메뉴 건너뛰기




Volumn 551, Issue 1, 2003, Pages 5-12

Calmodulin kinase modulates Ca2+ release in mouse skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; INHIBITOR PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; PEPTIDE;

EID: 0041353464     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2003.042002     Document Type: Review
Times cited : (32)

References (43)
  • 1
    • 0005458810 scopus 로고
    • Metabolic changes in muscle during exercise; their effect on muscle function
    • Allen DG, Duty S & Westerblad H (1993). Metabolic changes in muscle during exercise; their effect on muscle function. Proc Aust Physiol Soc 24, 65-75.
    • (1993) Proc. Aust. Physiol. Soc. , vol.24 , pp. 65-75
    • Allen, D.G.1    Duty, S.2    Westerblad, H.3
  • 2
    • 0035498508 scopus 로고    scopus 로고
    • Role of phosphate and calcium stores in muscle fatigue
    • Allen DG & Westerblad H (2001). Role of phosphate and calcium stores in muscle fatigue. J Physiol 536, 657-665.
    • (2001) J. Physiol. , vol.536 , pp. 657-665
    • Allen, D.G.1    Westerblad, H.2
  • 3
    • 0034743560 scopus 로고    scopus 로고
    • 2+ channels: Is a unifying mechanism at hand?
    • 2+ channels: is a unifying mechanism at hand? J Mol Cell Cardiol 33, 639-650.
    • (2001) J. Mol. Cell Cardiol. , vol.33 , pp. 639-650
    • Anderson, M.E.1
  • 4
    • 0032103008 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse
    • Andrade FH, Reid MB, Allen DG & Westerblad H (1998). Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse. J Physiol 509, 565-575.
    • (1998) J. Physiol. , vol.509 , pp. 565-575
    • Andrade, F.H.1    Reid, M.B.2    Allen, D.G.3    Westerblad, H.4
  • 6
    • 0032185669 scopus 로고    scopus 로고
    • α KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle
    • Bayer KU, Harbers K & Schulman H (1998). α KAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle. EMBO J 17, 5598-5605.
    • (1998) EMBO J. , vol.17 , pp. 5598-5605
    • Bayer, K.U.1    Harbers, K.2    Schulman, H.3
  • 7
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla US & Iyengar R (1999). Emergent properties of networks of biological signaling pathways. Science 283, 381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 8
    • 0020478639 scopus 로고
    • A calmodulin-dependent protein kinase system from skeletal muscle sarcoplasmic reticulum. Phosphorylation of a 60,000-dalton protein
    • Campbell KP & MacLennan DH (1982). A calmodulin-dependent protein kinase system from skeletal muscle sarcoplasmic reticulum. Phosphorylation of a 60,000-dalton protein. J Biol Chem 257, 1238-1246.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1238-1246
    • Campbell, K.P.1    MacLennan, D.H.2
  • 10
    • 0025295430 scopus 로고
    • Specific association of calmodulin-dependent protein kinase and related substrates with the junctional sarcoplasmic reticulum of skeletal muscle
    • Chu A, Sumbilla C, Inesi G, Jay SD & Campbell KP (1990). Specific association of calmodulin-dependent protein kinase and related substrates with the junctional sarcoplasmic reticulum of skeletal muscle. Biochemistry 29, 5899-5905.
    • (1990) Biochemistry , vol.29 , pp. 5899-5905
    • Chu, A.1    Sumbilla, C.2    Inesi, G.3    Jay, S.D.4    Campbell, K.P.5
  • 11
    • 0034790043 scopus 로고    scopus 로고
    • Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in rabbit fast-twitch muscle sarcoplasmic reticulum
    • Colpo P, Nori A, Sacchetto R, Damiani E & Margreth A (2001). Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in rabbit fast-twitch muscle sarcoplasmic reticulum. Mol Cell Biochem 223, 139-145.
    • (2001) Mol. Cell Biochem. , vol.223 , pp. 139-145
    • Colpo, P.1    Nori, A.2    Sacchetto, R.3    Damiani, E.4    Margreth, A.5
  • 12
    • 0035369435 scopus 로고    scopus 로고
    • Role of myoplasmic phosphate in contractile function of skeletal muscle: Studies on creatine kinase-deficient mice
    • Dahlstedt AJ, Katz A & Westerblad H (2001). Role of myoplasmic phosphate in contractile function of skeletal muscle: studies on creatine kinase-deficient mice. J Physiol 533, 379-388.
    • (2001) J. Physiol. , vol.533 , pp. 379-388
    • Dahlstedt, A.J.1    Katz, A.2    Westerblad, H.3
  • 13
    • 0034063864 scopus 로고    scopus 로고
    • Is creatine kinase responsible for fatigue? Studies of skeletal muscle deficient of creatine kinase
    • Dahlstedt AJ, Katz A, Wieringa B & Westerblad H (2000). Is creatine kinase responsible for fatigue? Studies of skeletal muscle deficient of creatine kinase. FASEB J 14, 982-990.
    • (2000) FASEB J. , vol.14 , pp. 982-990
    • Dahlstedt, A.J.1    Katz, A.2    Wieringa, B.3    Westerblad, H.4
  • 14
    • 0034627188 scopus 로고    scopus 로고
    • Phosphorylation of anchoring protein by calmodulin protein kinase associated to the sarcoplasmic reticulum of rabbit fast-twitch muscle
    • Damiani E, Sacchetto R & Margreth A (2000a). Phosphorylation of anchoring protein by calmodulin protein kinase associated to the sarcoplasmic reticulum of rabbit fast-twitch muscle. Biochem Biophys Res Commun 279, 181-189.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 181-189
    • Damiani, E.1    Sacchetto, R.2    Margreth, A.3
  • 17
    • 0036512386 scopus 로고    scopus 로고
    • Bi-directional coupling between dihydropyridine receptors and ryanodine receptors
    • Dirksen RT (2002). Bi-directional coupling between dihydropyridine receptors and ryanodine receptors. Front Biosci 7, d659-d670.
    • (2002) Front Biosci. , vol.7
    • Dirksen, R.T.1
  • 18
  • 19
    • 0035200868 scopus 로고    scopus 로고
    • Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII
    • Dulhunty AF, Laver D, Curtis SM, Pace S, Haarmann C & Gallant EM (2001). Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII. Biophys J 81, 3240-3252.
    • (2001) Biophys. J. , vol.81 , pp. 3240-3252
    • Dulhunty, A.F.1    Laver, D.2    Curtis, S.M.3    Pace, S.4    Haarmann, C.5    Gallant, E.M.6
  • 20
    • 0033781028 scopus 로고    scopus 로고
    • Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels
    • Dzhura I, Wu Y, Colbran RJ, Balser JR & Anderson ME (2000). Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels. Nat Cell Biol 2, 173-177.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 173-177
    • Dzhura, I.1    Wu, Y.2    Colbran, R.J.3    Balser, J.R.4    Anderson, M.E.5
  • 21
    • 0035449318 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent protein kinase II in dorsal root ganglion neurons
    • 2+-calmodulin-dependent protein kinase II in dorsal root ganglion neurons. J Neurosci 21, 6694-6705.
    • (2001) J. Neurosci. , vol.21 , pp. 6694-6705
    • Eshete, F.1    Fields, R.D.2
  • 22
    • 0034783773 scopus 로고    scopus 로고
    • Spinal and supraspinal factors in human muscle fatigue
    • Gandevia SC (2001). Spinal and supraspinal factors in human muscle fatigue. Physiol Rev 81, 1725-1789.
    • (2001) Physiol. Rev. , vol.81 , pp. 1725-1789
    • Gandevia, S.C.1
  • 23
    • 0028089680 scopus 로고
    • Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from skeletal muscle
    • Hain J, Nath S, Mayrleitner M, Fleischer S & Schindler H (1994). Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from skeletal muscle. Biophys J 67, 1823-1833.
    • (1994) Biophys. J. , vol.67 , pp. 1823-1833
    • Hain, J.1    Nath, S.2    Mayrleitner, M.3    Fleischer, S.4    Schindler, H.5
  • 24
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • Hanson PI, Meyer T, Stryer L & Schulman H (1994). Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron 12, 943-956.
    • (1994) Neuron , vol.12 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 25
    • 0037097022 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. Biochem J 364, 593-611.
    • (2002) Biochem. J. , vol.364 , pp. 593-611
    • Hudmon, A.1    Schulman, H.2
  • 27
    • 0036548732 scopus 로고    scopus 로고
    • 2+ release in skeletal muscle: Insights from skinned fibers
    • 2+ release in skeletal muscle: insights from skinned fibers. Front Biosci 7, d834-842.
    • (2002) Front Biosci. , vol.7
    • Lamb, G.D.1
  • 28
    • 0023242419 scopus 로고
    • The temperature dependence of isometric contractions of single, intact fibres dissected from a mouse foot muscle
    • Lännergren J & Westerblad H (1987). The temperature dependence of isometric contractions of single, intact fibres dissected from a mouse foot muscle. J Physiol 390, 285-293.
    • (1987) J. Physiol. , vol.390 , pp. 285-293
    • Lännergren, J.1    Westerblad, H.2
  • 29
    • 0030906866 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent protein kinase II on cardiac excitation-contraction coupling in ferret ventricular myocytes
    • 2+-calmodulin-dependent protein kinase II on cardiac excitation-contraction coupling in ferret ventricular myocytes. J Physiol 501, 17-31.
    • (1997) J. Physiol. , vol.501 , pp. 17-31
    • Li, L.1    Satoh, H.2    Ginsburg, K.S.3    Bers, D.M.4
  • 30
    • 0029080486 scopus 로고
    • Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism
    • Lokuta AJ, Rogers TB, Lederer WJ & Valdivia HH (1995). Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism. J Physiol 487, 609-622.
    • (1995) J. Physiol. , vol.487 , pp. 609-622
    • Lokuta, A.J.1    Rogers, T.B.2    Lederer, W.J.3    Valdivia, H.H.4
  • 31
    • 0036702526 scopus 로고    scopus 로고
    • Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat to heartbeat and beyond
    • Maier LS & Bers DM (2002). Calcium, calmodulin, and calcium-calmodulin kinase II: heartbeat to heartbeat and beyond. J Mol Cell Cardiol 34, 919-939.
    • (2002) J. Mol. Cell Cardiol. , vol.34 , pp. 919-939
    • Maier, L.S.1    Bers, D.M.2
  • 32
    • 4243279444 scopus 로고    scopus 로고
    • Structural interaction between RYRs and DHPRs in calcium release units of cardiac and skeletal muscle cells
    • Protasi F (2002). Structural interaction between RYRs and DHPRs in calcium release units of cardiac and skeletal muscle cells. Front Biosci 7, d650-658.
    • (2002) Front Biosci. , vol.7
    • Protasi, F.1
  • 33
    • 0034702973 scopus 로고    scopus 로고
    • 2+-ATPase slow-twitch isoform and of beta calmodulin-dependent protein kinase in phospholamban-deficient sarcoplasmic reticulum of rabbit masseter muscle
    • 2+-ATPase slow-twitch isoform and of beta calmodulin-dependent protein kinase in phospholamban-deficient sarcoplasmic reticulum of rabbit masseter muscle. FEBS Lett 481, 255-260.
    • (2000) FEBS Lett. , vol.481 , pp. 255-260
    • Sacchetto, R.1    Damiani, E.2    Pallanca, A.3    Margreth, A.4
  • 34
    • 0026799405 scopus 로고
    • Inactivation of the sarcoplasmic reticulum calcium channel by protein kinase
    • Wang J & Best PM (1992). Inactivation of the sarcoplasmic reticulum calcium channel by protein kinase. Nature 359, 739-741.
    • (1992) Nature , vol.359 , pp. 739-741
    • Wang, J.1    Best, P.M.2
  • 36
    • 0029867353 scopus 로고    scopus 로고
    • The effects of intracellular injections of phosphate on intracellular calcium and force in single fibres of mouse skeletal muscle
    • Westerblad H & Allen DG (1996b). The effects of intracellular injections of phosphate on intracellular calcium and force in single fibres of mouse skeletal muscle. Pflugers Arch 431, 964-970.
    • (1996) Pflugers Arch. , vol.431 , pp. 964-970
    • Westerblad, H.1    Allen, D.G.2
  • 38
    • 0027240491 scopus 로고
    • Intracellular calcium concentration during low-frequency fatigue in isolated single fibers of mouse skeletal muscle
    • Westerblad H, Duty S & Allen DG (1993). Intracellular calcium concentration during low-frequency fatigue in isolated single fibers of mouse skeletal muscle. J Appl Physiol 75, 382-388.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 382-388
    • Westerblad, H.1    Duty, S.2    Allen, D.G.3
  • 39
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher DR, Kovacs RJ, Schulman H, Cefali DC & Jones LR (1991). Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 266, 11144-11152.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5
  • 41
    • 0035957010 scopus 로고    scopus 로고
    • Calmodulin kinase is a molecular switch for cardiac excitation-contraction coupling
    • Wu Y, Colbran RJ & Anderson ME (2001). Calmodulin kinase is a molecular switch for cardiac excitation-contraction coupling. Proc Natl Acad Sci U S A 98, 2877-2881.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 2877-2881
    • Wu, Y.1    Colbran, R.J.2    Anderson, M.E.3
  • 42
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type calcium channels
    • Zühlke RD, Pitt GS, Deisseroth K, Tsien RW & Reuter H (1999). Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature 399, 159-162.
    • (1999) Nature , vol.399 , pp. 159-162
    • Zühlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.