Postulated role of interdomain interactions within the type 1 ryanodine receptor in the low gain of Ca -induced Ca release activity of mammalian skeletal muscle sarcoplasmic reticulum

نویسندگان

  • Takashi Murayama
  • Toshiharu Oba
  • Shigeki Kobayashi
  • Noriaki Ikemoto
  • Yasuo Ogawa
چکیده

Takashi Murayama, Toshiharu Oba, Shigeki Kobayashi, Noriaki Ikemoto, and Yasuo Ogawa Department of Pharmacology, Juntendo University School of Medicine, Tokyo; Department of Regulatory Cell Physiology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan; Boston Biomedical Research Institute, Watertown; and Department of Neurology, Harvard Medical School, Boston, Massachusetts

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Postulated role of interdomain interactions within the type 1 ryanodine receptor in the low gain of Ca2+-induced Ca2+ release activity of mammalian skeletal muscle sarcoplasmic reticulum.

Ryanodine receptor (RyR) type 1 (RyR1) exhibits a markedly lower gain of Ca(2+)-induced Ca(2+) release (CICR) activity than RyR type 3 (RyR3) in the sarcoplasmic reticulum (SR) of mammalian skeletal muscle (selective stabilization of the RyR1 channel), and this reduction in the gain is largely eliminated using 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). We have invest...

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Mutations of Ca(2+)-activated proteases (calpains) cause muscular dystrophies. Nevertheless, the specific role of calpains in Ca(2+) signalling during the onset of dystrophies remains unclear. We investigated Ca(2+) handling in skeletal cells from calpain 3-deficient mice. [Ca(2+)](i) responses to caffeine, a ryanodine receptor (RyR) agonist, were decreased in -/- myotubes and absent in -/- myo...

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Postulated role of interdomain interaction between regions 1 and 2 within type 1 ryanodine receptor in the pathogenesis of porcine malignant hyperthermia.

We have demonstrated recently that CICR (Ca2+-induced Ca2+ release) activity of RyR1 (ryanodine receptor 1) is held to a low level in mammalian skeletal muscle ('suppression' of the channel) and that this is largely caused by the interdomain interaction within RyR1 [Murayama, Oba, Kobayashi, Ikemoto and Ogawa (2005) Am. J. Physiol. Cell Physiol. 288, C1222-C1230]. To test the hypothesis that ab...

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Nicotinic acid-adenine dinucleotide phosphate activates the skeletal muscle ryanodine receptor.

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تاریخ انتشار 2005