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Volumn 74, Issue 3, 1998, Pages 1263-1277

Sulfhydryl oxidation modifies the calcium dependence of ryanodine- sensitive calcium channels of excitable cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; RYANODINE; THIOL DERIVATIVE;

EID: 0031951413     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77840-3     Document Type: Article
Times cited : (184)

References (53)
  • 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. 1983. Heavy metals induce rapid calcium release from sarcoplasmic reticulum vesicles isolated from skeletal muscle. Proc. Natl. Acad. Sci. USA. 80: 1526-1530.
    • (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
  • 2
    • 0029417220 scopus 로고
    • 2+ release channel ryanodine receptor from skeletal muscle sarcoplasmic reticulum
    • 2+ release channel ryanodine receptor from skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 270: 29644-29647.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29644-29647
    • Abramson, J.J.1    Zable, A.C.2    Favero, T.G.3    Salama, G.4
  • 4
    • 0020646352 scopus 로고
    • 2+ release in skeletal muscle sarcoplasmic reticulum by sulfhydryl reagents and chlorpromazine
    • 2+ release in skeletal muscle sarcoplasmic reticulum by sulfhydryl reagents and chlorpromazine. Arch. Biochem. Biophys. 221:458-466.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 458-466
    • Bindoli, A.1    Fleischer, S.2
  • 5
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • Bonfoco, E., D. Krainc, M. Ankarcrona, P. Nicotera, and S. A. Lipton. 1995. Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc. Natl. Acad. Sci. USA. 92: 7162-7166.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankarcrona, M.3    Nicotera, P.4    Lipton, S.A.5
  • 6
    • 0018370639 scopus 로고
    • Specific covalent modification of thiols: Applications in the study of enzymes and other biomolecules
    • Brocklehurst, K. 1979. Specific covalent modification of thiols: applications in the study of enzymes and other biomolecules. Int. J. Biochem. 10:259-274.
    • (1979) Int. J. Biochem. , vol.10 , pp. 259-274
    • Brocklehurst, K.1
  • 7
    • 0027482905 scopus 로고
    • Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence
    • Bull, R., and J. J. Marengo. 1993. Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence. FEBS Lett. 331:223-227.
    • (1993) FEBS Lett. , vol.331 , pp. 223-227
    • Bull, R.1    Marengo, J.J.2
  • 8
    • 0028230675 scopus 로고
    • Calcium-dependent halothane activation of sarcoplasmic reticulum calcium channels from frog skeletal muscle
    • Cell Physiol. 35
    • Bull, R., and J. J. Marengo. 1994. Calcium-dependent halothane activation of sarcoplasmic reticulum calcium channels from frog skeletal muscle. Am. J. Physiol. 266 (Cell Physiol. 35):C391-C396.
    • (1994) Am. J. Physiol. , vol.266
    • Bull, R.1    Marengo, J.J.2
  • 9
    • 85030307677 scopus 로고    scopus 로고
    • Functional expression of cDNA encoding the type 3 ryanodine receptor of rabbit uterus in HEK293 cells
    • Chen, S. R. W., X. Lai, and L. Zhang. 1997. Functional expression of cDNA encoding the type 3 ryanodine receptor of rabbit uterus in HEK293 cells. Biophys. J. 72:A13.
    • (1997) Biophys. J. , vol.72
    • Chen, S.R.W.1    Lai, X.2    Zhang, L.3
  • 13
    • 0031570282 scopus 로고    scopus 로고
    • Rapid kinetic studies of SH-oxidation induced calcium release from sarcoplasmic reticulum vesicles
    • Donoso, P., P. Rodríguez, and P. Marambio. 1997. Rapid kinetic studies of SH-oxidation induced calcium release from sarcoplasmic reticulum vesicles. Arch. Biochem. Biophys. 341:295-299.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 295-299
    • Donoso, P.1    Rodríguez, P.2    Marambio, P.3
  • 14
    • 0027479430 scopus 로고
    • Free radicals and calcium homeostasis: Relevance to malignant hyperthermia?
    • Duthie, G. G., and J. R. Arthur. 1993. Free radicals and calcium homeostasis: relevance to malignant hyperthermia? Free Radic. Biol. Med. 14:435-442.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 435-442
    • Duthie, G.G.1    Arthur, J.R.2
  • 18
    • 0029018175 scopus 로고
    • Molecular structure and tissue distribution of ryanodine receptor calcium channels
    • Giannini, G., and V. Sorrentino. 1995. Molecular structure and tissue distribution of ryanodine receptor calcium channels. Med. Res. Rev. 15:313-323.
    • (1995) Med. Res. Rev. , vol.15 , pp. 313-323
    • Giannini, G.1    Sorrentino, V.2
  • 19
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • Gosh, A., and M. E. Greenberg. 1995. Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science. 268: 239-247.
    • (1995) Science , vol.268 , pp. 239-247
    • Gosh, A.1    Greenberg, M.E.2
  • 20
    • 0026471048 scopus 로고
    • Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain
    • Hakamata, Y., J. Nakai, H. Takeshima, and K. Imoto. 1992. Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain. FEBS Lett. 312:229-235.
    • (1992) FEBS Lett. , vol.312 , pp. 229-235
    • Hakamata, Y.1    Nakai, J.2    Takeshima, H.3    Imoto, K.4
  • 21
    • 0027209844 scopus 로고
    • Triads and transverse tubules isolated from frog skeletal muscle contain high levels of inositol 1,4,5-trisphosphate
    • Hidalgo, C., J. Jorquera, V. Tapia, and P. Donoso. 1993. Triads and transverse tubules isolated from frog skeletal muscle contain high levels of inositol 1,4,5-trisphosphate. J. Biol. Chem. 268:15111-15117.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15111-15117
    • Hidalgo, C.1    Jorquera, J.2    Tapia, V.3    Donoso, P.4
  • 22
    • 0025238667 scopus 로고
    • The cardiac sarcoplasmic reticulum calcium-release channel: Modulation of ryanodine binding and single-channel activity
    • Holmberg, S. R. M., and A. J. Williams. 1990. The cardiac sarcoplasmic reticulum calcium-release channel: modulation of ryanodine binding and single-channel activity. Biochim. Biophys. Acta. 1022:187-193.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 187-193
    • Holmberg, S.R.M.1    Williams, A.J.2
  • 25
    • 0028031728 scopus 로고
    • Direct evidence for the existence and functional role of hyperactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin
    • Liu, G., J. J. Abramson, A. C. Zable, and I. N. Pessah. 1994. Direct evidence for the existence and functional role of hyperactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin. Mol. Pharmacol. 45:189-200.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 189-200
    • Liu, G.1    Abramson, J.J.2    Zable, A.C.3    Pessah, I.N.4
  • 26
    • 0029999080 scopus 로고    scopus 로고
    • Calcium dependence of ryanodine-sensitive calcium channels from brain cortex endoplasmic reticulum
    • Marengo, J. J., R. Bull, and C. Hidalgo. 1996. Calcium dependence of ryanodine-sensitive calcium channels from brain cortex endoplasmic reticulum. FEBS Lett. 383:59-62.
    • (1996) FEBS Lett. , vol.383 , pp. 59-62
    • Marengo, J.J.1    Bull, R.2    Hidalgo, C.3
  • 27
    • 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) Annu. Rev. Physiol. , vol.56 , pp. 485-508
    • Meissner, G.1
  • 29
    • 0029928519 scopus 로고    scopus 로고
    • Properties of RyR3 ryanodine receptor isoform in mammalian brain
    • Murayama, T., and Y. Ogawa. 1996. Properties of RyR3 ryanodine receptor isoform in mammalian brain. J. Biol. Chem. 271:5079-5084.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5079-5084
    • Murayama, T.1    Ogawa, Y.2
  • 30
    • 0344881370 scopus 로고    scopus 로고
    • Properties of homotetrameric RyR3 ryanodine receptor in mammalian diaphragm muscle
    • Murayama, T., and Y. Ogawa. 1997. Properties of homotetrameric RyR3 ryanodine receptor in mammalian diaphragm muscle. Biophys. J. 72: A168.
    • (1997) Biophys. J. , vol.72
    • Murayama, T.1    Ogawa, Y.2
  • 31
    • 0023727041 scopus 로고
    • Calcium release from isolated sarcoplasmic reticulum due to 4,4′-dithiodipyndine
    • Nagura, S., T. Kawasaki, T. Taguchi, and M. Kasai. 1988. Calcium release from isolated sarcoplasmic reticulum due to 4,4′-dithiodipyndine. J. Biochem. 104:461-465.
    • (1988) J. Biochem. , vol.104 , pp. 461-465
    • Nagura, S.1    Kawasaki, T.2    Taguchi, T.3    Kasai, M.4
  • 32
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • Nakai, J., T. Imagawa, Y. Hakamata, M. Shigekawa, H. Takeshima, and S. Numa. 1990. Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett. 271:168-177.
    • (1990) FEBS Lett. , vol.271 , pp. 168-177
    • Nakai, J.1    Imagawa, T.2    Hakamata, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 33
    • 0028814907 scopus 로고
    • Physiological differences between the α and β ryanodine receptors of fish skeletal muscle
    • O'Brien, J., H. H. Valdivia, and B. A. Block. 1995. Physiological differences between the α and β ryanodine receptors of fish skeletal muscle. Biophys. J. 68:471-482.
    • (1995) Biophys. J. , vol.68 , pp. 471-482
    • O'Brien, J.1    Valdivia, H.H.2    Block, B.A.3
  • 34
    • 0028041274 scopus 로고
    • Role of ryanodine receptors
    • Ogawa, Y. 1994. Role of ryanodine receptors. Crit. Rev. Biochem. Mol. 29:229-274.
    • (1994) Crit. Rev. Biochem. Mol. , vol.29 , pp. 229-274
    • Ogawa, Y.1
  • 36
    • 0029923335 scopus 로고    scopus 로고
    • α and β isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3
    • Ottini, L., G. Marziali, A. Conti, A. Chalesworth, and V. Sorrentino. 1996. α and β isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3. Biochem. J. 315: 207-216.
    • (1996) Biochem. J. , vol.315 , pp. 207-216
    • Ottini, L.1    Marziali, G.2    Conti, A.3    Chalesworth, A.4    Sorrentino, V.5
  • 37
    • 0028332825 scopus 로고
    • Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle
    • Oyamada, H., T. Murayama, T. Takagi, M. Iino, N. Iwabe, T. Miyata, Y. Ogawa, and M. Endo. 1994. Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle. J. Biol. Chem. 269:17206-17214.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17206-17214
    • Oyamada, H.1    Murayama, T.2    Takagi, T.3    Iino, M.4    Iwabe, N.5    Miyata, T.6    Ogawa, Y.7    Endo, M.8
  • 42
    • 0026785006 scopus 로고
    • 2+ release from sarcoplasmic reticulum of skinned rabbit psoas fibers
    • 2+ release from sarcoplasmic reticulum of skinned rabbit psoas fibers. J. Physiol. (Lond.). 454:389-420.
    • (1992) J. Physiol. (Lond.) , vol.454 , pp. 389-420
    • Salama, G.1    Abramson, J.J.2    Pike, G.K.3
  • 44
    • 0023029513 scopus 로고
    • Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum
    • Smith, J. S., R. Coronado, and G. Meissner. 1986. Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum. J. Gen. Physiol. 88:573-588.
    • (1986) J. Gen. Physiol. , vol.88 , pp. 573-588
    • Smith, J.S.1    Coronado, R.2    Meissner, G.3
  • 46
    • 0028227553 scopus 로고
    • 2+-release channels of skeletal sarcoplasmic reticulum vesicles reconstituted in lipid bilayers
    • 2+-release channels of skeletal sarcoplasmic reticulum vesicles reconstituted in lipid bilayers. Arch. Biochem. Biophys. 308:214-221.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 214-221
    • Stoyanovsky, D.A.1    Salama, G.2    Kegan, V.E.3
  • 47
    • 0026569861 scopus 로고
    • Photooxidation of skeletal muscle sarcoplasmic reticulum induces rapid calcium release
    • Stuart, J., I. N. Pessah, T. G. Favero, and J. J. Abramson. 1992. Photooxidation of skeletal muscle sarcoplasmic reticulum induces rapid calcium release. Arch. Biochem. Biophys. 292:512-521.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 512-521
    • Stuart, J.1    Pessah, I.N.2    Favero, T.G.3    Abramson, J.J.4
  • 48
    • 0029662341 scopus 로고    scopus 로고
    • 2+ release channels: Does diversity in form equal diversity in function?
    • 2+ release channels: does diversity in form equal diversity in function? Physiol. Rev. 76:1027-1071.
    • (1996) Physiol. Rev. , vol.76 , pp. 1027-1071
    • Sutko, J.L.1    Airey, J.A.2
  • 50
    • 0022972116 scopus 로고
    • Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum vesicles
    • Trimm, J. L., G. Salama, and J. J. Abramson. 1986. Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum vesicles. J. Biol. Chem. 261:16092-16098.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16092-16098
    • Trimm, J.L.1    Salama, G.2    Abramson, J.J.3
  • 51
    • 0028641248 scopus 로고
    • Apoptosis and free radicals
    • Wood, K. A., and R. J. Youle. 1994. Apoptosis and free radicals. Ann. N.Y. Acad. Sci. 738:400-407.
    • (1994) Ann. N.Y. Acad. Sci. , vol.738 , pp. 400-407
    • Wood, K.A.1    Youle, R.J.2
  • 53
    • 0030610319 scopus 로고    scopus 로고
    • 2+ channel/ryanodine receptor: Modulation by endogenous effectors, drugs and disease states
    • 2+ channel/ryanodine receptor: modulation by endogenous effectors, drugs and disease states. Pharmacol. Rev. 49:1-51.
    • (1997) Pharmacol. Rev. , vol.49 , pp. 1-51
    • Zucchi, R.1    Ronca-Testoni, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.