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

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.

1989 ◽  
Vol 3 (1) ◽  
pp. 1-9
Author(s):  
Masaki Wakamatsu ◽  
Michio Yamamoto ◽  
Yutaka Kirino ◽  
Hiromi Katoh ◽  
Hiroyuki Shimonaka ◽  
...  

1998 ◽  
Vol 335 (3) ◽  
pp. 541-547 ◽  
Author(s):  
Naohiro YAMAGUCHI ◽  
Michiki KASAI

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.


2002 ◽  
Vol 16 (1) ◽  
pp. 70-71
Author(s):  
Tetsuo Takaya ◽  
Kenji Ito ◽  
Mamoru Takiguchi ◽  
Yasuko Ichihara ◽  
Junji Sasaki ◽  
...  

1989 ◽  
Vol 3 (2) ◽  
pp. 243-243
Author(s):  
Masaki Wakamatsu ◽  
Michio Yamamoto ◽  
Yutaka Kirino ◽  
Hiromi Katoh ◽  
Hiroyuki Shimonaka ◽  
...  

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