alpha-actinin. These results showed that there was no change in myofibrillar alpha-actinin content when up to 15% of the total alpha-actinin was the labeled protein. Measurement of the time-course of fluorescein alpha-actinin incorporation by quantitative fluorescence microscopy showed that the increase in Z-line fluorescence was well described by a rapid (unresolved) incorporation of fluorescence followed by a much slower phase. The slower phase was independent of fluorescein alpha-actinin concentration (2.5-160 nM) and had an apparent rate of 0.008-0.016 min(-1). Pretreatment of myofibrils with fluorescein alpha-actinin followed by incubation with unlabeled alpha-actinin resulted in a decrease in Z-line fluorescence with an apparent rate of 0.021 min(-1). The slow phase was interpreted as representing the dissociation rate of intrinsic Z-line alpha-actinin. Thus, the dissociation rate for the in situ interaction of alpha-actinin with actin appears to be three orders of magnitude slower than that determined from solution studies.
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