ArticleBiophysical journal2004
Diffusion of single cardiac ryanodine receptors in lipid bilayers is decreased by annexin 12.
Article in Biophysical journal, 2004. 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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Who cites it
3 citing papers in PubMed, 19 citations in OpenAlex.
- Flux regulation of cardiac ryanodine receptor channels.The Journal of general physiology · 2010Article
- "Optical patch-clamping": single-channel recording by imaging Ca2+ flux through individual muscle acetylcholine receptor channels.The Journal of general physiology · 2005Article
- Imaging single cardiac ryanodine receptor Ca2+ fluxes in lipid bilayers.Biophysical journal · 2004Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Diffusion of cardiac ryanodine receptors (RyR2) in lipid bilayers was characterized. RyR2 location was monitored by imaging fluo-3 fluorescence due to Ca2+ flux through RyR2 channels or fluorescence from RyR2 conjugated with Alexa 488 or containing green fluorescent protein. Single channel currents were recorded to ensure that functional channels were studied. RyR2 exhibited an apparent diffusion coefficient (DRyR) of 1.2 x 10(-8) cm2 s(-1) and a mean path length of 5.0 microm. Optimal use of optical methods for analysis of RyR2 channel function requires that RyR2 diffusion be limited. Therefore, we tested the effect of annexin 12, which interacts with anionic phospholipids in a Ca2+-dependent manner. Addition of annexin 12 (0.25-4.0 microM) to the trans side of bilayers containing an 80:20 ratio of phosphatidylethanolamine/phosphatidylserine decreased RyR2 diffusion in a concentration-dependent manner. Annexin 12 (2 microM) decreased the apparent DRyR 683-fold from 1.2-10(-8) to 1.8 x 10(-11) cm2 s(-1) and the mean path length 10-fold from 5.0 to 0.5 micro m without obvious changes in the conductance of the native bilayer or in activation of RyR2 channels by Ca2+ or suramin. Thus, annexin 12 may provide a useful tool for optimizing optical analysis of RyR2 channels in lipid bilayers.
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