ArticleThe Journal of membrane biology2004
Regulation of muscle Cav1.1 channels by long-term depolarization involves proteolysis of the alpha1s subunit.
Article in The Journal of membrane biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
The trial behind it
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
2 citing papers in PubMed, 5 citations in OpenAlex.
- Article
- Sustained CGRP1 receptor stimulation modulates development of EC coupling by cAMP/PKA signalling pathway in mouse skeletal myotubes.The Journal of physiology · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The effects of long-term depolarization on frog skeletal muscle Cav1.1 channels were assessed. Voltage-clamp and Western-blot experiments revealed that long-term depolarization brings about a drastic reduction in the amplitude of currents flowing through Cav1.1 channels and in the levels of the alpha1s subunit, the main subunit of muscle L-type channels. The decline of both phenomena was prevented by the action of the protease inhibitors E64 (50 microM) and leupeptin (50 microM). In contrast, long-term depolarization had no effect on beta1, the auxiliary subunit of alpha1s. The levels of mRNAs coding the alpha1s and the beta1 subunits were measured by RNase protection assays. Neither the content of the alpha1s nor the beta1 subunit mRNAs were affected by long-term depolarization, indicating that the synthesis of Cav1.1 channels remained unaffected. Taken together, our experiments suggest that the reduction in the amplitude of membrane currents and in the alpha1s subunit levels is caused by increased degradation of this subunit by a Ca2+-dependent protease.
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Registered trials
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