Structural and Functional Characterization of the Purified Cardiac Ryanodine Receptor-Ca2+ Release Channel Complex

Anderson, Kristin A.; Lai, F. Anthony; Liu, Qi-Yi; Rousseau, Éric; Erickson, H P; Meissner, Gerhard

doi:10.1016/s0021-9258(19)85090-1

Cited by 206 publications

(27 citation statements)

References 36 publications

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“…Channels present in SR vesicles isolated from mammalian cardiac muscle show sigmoidal activation by cis M [Ca 2ϩ ]. Most reports show a lack of inhibition by increasing [Ca 2ϩ ] up to 1-2 mM (Rousseau et al, 1986;Anderson et al, 1989;Holmberg and Williams, 1990;Chu et al, 1993). This type of calcium dependence will be named the C calcium dependence (for cardiac).…”

Section: Introductionmentioning

confidence: 99%

Sulfhydryl Oxidation Modifies the Calcium Dependence of Ryanodine-Sensitive Calcium Channels of Excitable Cells

Marengo

Hidalgo

Bull

1998

Biophysical Journal

196

155

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The calcium dependence of ryanodine-sensitive single calcium channels was studied after fusing with planar lipid bilayers sarcoendoplasmic reticulum vesicles isolated from excitable tissues. Native channels from mammalian or amphibian skeletal muscle displayed three different calcium dependencies, cardiac (C), mammalian skeletal (MS), and low fractional open times (low Po), as reported for channels from brain cortex. Native channels from cardiac muscle presented only the MS and C dependencies. Channels with the MS or low Po behaviors showed bell-shaped calcium dependencies, but the latter had fractional open times of <0.1 at all [Ca2+]. Channels with C calcium dependence were activated by [Ca2+] < 10 microM and were not inhibited by increasing cis [Ca2+] up to 0.5 mM. After oxidation with 2,2'-dithiodipyridine or thimerosal, channels with low Po or MS dependencies increased their activity. These channels modified their calcium dependencies sequentially, from low Po to MS and C, or from MS to C. Reduction with glutathione of channels with C dependence (native or oxidized) decreased their fractional open times in 0.5 mM cis [Ca2+], from near unity to 0.1-0.3. These results show that all native channels displayed at least two calcium dependencies regardless of their origin, and that these changed after treatment with redox reagents.

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Section: Introductionmentioning

confidence: 99%

Sulfhydryl Oxidation Modifies the Calcium Dependence of Ryanodine-Sensitive Calcium Channels of Excitable Cells

Marengo

Hidalgo

Bull

1998

Biophysical Journal

196

155

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“…These limitations have been overcome by the purification of the SR Ca 2+ release channel protein and its consequent separation from other SR channel species. Purification has been aided by the specific, high affinity interaction of ryanodine with the SR Ca 2+ release channel (Inui, Saito, and Fleischer, 1987a, b;Lai, Erickson, Rousseau, Liu, and Meissner, 1988a, b;Smith, Imagawa, Ma, Fill, Campbell, and Coronado, 1988;Anderson, Lai, Liu, Rousseau, Erickson, and Meissner, 1989). The purified ryanodine receptors of skeletal (Smith et al, 1988;Lai et al, 1988b) and cardiac (Lai et al, 1988a;Anderson et al, 1989) muscle function as ligand-regulated, cation-selective channels displaying a range of gating and conduction properties characteristic of the native SR Ca z+ release channel.…”

Section: Introductionmentioning

confidence: 99%

Divalent cation conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum.

Tinker

Williams

1992

The Journal of General Physiology

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A B S T R A C T The conduction properties of the alkaline earth divalent cations were determined in the purified sheep cardiac sarcoplasmic reticulum ryanodine receptor channel after reconstitution into planar phospholipid bilayers. Under bi-ionic conditions there was little difference in permeability among Ba 2÷, Ca ~+, Sr ~+, and Mg 2÷. However, there was a significant difference between the divalent cations and K +, with the divalent cations between 5.8-and 6.7-fold more permeant. Singlechannel conductances were determined under symmetrical ionic conditions with 210 mM Ba ~÷ and Sr 2+ and from the single-channel current-voltage relationship under bi-ionic conditions with 210 mM divalent cations and 210 mM K +. Singlechannel conductance ranged from 202 pS for Ba 2+ to 89 pS for Mg 2+ and fell in the sequence Ba 2+ > Sr 2+ > Ca ~+ > Mg 2+. Near-maximal single-channel conductance is observed at concentrations as low as 2 mM Ba 2+. Single-channel conductance and current measurements in mixtures of Ba2+-Mg 2+ and Ba2+-Ca 2+ reveal no anomalous behavior as the mole fraction of the ions is varied. The Ca2+-K + reversal potential determined under bi-ionic conditions was independent of the absolute value of the ion concentrations. The data are compatible with the ryanodine receptor channel acting as a high conductance channel displaying moderate discrimination between divalent and monovalent cations. The channel behaves as though ion translocation occurs in single file with at most one ion able to occupy the conduction pathway at a time.

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“…Muscle contraction is initiated by the rapid release of Ca2" through the sarcoplasmic reticulum Ca2" release channel (1, 2). The Ca2' release channels of both skeletal and cardiac SR have been intensively investigated (3)(4)(5). If the SR membrane were permeable only to Ca2 , its membrane potential would very rapidly approach the Ca2' equilibrium potential, and Ca2' release would dramatically decrease (6,7).…”

Section: Introductionmentioning

confidence: 99%

Blockade of cardiac sarcoplasmic reticulum K+ channel by Ca2+: two-binding-site model of blockade

Liu

Strauss

1991

Biophysical Journal

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Potassium countercurrent through the SR K+ channel plays an important role in Ca2+ release from the SR. To see if Ca2+ regulates the channel, we incorporated canine cardiac SR K+ channel into lipid bilayers. Calcium ions present in either the SR lumenal (trans) or cytoplasmic (cis) side blocked the cardiac SR K+ channel in a voltage-dependent manner. When Ca2+ was present on both sides, however, the block appeared to be voltage independent. A two-binding site model of blockade by an impermeant divalent cation (Ca2+) can explain this apparent contradiction. Estimates of SR Ca2+ concentration suggest that under physiological conditions the cardiac SR K+ channel is partially blocked by Ca2+ ions present in the lumen of the SR. The reduction in lumenal [Ca2+] during Ca2+ release could increase K+ conductance.

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Structural and Functional Characterization of the Purified Cardiac Ryanodine Receptor-Ca2+ Release Channel Complex

Cited by 206 publications

References 36 publications

Sulfhydryl Oxidation Modifies the Calcium Dependence of Ryanodine-Sensitive Calcium Channels of Excitable Cells

Sulfhydryl Oxidation Modifies the Calcium Dependence of Ryanodine-Sensitive Calcium Channels of Excitable Cells

Divalent cation conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum.

Blockade of cardiac sarcoplasmic reticulum K+ channel by Ca2+: two-binding-site model of blockade

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