메뉴 건너뛰기




Volumn 274, Issue 4 43-4, 1998, Pages

Sulfhydryls associated with H2O2-induced channel activation are on luminal side of ryanodine receptors

Author keywords

Calcium release channel; Frog skeletal muscle; p chloromercuriphenylsulfonic acid; Sulfhydryl oxidation

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; CATALASE; CHLOROMERCURIBENZENESULFONIC ACID; HYDROGEN PEROXIDE; RYANODINE RECEPTOR; THIOL DERIVATIVE; CALCIUM; THIOL REAGENT;

EID: 0032040180     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.274.4.c914     Document Type: Article
Times cited : (36)

References (34)
  • 1
    • 0020567249 scopus 로고
    • Heavy metals induce rapid calcium release from sarcoplasmic reticulum vesicles isolated from skeletal muscle
    • Abramson, J. J., J. L. Trimm, L. Weden, and G. Salama. Heavy metals induce rapid calcium release from sarcoplasmic reticulum vesicles isolated from skeletal muscle. Proc. Natl. Acad. Sci. USA, 80: 1526-1530, 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1526-1530
    • Abramson, J.J.1    Trimm, J.L.2    Weden, L.3    Salama, G.4
  • 3
    • 0002117417 scopus 로고
    • Antioxidant enzymes as mechanistic probes of oxygen-dependent toxicity
    • edited by A. E. Taylor, S. Matalon, and P. A. Ward. Bethesda, MD: Am. Physiol. Soc., (Clin. Physiol. Ser.)
    • Beckman, J. S., and B. A. Freeman. Antioxidant enzymes as mechanistic probes of oxygen-dependent toxicity. In: Physiology of Oxygen Radicals, edited by A. E. Taylor, S. Matalon, and P. A. Ward. Bethesda, MD: Am. Physiol. Soc., 1986, p. 39-53. (Clin. Physiol. Ser.)
    • (1986) Physiology of Oxygen Radicals , pp. 39-53
    • Beckman, J.S.1    Freeman, B.A.2
  • 4
    • 0027939709 scopus 로고
    • 2 and dithiothreitol
    • Heart Circ. Physiol. 36
    • 2 and dithiothreitol. Am. J. Physiol. 267 (Heart Circ. Physiol. 36): H1010-H1016, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Boraso, A.1    Williams, A.J.2
  • 5
    • 0027482905 scopus 로고
    • Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence
    • Bull, R., and J. J. Marengo. Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence. FEBS Lett. 331: 223-227, 1993.
    • (1993) FEBS Lett. , vol.331 , pp. 223-227
    • Bull, R.1    Marengo, J.J.2
  • 6
    • 0026579744 scopus 로고
    • Alterations in the sarcoplasmic reticulum: A possible link to exercise-induced muscle damage
    • Byrd, S. K. Alterations in the sarcoplasmic reticulum: a possible link to exercise-induced muscle damage. Med. Sci. Sports Exerc. 24: 531-536, 1992.
    • (1992) Med. Sci. Sports Exerc. , vol.24 , pp. 531-536
    • Byrd, S.K.1
  • 9
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solution containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A., and F. Fabiato. Calculator programs for computing the composition of the solution containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. Paris 74: 463-505, 1979.
    • (1979) J. Physiol. Paris , vol.74 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 10
    • 0028828942 scopus 로고
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 270: 25557-25563, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25557-25563
    • Favero, G.1    Zable, A.C.2    Abramson, J.J.3
  • 12
    • 0027276410 scopus 로고
    • Effects of repeated tetanic stimulation on excitation-contraction coupling in cut muscle fibres of the frog
    • Gyorke, S. Effects of repeated tetanic stimulation on excitation-contraction coupling in cut muscle fibres of the frog. J. Physiol. (Lond.) 464: 699-710, 1993.
    • (1993) J. Physiol. (Lond.) , vol.464 , pp. 699-710
    • Gyorke, S.1
  • 13
    • 0022409022 scopus 로고
    • Electron spin resonance studies of intact mammalian skeletal muscle
    • Jackson, M. J., R. H. T. Edwards, and M. C. R. Symons. Electron spin resonance studies of intact mammalian skeletal muscle. Biochim. Biophys. Acta 845: 185-190, 1985.
    • (1985) Biochim. Biophys. Acta , vol.845 , pp. 185-190
    • Jackson, M.J.1    Edwards, R.H.T.2    Symons, M.C.R.3
  • 14
    • 0023846309 scopus 로고
    • Free radical chemistry: Relationship to exercise
    • Jenkins, R. R. Free radical chemistry: relationship to exercise. Sports Med. 5: 156-170, 1988.
    • (1988) Sports Med. , vol.5 , pp. 156-170
    • Jenkins, R.R.1
  • 15
    • 0025766630 scopus 로고
    • Study of the mechanisms of hydrogen peroxide and hydroxyl free radical-induced cellular injury and calcium overload in cardiac myocytes
    • Josephson, R. A., H. S. Silverman, E. G. Lakatta, M. D. Stern, and J. L. Zweier. Study of the mechanisms of hydrogen peroxide and hydroxyl free radical-induced cellular injury and calcium overload in cardiac myocytes. J. Biol. Chem. 266: 2354-2361, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2354-2361
    • Josephson, R.A.1    Silverman, H.S.2    Lakatta, E.G.3    Stern, M.D.4    Zweier, J.L.5
  • 16
    • 0024434876 scopus 로고
    • Caffeine treatment inhibits drug-induced calcium release from sarcoplasmic reticulum and caffeine contracture but not tetanus in frog skeletal muscle
    • Koshita, M., and T. Oba. Caffeine treatment inhibits drug-induced calcium release from sarcoplasmic reticulum and caffeine contracture but not tetanus in frog skeletal muscle. Can. J. Physiol. Pharmacol. 67: 890-895, 1989.
    • (1989) Can. J. Physiol. Pharmacol. , vol.67 , pp. 890-895
    • Koshita, M.1    Oba, T.2
  • 17
    • 0026697875 scopus 로고
    • Amphibian ryanodine receptor isoforms are related to those of mammalian skeletal or cardiac muscle
    • Cell Physiol. 32
    • Lai, F. A., Q.-Y. Liu, L. Xu, A. El-Hashem, N. R. Kramarcy, R. Sealock, and G. Meissner. Amphibian ryanodine receptor isoforms are related to those of mammalian skeletal or cardiac muscle. Am. J. Physiol. 263 (Cell Physiol. 32): C365-C372, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Lai, F.A.1    Liu, Q.-Y.2    Xu, L.3    El-Hashem, A.4    Kramarcy, N.R.5    Sealock, R.6    Meissner, G.7
  • 18
    • 0028180422 scopus 로고
    • 2+ release channels and their regulation by endogenous effectors
    • 2+ release channels and their regulation by endogenous effectors. Annu. Rev. Physiol. 56: 485-508, 1994.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 485-508
    • Meissner, G.1
  • 19
    • 0029797315 scopus 로고    scopus 로고
    • 2+-release channel gating by anion channel blockers
    • Cell Physiol. 40
    • 2+-release channel gating by anion channel blockers. Am. J. Physiol. 271 (Cell Physiol. 40): C819-C824, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Oba, T.1    Koshita, M.2    Van Helden, D.F.3
  • 20
    • 0030239189 scopus 로고    scopus 로고
    • 2+-release channel in frog skeletal muscle
    • Cell Physiol. 40
    • 2+-release channel in frog skeletal muscle. Am. J. Physiol. 271 (Cell Physiol. 40): C810-C818, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Oba, T.1    Koshita, M.2    Yamaguchi, M.3
  • 23
    • 0028332825 scopus 로고
    • Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle
    • Oyamada, H., T. Murayama, T. Takagi, M. lino, N. Iwabe, T. Miyata, Y. Ogawa, and M. Endo. Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle. J. Biol. Chem. 269: 17206-17214, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17206-17214
    • Oyamada, H.1    Murayama, T.2    Takagi, T.3    Lino, M.4    Iwabe, N.5    Miyata, T.6    Ogawa, Y.7    Endo, M.8
  • 24
    • 0031048040 scopus 로고    scopus 로고
    • Methanethiosulfonate derivatives inhibit current through the ryanodine receptor/channel
    • Quinn, K. E., and B. E. Ehrlich. Methanethiosulfonate derivatives inhibit current through the ryanodine receptor/channel. J. Gen. Physiol. 109: 255-264, 1997.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 255-264
    • Quinn, K.E.1    Ehrlich, B.E.2
  • 25
    • 0027976272 scopus 로고
    • Exercise causes oxidative damage to rat skeletal muscle microsomes while increasing cellular sulfhydryls
    • Rajgura, S. U., G. S. Yeargans, and N. W. Seidler. Exercise causes oxidative damage to rat skeletal muscle microsomes while increasing cellular sulfhydryls. Life Sci. 54: 149-157, 1994.
    • (1994) Life Sci. , vol.54 , pp. 149-157
    • Rajgura, S.U.1    Yeargans, G.S.2    Seidler, N.W.3
  • 26
    • 0026438910 scopus 로고
    • Reactive oxygen in skeletal muscle. I. Intracellular oxidant kinetics and fatigue in vitro
    • Reid, M. B., K. E. Haack, K. M. Franchek, P. A. Valberg, L. Kobzik, and M. S. West. Reactive oxygen in skeletal muscle. I. Intracellular oxidant kinetics and fatigue in vitro. J. Appl. Physiol. 73: 1797-1804, 1992.
    • (1992) J. Appl. Physiol. , vol.73 , pp. 1797-1804
    • Reid, M.B.1    Haack, K.E.2    Franchek, K.M.3    Valberg, P.A.4    Kobzik, L.5    West, M.S.6
  • 27
    • 0027425836 scopus 로고
    • Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle
    • Reid, M. B., F. A. Khawli, and M. R. Moody. Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle. J. Appl. Physiol. 75: 1081-1087, 1993.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1081-1087
    • Reid, M.B.1    Khawli, F.A.2    Moody, M.R.3
  • 28
    • 0025809446 scopus 로고
    • Voltage sensor of excitation-contraction coupling in skeletal muscle
    • Rios, E., and G. Pizarro. Voltage sensor of excitation-contraction coupling in skeletal muscle. Physiol. Rev. 72: 849-908, 1991.
    • (1991) Physiol. Rev. , vol.72 , pp. 849-908
    • Rios, E.1    Pizarro, G.2
  • 29
    • 0021689677 scopus 로고
    • 2+ release by acting at the apparent physiological release site in sarcoplasmic reticulum
    • 2+ release by acting at the apparent physiological release site in sarcoplasmic reticulum. J. Biol. Chem. 259: 13363-13369, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13363-13369
    • Salama, G.1    Abramson, J.2
  • 30
    • 0026785006 scopus 로고
    • 2+ release from the sarcoplasmic reticulum of skinned rabbit psoas fibres
    • 2+ release from the sarcoplasmic reticulum of skinned rabbit psoas fibres. J. Physiol. (Lond.) 454: 389-420, 1992.
    • (1992) J. Physiol. (Lond.) , vol.454 , pp. 389-420
    • Salama, G.1    Abramson, J.J.2    Pike, G.K.3
  • 31
    • 0025023848 scopus 로고
    • Biochemical mechanisms for oxygen free radical formation during exercise
    • Sjodin, B., Y. H. Westing, and F. S. Apple. Biochemical mechanisms for oxygen free radical formation during exercise. Sports Med. 10: 236-254, 1990.
    • (1990) Sports Med. , vol.10 , pp. 236-254
    • Sjodin, B.1    Westing, Y.H.2    Apple, F.S.3
  • 32
    • 0026748872 scopus 로고
    • The temporal relationship between endothelial cell dysfunction and skeletal muscle damage after ischemia and reperfusion
    • Sternbergh, W. C., III, and B. Adelman. The temporal relationship between endothelial cell dysfunction and skeletal muscle damage after ischemia and reperfusion. J. Vasc. Surg. 16: 30-39, 1992.
    • (1992) J. Vasc. Surg. , vol.16 , pp. 30-39
    • Sternbergh III, W.C.1    Adelman, B.2
  • 34
    • 0022972116 scopus 로고
    • Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum vesicles
    • Trimm, J. L., G. Salama, and J. J. Abramson. Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum vesicles. J. Biol. Chem. 261: 16092-16098, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16092-16098
    • Trimm, J.L.1    Salama, G.2    Abramson, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.