Control of Calcium Release in Functioning Skeletal Muscle Fibers

Schneider, Martin F.

doi:10.1146/annurev.ph.56.030194.002335

Cited by 294 publications

(178 citation statements)

References 67 publications

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“…It interacts with dihydropyridine receptor (DHPR) complexes, located in the transverse tubular membrane, and organizes them into tetrad arrays (10)(11)(12)(13). Structural changes in the DHPR, produced upon plasma membrane depolarization, result in RyR1-mediated Ca 2ϩ release from the SR (orthograde coupling) (14,15), whereas Ca 2ϩ entry from extracellular spaces through the DHPR ␣1-subunit (Ca V 1.1) is enhanced by retrograde interaction with RyR1. RyR1 is a homotetramer with a subunit mass of Ϸ565 kDa.…”

mentioning

confidence: 99%

An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

Zvaritch

Depreux

Kraeva

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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A heterozygous Ile4898 to Thr (I4898T) mutation in the human type 1 ryanodine receptor/Ca 2+ release channel (RyR1) leads to a severe form of central core disease. We created a mouse line in which the corresponding Ryr1 I4895T mutation was introduced by using a “knockin” protocol. The heterozygote does not exhibit an overt disease phenotype, but homozygous (IT/IT) mice are paralyzed and die perinatally, apparently because of asphyxia. Histological analysis shows that IT/IT mice have greatly reduced and amorphous skeletal muscle. Myotubes are small, nuclei remain central, myofibrils are disarranged, and no cross striation is obvious. Many areas indicate probable degeneration, with shortened myotubes containing central stacks of pyknotic nuclei. Other manifestations of a delay in completion of late stages of embryogenesis include growth retardation and marked delay in ossification, dermatogenesis, and cardiovascular development. Electron microscopy of IT/IT muscle demonstrates appropriate targeting and positioning of RyR1 at triad junctions and a normal organization of dihydropyridine receptor (DHPR) complexes into RyR1-associated tetrads. Functional studies carried out in cultured IT/IT myotubes show that ligand-induced and DHPR-activated RyR1 Ca 2+ release is absent, although retrograde enhancement of DHPR Ca 2+ conductance is retained. IT/IT mice, in which RyR1-mediated Ca 2+ release is abolished without altering the formation of the junctional DHPR-RyR1 macromolecular complex, provide a valuable model for elucidation of the role of RyR1-mediated Ca 2+ signaling in mammalian embryogenesis.

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mentioning

confidence: 99%

An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

Zvaritch

Depreux

Kraeva

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…In cardiac muscle, Ca 2+ -release from the sarcoplasmic reticulum (SR) is triggered by Ca 2+ entering the cell via L-type sarcolemmal Ca 2+ channels and is termed Ca 2+ -induced Ca 2+ -release (CICR) (Fabiato, 1985;Beuckelmann & Wier, 1988;Nabauer et al, 1989;Bers, 1991). In mammalian skeletal muscle, depolarization of the T-tubule membrane leads to SR Ca 2+ -release without the need for Ca 2+ entry and is termed voltage-dependent Ca 2+ -release (VDCR) or directlycoupled Ca 2+ -release (Schneider & Chandler, 1973;Ashley et al, 1991;Rios & Pizarro, 1991;Schneider, 1994). In both types of muscle, the SR Ca 2+ -release/ryanodine receptor channels (RyR) act as the pathway for Ca 2+ release into the cytoplasm.…”

Section: Introductionmentioning

confidence: 99%

Evidence for novel caffeine and Ca²⁺ binding sites on the lobster skeletal ryanodine receptor

Zhang¹,

Williams²,

Sitsapesan³

1999

British J Pharmacology

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1 The e ects of Ca 2+ , ATP and ca eine on the gating of lobster skeletal muscle ryanodine receptors (RyR) was investigated after reconstitution of the channels into planar phospholipid bilayers and by using [ 3 H]-ryanodine binding studies. 2 The single channel studies reveal that the EC 50 (60 mM) for activation of the lobster skeletal RyR by Ca 2+ as the sole ligand is higher than for any other isoform of RyR studied. 3 Inactivation of the channel by Ca 2+ (EC 50 =1 mM) occurs at concentrations slightly higher than those required to inactivate mammalian skeletal RyR (RyR1) but lower than those required to inactivate mammalian cardiac RyR (RyR2). 4 Lifetime analysis demonstrates that cytosolic Ca 2+ , as the sole activating ligand, cannot fully open the lobster skeletal RyR (maximum Po approximately 0.2). The mechanism for the increase in open probability (Po) is an increase in both the frequency and the duration of the open events. 5 ATP is a very e ective activator of the lobster RyR and can almost fully open the channel in the presence of activating cytosolic [Ca 2+ ]. In the presence of 700 mM Ca 2+ , 1 mM ATP increased Po to approximately 0.8. 6 Ca eine, often used as a tool to identify the presence of RyR channels, is relatively ine ective and cannot increase Po above the level that can be attained with Ca 2+ alone. 7 The results reveal that ca eine increases Po by a di erent mechanism to that of cytosolic Ca 2+ demonstrating that the mechanism for channel activation by ca eine is not`sensitization' to cytosolic Ca 2+ . 8 By studying the mechanisms involved in the activation of the lobster RyR we have demonstrated that the channel responds in a unique manner to Ca 2+ and to ca eine. The results strongly indicate that these ligand binding sites on the channel are di erent to those on mammalian isoforms of RyR.

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“…During the past 30 years, many properties of SR Ca release have been elucidated from studies on intact, cut, and skinned fibers, on iso-lated triads and SR vesicles, and on single SR Ca channels incorporated into lipid bilayers, as reviewed by Rios and Pizarro (1991), Schneider (1994), Meissner (1994), and Franzini-Armstrong andJorgensen (1994). The studies in intact and cut fibers have shown that the rate of Ca release from the SR into the myoplasm is under the control of the voltage across the membranes of the transverse tubular system.…”

Section: Introductionmentioning

confidence: 99%

A slow component of intramembranous charge movement during sarcoplasmic reticulum calcium release in frog cut muscle fibers.

Pape

Jong

Chandler

1996

The Journal of General Physiology

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Cut muscle fibers from Rana temporaria were mounted in a double Vaseline-gap chamber and equilibrated with an end-pool solution that contained 20 mM EGTA and 1.76 mM Ca (sarcomere length, temperature,[14][15][16] Sarcoplasmic reticulum (SR) Ca release, A[CaT], was estimated from changes in myoplasmic pH (Pape, P.C., D.-S. Jong, and W.K. Chandler. 1995. J. Gen. Physiol. 106:259-336). The maximal value of A[CaT] obtained during a depleting depolarization was assumed to equal the SR Ca content before stimulation, [CasR]R (expressed as myoplasmic concentration). After a depolarization to -55 to -40 mV in fibers with [CasR] R ---= 1,000-3,000 ~M, currents from intramembranous charge movement, Icm, showed an early I~ component. This was followed by an I v hump, which decayed within 50 ms to a small current that was maintained for as long as 500 ms. This slow current was probably a component of Icm because the amount of OFF charge, measured after depolarizations of different durations, increased according to the amount of ON charge. Icm was also measured after the SR had been depleted of most of its Ca, either by a depleting conditioning depolarization or by Ca removal from the end pools followed by a series of depleting depolarizations. The early I~ component was essentially unchanged by Ca depletion, the I v hump was increased (for [CasR]a > 200 ~M), the slow component was eliminated, and the total amount of OFF charge was essentially unchanged. These results suggest that the slow component of ON/~m is not movement of a new species of charge but is probably movement of Qv that is slowed by SR Ca release or some associated event such as the accompanying increase in myoplasmic free [Ca] that is expected to occur near the Ca release sites. The peak value of the apparent rate constant associated with this current, 2-4%/ms at pulse potentials between -48 and -40 mV, is decreased by half when [Casa]a --= 500-1,000 ~xM, which gives a peak rate of SR Ca release of N5-10 ~tM/ms.

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Control of Calcium Release in Functioning Skeletal Muscle Fibers

Cited by 294 publications

References 67 publications

An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

Evidence for novel caffeine and Ca²⁺ binding sites on the lobster skeletal ryanodine receptor

A slow component of intramembranous charge movement during sarcoplasmic reticulum calcium release in frog cut muscle fibers.

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Control of Calcium Release in Functioning Skeletal Muscle Fibers

Cited by 294 publications

References 67 publications

An Ryr1 I4895T mutation abolishes Ca 2+ release channel function and delays development in homozygous offspring of a mutant mouse line

An Ryr1 I4895T mutation abolishes Ca 2+ release channel function and delays development in homozygous offspring of a mutant mouse line

Evidence for novel caffeine and Ca2+ binding sites on the lobster skeletal ryanodine receptor

A slow component of intramembranous charge movement during sarcoplasmic reticulum calcium release in frog cut muscle fibers.

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An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

An Ryr1 ^I4895T mutation abolishes Ca ²⁺ release channel function and delays development in homozygous offspring of a mutant mouse line

Evidence for novel caffeine and Ca²⁺ binding sites on the lobster skeletal ryanodine receptor