Characterization of junctional and longitudinal sarcoplasmic reticulum from heart muscle.

Inui, Makoto; Wang, S; Saito, A; Fleischer, Sidney

doi:10.1016/s0021-9258(18)38047-5

Cited by 88 publications

(8 citation statements)

References 22 publications

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“…This means that ruthenium red added subsequent to ryanodine cannot close the channels and Ca2+ loading is not enhanced by ruthenium red (Fleischer et al, 1985). The low-affinity ryanodine binding in heart terminal cisternae was correlated with a closing of the channels, thereby enhancing Ca2+ loading (Inui et al, 1988). We now correlate the low-affinity ryanodine binding in skeletal muscle SR also with the pharmacologic effect of closing the channels.…”

Section: Resultsmentioning

confidence: 69%

“…"This value is the standard error in the line. ''Data from Inui et al (1988). figure 5: High concentrations of ryanodine close the calcium release channels in terminal cisternae of skeletal muscle SR. (A) Ca2+ loading is enhanced by preincubation with ryanodine.…”

Section: Resultsmentioning

confidence: 99%

“…Aliquots (50 µg) were then added into the Ca2+ loading assay medium (Fleischer et al, 1985;Inui et al, 1988). The Ca2+ loading assay medium in 1 mL contained 100 mM potassium phosphate buffer (pH 7.0), 1 mM MgCl2, 5 mM NaN3, and 0.…”

Section: Methodsmentioning

confidence: 99%

“…The binding has been characterized as having a very slow dissociation rate (f1/2 > 14 h) (Pessah et al, 1987). Further, the binding of ryanodine to skeletal terminal cisternae displayed a single type of binding (high affinity) (Pessah, 1985;Fleischer et al, 1985), whereas in heart, two types of binding (high and low affinity) were observed (Pessah et al, 1986(Pessah et al, ,1987Inui et al, 1988Inui et al, ,1987b. This study investigates further the binding of ryanodine to sarcoplasmic reticulum fractions of heart and skeletal muscle.…”

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confidence: 90%

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Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle

McGrew¹,

Wolleben²,

Siegl³

et al. 1989

Biochemistry

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Ryanodine is a specific ligand for the calcium release channel which mediates calcium release in excitation-contraction coupling in muscle. In this study, ryanodine binding in sarcoplasmic reticulum from heart muscle and skeletal muscle is further compared and correlated with function. The new findings include the following: (1) Two types of binding, high affinity (KD1 approximately 5-10 nM) and low affinity (KD2 approximately 3 microM), can now be discerned for the skeletal muscle receptor. KD1 is approximately the same as and KD2 of similar magnitude to that previously reported for heart. (2) The dissociation rates for the high-affinity binding have been directly measured for both heart and skeletal muscle (t1/2 approximately 30-40 min). These rates are more rapid than previously reported (t1/2 approximately 14 h). (3) KD1's obtained from the ratio of the dissociation and association rate constants agree with the dissociation constant measured by equilibrium binding Scatchard analysis. (4) Ryanodine binding to the low-affinity site can be correlated with a decrease in the dissociation rate constant (k-1) of the high-affinity site, and thereby in the apparent dissociation constant (KD1). The inhibition constant (KI) for inhibiting the high-affinity off rate obtained from a double-reciprocal plot of the change in off rate vs [ryanodine] is practically the same in heart (0.66 microM) and skeletal muscle (0.64 microM) and in the range of the KD2. The binding of cold ryanodine to the low-affinity site appears to lock the bound [3H]ryanodine onto the high-affinity site rather than to exchange with it. Thus, in this sense, the ryanodine receptor exhibits "positive cooperativity".(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 90%

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Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle

McGrew¹,

Wolleben²,

Siegl³

et al. 1989

Biochemistry

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“…Cardiac microsomes were 1 Abbreviations: SDS-PAGE, polyacrylamide gel electrophoresis in sodium dodecyl sulfate; SR, sarcoplasmic reticulum; HMW polypeptide, high molecular weight polypeptide. prepared from canine heart as described by Inui et al (1988) with the omission of DTT in the preparation procedure. Triads were prepared from rabbit skeletal muscle according to Mitchell et al (1983).…”

Section: Methodsmentioning

confidence: 99%

Comparison of the calcium release channel of cardiac and skeletal muscle sarcoplasmic reticulum by target inactivation analysis

McGrew¹,

Inui²,

Chadwick³

et al. 1989

Biochemistry

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The calcium release channel of sarcoplasmic reticulum which triggers muscle contraction in excitation-contraction coupling has recently been isolated. The channel has been found to be morphologically identical with the feet structures of the junctional face membrane of terminal cisternae and consists of an oligomer of a unique high molecular weight polypeptide. In this study, we compare the target size of the calcium release channel from heart and skeletal muscle using target inactivation analysis. The target molecular weights of the calcium release channel estimated by measuring ryanodine binding after irradiation are similar for heart (139,000) and skeletal muscle (143,000) and are smaller than the monomeric unit (estimated to be about 360,000). The target size, estimated by measuring polypeptide remaining after irradiation, was essentially the same for heart and skeletal muscle, 1,061,000 and 1,070,000, respectively, indicating an oligomeric association of protomers. Thus, the calcium release channel of both cardiac and skeletal muscle reacts uniquely with regard to target inactivation analysis in that (1) the size by ryanodine binding is smaller than the monomeric unit and (2) a single hit leads to destruction of more than one polypeptide, by measuring polypeptide remaining. Our target inactivation analysis studies indicate that heart and skeletal muscle receptors are structurally very similar.

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Design Principles of Reptilian Muscles: Calcium Cycling Strategies

Perni

Franzini‐Armstrong

2015

The Anatomical Record

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The ultrastructure of the sarcoplasmic reticulum (SR) in skeletal muscles was compared among different reptile species (watersnake, boa constrictor, lizard, and turtle) and a mammal (mouse). Morphometric analysis demonstrates a pattern of increasing calsequestrin (CASQ) content in the lumen of SR from turtle to lizard, watersnake, and boa constrictor, and this content is in all cases higher than in mouse. In all reptiles sampled except turtle, CASQ is not confined to the junctional sarcoplasmic reticulum (jSR) cisternae as it is in other species. It instead fills the entire longitudinal (free) SR (fSR) regions, and in the extreme case of snakes, the shape of the SR is modified around the extra CASQ. We suggest that high CASQ content may represent an ATP-saving adaptation that permits relatively low metabolic rates during prolonged periods of fasting and inactivity, particularly in watersnake and boa constrictor. Anat Rec, 299:352-360, 2016. V C 2015 Wiley Periodicals, Inc.

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Characterization of junctional and longitudinal sarcoplasmic reticulum from heart muscle.

Cited by 88 publications

References 22 publications

Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle

Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle

Comparison of the calcium release channel of cardiac and skeletal muscle sarcoplasmic reticulum by target inactivation analysis

Design Principles of Reptilian Muscles: Calcium Cycling Strategies

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