Effects of anesthetic and related agents on calcium-induced calcium release from sarcoplasmic reticulum isolated from rabbit skeletal muscle

1989 ◽  
Vol 3 (1) ◽  
pp. 1-9
Author(s):  
Masaki Wakamatsu ◽  
Michio Yamamoto ◽  
Yutaka Kirino ◽  
Hiromi Katoh ◽  
Hiroyuki Shimonaka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Rabbit Skeletal Muscle ◽  
Calcium Induced Calcium Release

scholarly journals Erratum to: Effects of Anesthetic and Related Agents on Calcium-induced Calcium Release from Sarcoplasmic Reticulum Isolated from Rabbit Skeletal Muscle

1989 ◽  
Vol 3 (2) ◽  
pp. 243-243
Author(s):  
Masaki Wakamatsu ◽  
Michio Yamamoto ◽  
Yutaka Kirino ◽  
Hiromi Katoh ◽  
Hiroyuki Shimonaka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Rabbit Skeletal Muscle ◽  
Calcium Induced Calcium Release

scholarly journals Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum.

1988 ◽  
Vol 92 (1) ◽  
pp. 1-26 ◽  
Author(s):  
J S Smith ◽  
T Imagawa ◽  
J Ma ◽  
M Fill ◽  
K P Campbell ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Binding Capacity ◽  
Ruthenium Red ◽  
Rabbit Skeletal Muscle ◽  
Permeability Ratio ◽  
Calcium Release Channel ◽  
Release Channel

The ryanodine receptor of rabbit skeletal muscle sarcoplasmic reticulum was purified as a single 450,000-dalton polypeptide from CHAPS-solubilized triads using immunoaffinity chromatography. The purified receptor had a [3H]ryanodine-binding capacity (Bmax) of 490 pmol/mg and a binding affinity (Kd) of 7.0 nM. Using planar bilayer recording techniques, we show that the purified receptor forms cationic channels selective for divalent ions. Ryanodine receptor channels were identical to the Ca-release channels described in native sarcoplasmic reticulum using the same techniques. In the present work, four criteria were used to establish this identity: (a) activation of channels by micromolar Ca and millimolar ATP and inhibition by micromolar ruthenium red, (b) a main channel conductance of 110 +/- 10 pS in 54 mM trans Ca, (c) a long-term open state of lower unitary conductance induced by ryanodine concentrations as low as 20 nM, and (d) a permeability ratio PCa/PTris approximately equal to 14. In addition, we show that the purified ryanodine receptor channel displays a saturable conductance in both monovalent and divalent cation solutions (gamma max for K and Ca = 1 nS and 172 pS, respectively). In the absence of Ca, channels had a broad selectivity for monovalent cations, but in the presence of Ca, they were selectively permeable to Ca against K by a permeability ratio PCa/PK approximately equal to 6. Receptor channels displayed several equivalent conductance levels, which suggest an oligomeric pore structure. We conclude that the 450,000-dalton polypeptide ryanodine receptor is the Ca-release channel of the sarcoplasmic reticulum and is the target site of ruthenium red and ryanodine.

Chemical modification of calcium release from the sarcoplasmic reticulum of mechanically skinned skeletal bullfrog muscle fibers

1986 ◽  
Vol 64 (10) ◽  
pp. 1267-1271 ◽  
Author(s):  
Takako Aoki ◽  
Toshiharu Oba ◽  
Ken Hotta
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Release Mechanism ◽  
Trinitrobenzenesulfonic Acid ◽  
Amino Acid Side Chains ◽  
Chloramine T ◽  
Tension Curve ◽  
Calcium Induced Calcium Release

Several types of reagents that react with amino acid side chains induced repetitive phasic contracture of skinned skeletal muscle from frogs. The presence of 10 mM procaine or 5 mM magnesium in the medium or disruption of the sarcoplasmic reticulum (SR) eliminated this contracture, indicating that the calcium-induced calcium-release mechanism of SR is involved in the contraction. Dithiothreitol inhibited the contracture induced by chloramine T, N-acetylimidazole, or p-chloromercuriphenylsulfonic acid (pCMPS) but not in the case of carbodiimide, phenylglyoxal, trinitrobenzenesulfonic acid, diethylpyrocarbonate (DEP), or N-chlorosuccinimide (NCS). Therefore, modification of groups other than the sulfhydryl ones seems to induce contractures under such conditions. The amplitude of the caffeine-induced contracture decreased after treatment with pCMPS, DEP, or NCS. NCS shifted the pCa–tension curve toward low pCa in the SR-disrupted fibers. This shift would explain the decrease in caffeine contracture. It is tentatively concluded that pCMPS and DEP release a large amount of calcium from SR.

scholarly journals Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

FEBS Letters ◽  
1988 ◽  
Vol 238 (2) ◽  
pp. 240-244 ◽  
Author(s):  
Alexander M. Rubtsov ◽  
Peter J. Quinn ◽  
Alexander A. Boldyrev
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Rabbit Skeletal Muscle

scholarly journals Identification of 30 kDa calsequestrin-binding protein, which regulates calcium release from sarcoplasmic reticulum of rabbit skeletal muscle

1998 ◽  
Vol 335 (3) ◽  
pp. 541-547 ◽  
Author(s):  
Naohiro YAMAGUCHI ◽  
Michiki KASAI
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Amino Acid Sequence ◽  
Calcium Release ◽  
Rabbit Skeletal Muscle ◽  
Cloning And Sequencing ◽  
Partial Amino Acid Sequence ◽  
Release Channel ◽  
Disulphonic Acid

In a previous study [Yamaguchi, Kawasaki and Kasai (1995) Biochem. Biophys. Res. Commun. 210, 648–653], we showed that the stilbene derivative 4,4´-di-isothiocyanostilbene-2,2´-disulphonic acid activates the Ca2+ channel in the sarcoplasmic reticulum (SR) in rabbit skeletal muscle, and it does not bind to the channel protein itself but to the SR 30 kDa protein. Furthermore, the 30 kDa protein was shown to bind to calsequestrin (CSQ), which is one of the regulators of the Ca2+ release channel in the SR. In the present study, we determined the partial amino acid sequence of the CSQ-binding 30 kDa protein and, consequently, this protein was proved to be highly similar to ADP/ATP translocase (AAT) expressed in the mitochondria in a variety of cells. By Western-blotting analysis, the CSQ-binding 30 kDa protein was recognized by the antibody raised against bovine cardiac AAT and, furthermore, depolarization-induced Ca2+ release monitored in the rabbit skeletal muscle triads was significantly activated by the antibody. As a result of cloning and sequencing of the cDNA encoding AAT of the rabbit skeletal muscle, the amino acid sequence was found to be the same as that of the CSQ-binding 30 kDa protein determined above. Furthermore, the expressed product of the cDNA encoding AAT in Escherichia coliwas proved to bind to CSQ. These results suggest that AAT itself is expressed in the rabbit skeletal muscle SR and regulates the Ca2+ release from the SR; that is, excitation–contraction coupling of the skeletal muscle cell.

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