Adaptation of Single Cardiac Ryanodine Receptor Channels

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Adaptation of single cardiac ryanodine receptor channels.

Single cardiac ryanodine receptor (RyR) channel adaptation was previously defined with Ca2+ stimuli produced by flash photolysis of DM-nitrophen (caged-Ca+2). Photolysis of DM-nitrophen induced a very fast Ca+2 overshoot (Ca+2 spike) at the leading edge of the Ca+2 stimuli. It has been suggested that adaptation (tau approximately 1.3 s) may reflect Ca+2 slowly coming off the RyR Ca+2 activation...

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Flux regulation of cardiac ryanodine receptor channels

The cardiac type 2 ryanodine receptor (RYR2) is activated by Ca2+-induced Ca2+ release (CICR). The inherent positive feedback of CICR is well controlled in cells, but the nature of this control is debated. Here, we explore how the Ca2+ flux (lumen-to-cytosol) carried by an open RYR2 channel influences its own cytosolic Ca2+ regulatory sites as well as those on a neighboring channel. Both flux-d...

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Modulation of Cardiac Ryanodine Receptor Channels by Alkaline Earth Cations

Cardiac ryanodine receptor (RyR2) function is modulated by Ca(2+) and Mg(2+). To better characterize Ca(2+) and Mg(2+) binding sites involved in RyR2 regulation, the effects of cytosolic and luminal earth alkaline divalent cations (M(2+): Mg(2+), Ca(2+), Sr(2+), Ba(2+)) were studied on RyR2 from pig ventricle reconstituted in bilayers. RyR2 were activated by M(2+) binding to high affinity activ...

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Ryanodine Receptor Adaptation

signal activates specialized Ca 2 1 release channels, the ryanodine receptors (RyRs), in the sarcoplasmic reticulum (SR). This process is called Ca 2 1 -induced Ca 2 1 release (CICR). Intuitively, the CICR process should be self-regenerating because the Ca 2 1 released from the SR should feedback and activate further SR Ca 2 1 release. However, the CICR process is precisely controlled in the he...

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Interactions of a Reversible Ryanoid (21-Amino-9α-Hydroxy-Ryanodine) with Single Sheep Cardiac Ryanodine Receptor Channels

The binding of ryanodine to a high affinity site on the sarcoplasmic reticulum Ca2+-release channel results in a dramatic alteration in both gating and ion handling; the channel enters a high open probability, reduced-conductance state. Once bound, ryanodine does not dissociate from its site within the time frame of a single channel experiment. In this report, we describe the interactions of a ...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 1997

ISSN: 0006-3495

DOI: 10.1016/s0006-3495(97)78705-8