Abstract
Ca(2+) channel properties of the mink ryanodine receptor type 3 (RyR3), expressed in HEK293 cells, were studied in planar lipid bilayers to which RyR3 rich membrane fragments had been fused. RyR3 channels were not active at resting levels of Ca(2+)(free) but were gated by an additional 1 mM ATP, exhibiting long open times. The second major finding was the absence of channel inactivation at millimolar Ca(2+)(free). Insertion of a myc tag at the N-terminus of RyR3 did not affect the channel properties. As to skeletal muscle, the observed type 3 channel properties appear physiologically meaningful by assisting type 1 channels in calcium release.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Adenosine Triphosphate / pharmacology*
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Animals
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Calcium / metabolism*
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Calcium / pharmacology
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Cell Line
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Electric Conductivity
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Humans
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Ion Channel Gating / drug effects*
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Kinetics
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Lipid Bilayers / metabolism
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Microsomes / drug effects
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Microsomes / metabolism
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Mink
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Ryanodine Receptor Calcium Release Channel / chemistry
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Ryanodine Receptor Calcium Release Channel / genetics
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Ryanodine Receptor Calcium Release Channel / metabolism*
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Sarcoplasmic Reticulum / drug effects
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Sarcoplasmic Reticulum / metabolism
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Transfection
Substances
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Lipid Bilayers
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Protein Isoforms
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Recombinant Fusion Proteins
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Ryanodine Receptor Calcium Release Channel
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Adenosine Triphosphate
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Calcium