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Volumn 1768, Issue 6, 2007, Pages 1498-1505

Thermogenic activity of Ca2+-ATPase from skeletal muscle heavy sarcoplasmic reticulum: The role of ryanodine Ca2+ channel

Author keywords

ATP hydrolysis; Ca2+ ATPase; Heat production; Heavy sarcoplasmic reticulum; Ryanodine Ca2+ channel

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM CHANNEL; MAGNESIUM; RUTHENIUM RED; RYANODINE RECEPTOR; CALCIUM; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 34249001978     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.03.016     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 0034611678 scopus 로고    scopus 로고
    • Towards a molecular understanding of adaptative thermogenesis
    • Lowell B.B., and Spiegelman B.M. Towards a molecular understanding of adaptative thermogenesis. Nature 404 (2000) 652-660
    • (2000) Nature , vol.404 , pp. 652-660
    • Lowell, B.B.1    Spiegelman, B.M.2
  • 2
    • 0033534524 scopus 로고    scopus 로고
    • Role of nonexercise activity thermogenesis in resistance to fat gain in humans
    • Levine J.A., Eberhardt N.L., and Jensen M.D. Role of nonexercise activity thermogenesis in resistance to fat gain in humans. Science 283 (1999) 212-214
    • (1999) Science , vol.283 , pp. 212-214
    • Levine, J.A.1    Eberhardt, N.L.2    Jensen, M.D.3
  • 4
    • 33645873573 scopus 로고    scopus 로고
    • Thermogenic mechanisms and their hormonal regulation
    • Silva J.E. Thermogenic mechanisms and their hormonal regulation. Physiol. Rev. 86 (2006) 435-464
    • (2006) Physiol. Rev. , vol.86 , pp. 435-464
    • Silva, J.E.1
  • 6
    • 0347989317 scopus 로고    scopus 로고
    • Brown adipose tissue: function and physiological significance
    • Cannon B., and Nedergaard J. Brown adipose tissue: function and physiological significance. Physiol. Rev. 84 (2004) 277-359
    • (2004) Physiol. Rev. , vol.84 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 7
    • 0025856240 scopus 로고
    • Significance of cation transport in control of energy metabolism and thermogenesis
    • Clausen T., Van Hardeveld C., and Everts M.E. Significance of cation transport in control of energy metabolism and thermogenesis. Physiol. Rev. 71 (1991) 733-774
    • (1991) Physiol. Rev. , vol.71 , pp. 733-774
    • Clausen, T.1    Van Hardeveld, C.2    Everts, M.E.3
  • 8
    • 0028941667 scopus 로고
    • Humoral thermogenesis and its role in maintaining energy balance
    • Jansk'y L. Humoral thermogenesis and its role in maintaining energy balance. Physiol. Rev. 75 (1995) 237-259
    • (1995) Physiol. Rev. , vol.75 , pp. 237-259
    • Jansk'y, L.1
  • 9
    • 0016733940 scopus 로고
    • Isolation and characterization of two types of sarcoplasmic reticulum vesicles
    • Meissner G. Isolation and characterization of two types of sarcoplasmic reticulum vesicles. Biochim. Biophys. Acta 389 (1975) 51-68
    • (1975) Biochim. Biophys. Acta , vol.389 , pp. 51-68
    • Meissner, G.1
  • 10
    • 0033405549 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum and the control of muscle contraction
    • Franzini-Armstrong C. The sarcoplasmic reticulum and the control of muscle contraction. FASEB J. 13 (1999) S266-S270
    • (1999) FASEB J. , vol.13
    • Franzini-Armstrong, C.1
  • 12
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito A., Seiler S.D., Chu A., and Fleischer S. Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J. Cell Biol. 99 (1984) 875-885
    • (1984) J. Cell Biol. , vol.99 , pp. 875-885
    • Saito, A.1    Seiler, S.D.2    Chu, A.3    Fleischer, S.4
  • 13
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. J. Biol. Chem. 261 (1986) 6300-6306
    • (1986) J. Biol. Chem. , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 14
    • 0022860249 scopus 로고
    • Functional characterization of junctional terminal cisternae from mammalian fast skeletal muscle sarcoplasmic reticulum
    • Chu A., Volpe P., Costello B., and Fleischer S. Functional characterization of junctional terminal cisternae from mammalian fast skeletal muscle sarcoplasmic reticulum. Biochemistry 25 (1986) 8315-8324
    • (1986) Biochemistry , vol.25 , pp. 8315-8324
    • Chu, A.1    Volpe, P.2    Costello, B.3    Fleischer, S.4
  • 16
    • 0031980883 scopus 로고    scopus 로고
    • Calcium pool size modulates the sensitivity of the ryanodine receptor channel and calcium-dependent ATPase of heavy sarcoplasmic reticulum to extravesicular free calcium concentration
    • Marie V., and Silva J.E. Calcium pool size modulates the sensitivity of the ryanodine receptor channel and calcium-dependent ATPase of heavy sarcoplasmic reticulum to extravesicular free calcium concentration. J. Cell. Physiol. 175 (1998) 283-294
    • (1998) J. Cell. Physiol. , vol.175 , pp. 283-294
    • Marie, V.1    Silva, J.E.2
  • 17
    • 0037338934 scopus 로고    scopus 로고
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans)
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans). J. Exp. Biol. 206 (2003) 805-812
    • (2003) J. Exp. Biol. , vol.206 , pp. 805-812
    • Morrissette, J.M.1    Franck, J.P.2    Block, B.A.3
  • 18
    • 0027296683 scopus 로고
    • 2+-ATPase and ryanodine receptor in cold-acclimated ducklings and thermogenesis
    • 2+-ATPase and ryanodine receptor in cold-acclimated ducklings and thermogenesis. Am. J. Physiol. 265 (1993) C507-C513
    • (1993) Am. J. Physiol. , vol.265
    • Dumonteil, E.1    Barre, H.2    Meissner, G.3
  • 19
    • 0035816710 scopus 로고    scopus 로고
    • 2+-ATPase
    • 2+-ATPase. J. Biol. Chem. 276 (2001) 25078-25087
    • (2001) J. Biol. Chem. , vol.276 , pp. 25078-25087
    • de Meis, L.1
  • 21
    • 0036628770 scopus 로고    scopus 로고
    • 2+-ATPases (SERCA): energy transduction and heat production in transport ATPases
    • 2+-ATPases (SERCA): energy transduction and heat production in transport ATPases. J. Membr. Biol. 188 (2002) 1-9
    • (2002) J. Membr. Biol. , vol.188 , pp. 1-9
    • de Meis, L.1
  • 22
    • 8544251330 scopus 로고    scopus 로고
    • Heat of PPi hydrolysis varies depending on the enzyme used. Yeast and corn vacuolar pyrophosphatase
    • da-Silva W.S., Bomfim F.M., Galina A., and De Meis L. Heat of PPi hydrolysis varies depending on the enzyme used. Yeast and corn vacuolar pyrophosphatase. J. Biol. Chem. 279 (2004) 45613-45617
    • (2004) J. Biol. Chem. , vol.279 , pp. 45613-45617
    • da-Silva, W.S.1    Bomfim, F.M.2    Galina, A.3    De Meis, L.4
  • 23
    • 7444269437 scopus 로고    scopus 로고
    • Catalysis, evolution and life
    • Szoke A., Scott W.G., and Hajdu J. Catalysis, evolution and life. FEBS Lett. 553 (2003) 18-20
    • (2003) FEBS Lett. , vol.553 , pp. 18-20
    • Szoke, A.1    Scott, W.G.2    Hajdu, J.3
  • 24
    • 0024979877 scopus 로고
    • Role of water in the energy of hydrolysis of phosphate compounds-energy transduction in biological membranes
    • de Meis L. Role of water in the energy of hydrolysis of phosphate compounds-energy transduction in biological membranes. Biochim. Biophys. Acta 973 (1989) 333-349
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 333-349
    • de Meis, L.1
  • 25
    • 0028905942 scopus 로고
    • 2+ and Sr2+ transport by the sarcoplasmic reticulum ATPase
    • 2+ and Sr2+ transport by the sarcoplasmic reticulum ATPase. J. Biol. Chem. 270 (1995) 4361-4367
    • (1995) J. Biol. Chem. , vol.270 , pp. 4361-4367
    • Yu, X.1    Inesi, G.2
  • 26
    • 0035817358 scopus 로고    scopus 로고
    • Slippage and uncoupling in P-type cation pumps: implications for energy transduction mechanisms and regulation of metabolism
    • Berman M.C. Slippage and uncoupling in P-type cation pumps: implications for energy transduction mechanisms and regulation of metabolism. Biochim. Biophys. Acta 1513 (2001) 95-121
    • (2001) Biochim. Biophys. Acta , vol.1513 , pp. 95-121
    • Berman, M.C.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0018801492 scopus 로고
    • The use of quench reagents for resolution of single transport cycles in sarcoplasmic reticulum
    • Chiesi M., and Inesi G. The use of quench reagents for resolution of single transport cycles in sarcoplasmic reticulum. J. Biol. Chem. 254 (1979) 10370-10377
    • (1979) J. Biol. Chem. , vol.254 , pp. 10370-10377
    • Chiesi, M.1    Inesi, G.2
  • 33
    • 0019887966 scopus 로고
    • The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase
    • Grubmeyer C., and Penefsky H.S. The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 256 (1981) 3718-3727
    • (1981) J. Biol. Chem. , vol.256 , pp. 3718-3727
    • Grubmeyer, C.1    Penefsky, H.S.2
  • 35
    • 84981840086 scopus 로고
    • Komplexone XXIX. Ein grosser chelateffekt besonderer
    • Schwartzenbach G., Senn H., and Anderegg G. Komplexone XXIX. Ein grosser chelateffekt besonderer. Helv. Chim. Acta 40 (1957) 1886-1900
    • (1957) Helv. Chim. Acta , vol.40 , pp. 1886-1900
    • Schwartzenbach, G.1    Senn, H.2    Anderegg, G.3
  • 36
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., and Fabiato F. Calculator programs for computing the composition of solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. 75 (1979) 463-505
    • (1979) J. Physiol. , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 37
    • 0022517661 scopus 로고
    • Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers
    • Sorenson M.M., Coelho H.S., and Reuben J.P. Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers. J. Membr. Biol. 90 (1986) 219-230
    • (1986) J. Membr. Biol. , vol.90 , pp. 219-230
    • Sorenson, M.M.1    Coelho, H.S.2    Reuben, J.P.3
  • 38
    • 4944256105 scopus 로고    scopus 로고
    • Ryanodine receptors are expressed and functionally active in mouse spermatogenic cells and their inhibition interferes with spermatogonial differentiation
    • Chiarella P., Puglisi R., Sorrentino V., Boitani C., and Stefanini M. Ryanodine receptors are expressed and functionally active in mouse spermatogenic cells and their inhibition interferes with spermatogonial differentiation. J. Cell. Sci. 117 (2004) 4127-4134
    • (2004) J. Cell. Sci. , vol.117 , pp. 4127-4134
    • Chiarella, P.1    Puglisi, R.2    Sorrentino, V.3    Boitani, C.4    Stefanini, M.5
  • 39
    • 0032537498 scopus 로고    scopus 로고
    • Complex formation between calsequestrin and the ryanodine receptor in fast- and slow-twitch rabbit skeletal muscle
    • Murray B.E., and Ohlendieck K. Complex formation between calsequestrin and the ryanodine receptor in fast- and slow-twitch rabbit skeletal muscle. FEBS Lett. 429 (1998) 317-322
    • (1998) FEBS Lett. , vol.429 , pp. 317-322
    • Murray, B.E.1    Ohlendieck, K.2
  • 40
    • 0019071217 scopus 로고
    • A comparison of vesicles derived from terminal cisternae and longitudinal tubules of sarcoplasmic reticulum isolated from rabbit skeletal muscle
    • Louis C.F., Nash-Adler P.A., Fudyma G., Shigekawa M., Akowitz A., and Katz A.M. A comparison of vesicles derived from terminal cisternae and longitudinal tubules of sarcoplasmic reticulum isolated from rabbit skeletal muscle. Eur. J. Biochem. 111 (1980) 1-9
    • (1980) Eur. J. Biochem. , vol.111 , pp. 1-9
    • Louis, C.F.1    Nash-Adler, P.A.2    Fudyma, G.3    Shigekawa, M.4    Akowitz, A.5    Katz, A.M.6
  • 41
    • 0024816693 scopus 로고
    • 2+-ATPase in the terminal cisternae and the longitudinal tubules fractions of sarcoplasmic reticulum
    • 2+-ATPase in the terminal cisternae and the longitudinal tubules fractions of sarcoplasmic reticulum. Eur. J. Biochem. 186 (1989) 677-681
    • (1989) Eur. J. Biochem. , vol.186 , pp. 677-681
    • Mészáros, L.G.1    Ikemoto, N.2
  • 42
    • 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 (1997) 1-50
    • (1997) Pharmacol. Rev. , vol.49 , pp. 1-50
    • Zucchi, R.1    Testoni-Ronca, S.2
  • 44
    • 0021986579 scopus 로고
    • 2+ on calcium accumulation by two fractions of sarcoplasmic reticulum from rabbit skeletal muscle
    • 2+ on calcium accumulation by two fractions of sarcoplasmic reticulum from rabbit skeletal muscle. Biochim. Biophys. Acta 812 (1985) 333-344
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 333-344
    • Watras, J.1
  • 45
    • 0020195852 scopus 로고
    • 2+ release from fragmented sarcoplasmic reticulum: a comparison with skinned muscle fiber studies
    • 2+ release from fragmented sarcoplasmic reticulum: a comparison with skinned muscle fiber studies. Biochem. J. 92 (1982) 1287-1296
    • (1982) Biochem. J. , vol.92 , pp. 1287-1296
    • Kirino, Y.1    Shimizu, H.2
  • 46
    • 0026868856 scopus 로고
    • Modulation by ryanodine of active calcium loading and caffeine-induced calcium release of heavy sarcoplasmic reticulum vesicles
    • Hasselbach W., and Migala A. Modulation by ryanodine of active calcium loading and caffeine-induced calcium release of heavy sarcoplasmic reticulum vesicles. Z. Naturforsch. 47 (1992) 429-439
    • (1992) Z. Naturforsch. , vol.47 , pp. 429-439
    • Hasselbach, W.1    Migala, A.2
  • 47
    • 0013857284 scopus 로고
    • The influence of oxalate on calcium transport of isolated sarcoplasmic reticular vesicles
    • Makinose M., and Hasselbach W. The influence of oxalate on calcium transport of isolated sarcoplasmic reticular vesicles. Biochem. Z. 1343 (1965) 360-382
    • (1965) Biochem. Z. , vol.1343 , pp. 360-382
    • Makinose, M.1    Hasselbach, W.2
  • 48
    • 0024517957 scopus 로고
    • Regulation of steady state filling in sarcoplasmic reticulum. Roles of back-inhibition, leakage, and slippage of the calcium pump
    • Inesi G., and de Meis L. Regulation of steady state filling in sarcoplasmic reticulum. Roles of back-inhibition, leakage, and slippage of the calcium pump. J. Biol. Chem. 264 (1989) 5929-5936
    • (1989) J. Biol. Chem. , vol.264 , pp. 5929-5936
    • Inesi, G.1    de Meis, L.2
  • 49
    • 0023069451 scopus 로고
    • Intracellular Calcium Homeostasis
    • Carafoli E. Intracellular Calcium Homeostasis. Annu. Rev. Biochem. 56 (1987) 395-433
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 50
    • 0032531818 scopus 로고    scopus 로고
    • Calcium: a life and death signal
    • Berridge M.I., Bootman M.D., and Lipp P. Calcium: a life and death signal. Nature 395 (1998) 645-648
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.I.1    Bootman, M.D.2    Lipp, P.3
  • 51
    • 0033624484 scopus 로고    scopus 로고
    • 2+ signalling and muscle disease
    • 2+ signalling and muscle disease. Eur. J. Biochem. 267 (2000) 5291-5297
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5291-5297
    • MacLennan, D.H.1
  • 52
    • 0035161109 scopus 로고    scopus 로고
    • Heat production during anesthetic-induced malignant hyperthermia
    • Nelson T.E. Heat production during anesthetic-induced malignant hyperthermia. Biosci. Rep. (2001) 169-179
    • (2001) Biosci. Rep. , pp. 169-179
    • Nelson, T.E.1
  • 53
    • 17644363740 scopus 로고    scopus 로고
    • 2+ signaling in HEK-293 and skeletal muscle cells expressing recombinant ryanodine receptors harboring malignant hyperthermia and central core disease mutations
    • 2+ signaling in HEK-293 and skeletal muscle cells expressing recombinant ryanodine receptors harboring malignant hyperthermia and central core disease mutations. J. Biol. Chem. 280 (2005) 15380-15389
    • (2005) J. Biol. Chem. , vol.280 , pp. 15380-15389
    • Brini, M.1    Manni, S.2    Pierobon, N.3    Du, G.G.4    Sharma, P.5    MacLennan, D.H.6    Carafoli, E.7
  • 56
    • 0019315398 scopus 로고
    • Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient
    • de Meis L., Martins O.B., and Alves E.W. Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient. Biochemistry 19 (1980) 4252-4261
    • (1980) Biochemistry , vol.19 , pp. 4252-4261
    • de Meis, L.1    Martins, O.B.2    Alves, E.W.3
  • 57
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C., Nomura H., and Tsuda T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 18 (2004) 361-368
    • (2004) Nature , vol.18 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 58
    • 0031789887 scopus 로고    scopus 로고
    • Energy, life, and ATP
    • Boyer P.D. Energy, life, and ATP. Biosci. Rep. 18 (1998) 97-117
    • (1998) Biosci. Rep. , vol.18 , pp. 97-117
    • Boyer, P.D.1


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