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Journal of General Physiology
Volumn 141, Issue 1, 2013, Pages 85-94
Increased intracellular magnesium attenuates β-adrenergic stimulation of the cardiac Cav1.2 channel
Author keywords

[No Author keywords available]
Indexed keywords

1,4 DIHYDRO 2,6 DIMETHYL 5 NITRO 4 [2 (TRIFLUOROMETHYL)PHENYL] 3 PYRIDINECARBOXYLIC ACID METHYL ESTER; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CALCIUM CHANNEL L TYPE; CALCIUM CHANNEL STIMULATING AGENT; CAV1.2 PROTEIN, MOUSE; ISOPRENALINE; MAGNESIUM;
EID: 84872243420     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210864     Document Type: Article
Times cited : (7)
References (56)
  • 1
    • 0017353460 scopus 로고
    • Activation of cardiac adenylate cyclase: hormonal modification of the magnesium ion requirement
    • Alvarez, R., and J.J. Bruno. 1977. Activation of cardiac adenylate cyclase: hormonal modification of the magnesium ion requirement. Proc. Natl. Acad. Sci. USA. 74:92-95. http://dx.doi.org/10.1073/ pnas.74.1.92
    • (1977) Proc. Natl. Acad. Sci. , vol.74 , pp. 92-95
    • Alvarez, R.1    Bruno, J.J.2
  • 3
    • 33645391981 scopus 로고    scopus 로고
    • Regulatory properties of adenylate cyclases type 5 and 6: A progress report
    • Beazely, M.A., and V.J. Watts. 2006. Regulatory properties of adenylate cyclases type 5 and 6: A progress report. Eur. J. Pharmacol. 535:1-12. http://dx.doi.org/10.1016/j.ejphar.2006.01.054
    • (2006) Eur. J. Pharmacol. , vol.535 , pp. 1-12
    • Beazely, M.A.1    Watts, V.J.2
  • 7
    • 67749101940 scopus 로고    scopus 로고
    • 2+, the proximal C-terminal EF-hand, and the distal C-terminal domain
    • 2+, the proximal C-terminal EF-hand, and the distal C-terminal domain. J. Gen. Physiol. 134:81-94. http://dx.doi.org/10.1085/jgp.200910209
    • (2009) J. Gen. Physiol. , vol.134 , pp. 81-94
    • Brunet, S.1    Scheuer, T.2    Catterall, W.A.3
  • 9
    • 0034518423 scopus 로고    scopus 로고
    • 2+ channels. Annu
    • 2+ channels. Annu. Rev. Cell Dev. Biol. 16:521-555. http://dx.doi.org/10.1146/annurev.cellbio.16.1.521
    • (2000) Rev. Cell Dev. Biol. , vol.16 , pp. 521-555
    • Catterall, W.A.1
  • 10
    • 0019321925 scopus 로고
    • Adenylate cyclase: the role of magnesium and other divalent cations
    • Cech, S.Y., W.C. Broaddus, and M.E. Maguire. 1980. Adenylate cyclase: the role of magnesium and other divalent cations. Mol. Cell. Biochem. 33:67-92. http://dx.doi.org/10.1007/BF00224572
    • (1980) Mol. Cell. Biochem. , vol.33 , pp. 67-92
    • Cech, S.Y.1    Broaddus, W.C.2    Maguire, M.E.3
  • 11
    • 0025840253 scopus 로고
    • Characterization of the two size forms of the α1 subunit of skeletal muscle L-type calcium channels
    • De Jongh, K.S., C. Warner, A.A. Colvin, and W.A. Catterall. 1991. Characterization of the two size forms of the α1 subunit of skeletal muscle L-type calcium channels. Proc. Natl. Acad. Sci. USA. 88:10778-10782. http://dx.doi.org/10.1073/pnas.88.23.10778
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 10778-10782
    • De Jongh, K.S.1    Warner, C.2    Colvin, A.A.3    Catterall, W.A.4
  • 12
    • 0029795275 scopus 로고    scopus 로고
    • Specific phosphorylation of a site in the full-length form of the alpha 1 subunit of the cardiac L-type calcium channel by adenosine 3',5'-cyclic monophosphate-dependent protein kinase
    • De Jongh, K.S., B.J. Murphy, A.A. Colvin, J.W. Hell, M. Takahashi, and W.A. Catterall. 1996. Specific phosphorylation of a site in the full-length form of the alpha 1 subunit of the cardiac L-type calcium channel by adenosine 3',5'-cyclic monophosphate-dependent protein kinase. Biochemistry. 35:10392-10402. http://dx.doi.org/10.1021/bi953023c
    • (1996) Biochemistry , vol.35 , pp. 10392-10402
    • De Jongh, K.S.1    Murphy, B.J.2    Colvin, A.A.3    Hell, J.W.4    Takahashi, M.5    Catterall, W.A.6
  • 13
    • 1942517938 scopus 로고    scopus 로고
    • 2+ current in mouse cardiac myocytes
    • 2+ current in mouse cardiac myocytes. J. Physiol. 556:79-93. http://dx.doi.org/10.1113/jphysiol.2003.059329
    • (2004) J. Physiol. , vol.556 , pp. 79-93
    • duBell, W.H.1    Rogers, T.B.2
  • 14
    • 77958048278 scopus 로고    scopus 로고
    • Molecular mechanism of calcium channel regulation in the fight-or-flight response
    • ra70
    • Fuller, M.D., M.A. Emrick, M. Sadilek, T. Scheuer, and W.A. Catterall. 2010. Molecular mechanism of calcium channel regulation in the fight-or-flight response. Sci. Signal. 3:ra70. http:// dx.doi.org/10.1126/scisignal.2001152
    • (2010) Sci. Signal. , vol.3
    • Fuller, M.D.1    Emrick, M.A.2    Sadilek, M.3    Scheuer, T.4    Catterall, W.A.5
  • 15
    • 0030042273 scopus 로고    scopus 로고
    • Transfer of 1,4-dihydropyridine sensitivity from L-type to class A (BI) calcium channels
    • Grabner, M., Z.Y. Wang, S. Hering, J. Striessnig, and H. Glossmann. 1996. Transfer of 1,4-dihydropyridine sensitivity from L-type to class A (BI) calcium channels. Neuron. 16:207-218. http://dx.doi.org/10.1016/S0896-6273(00)80037-9
    • (1996) Neuron , vol.16 , pp. 207-218
    • Grabner, M.1    Wang, Z.Y.2    Hering, S.3    Striessnig, J.4    Glossmann, H.5
  • 17
    • 0024439601 scopus 로고
    • Effects of magnesium on inactivation of the voltage-gated calcium current in cardiac myocytes
    • Hartzell, H.C., and R.E. White. 1989. Effects of magnesium on inactivation of the voltage-gated calcium current in cardiac myocytes. J. Gen. Physiol. 94:745-767. http://dx.doi.org/10.1085/jgp.94.4.745
    • (1989) J. Gen. Physiol. , vol.94 , pp. 745-767
    • Hartzell, H.C.1    White, R.E.2
  • 18
    • 0029126640 scopus 로고
    • Effects of protein phosphatase and kinase inhibitors on the cardiac L-type Ca current suggest two sites are phosphorylated by protein kinase A and another protein kinase
    • Hartzell, H.C., Y. Hirayama, and J. Petit-Jacques. 1995. Effects of protein phosphatase and kinase inhibitors on the cardiac L-type Ca current suggest two sites are phosphorylated by protein kinase A and another protein kinase. J. Gen. Physiol. 106:393-414. http://dx.doi.org/10.1085/jgp.106.3.393
    • (1995) J. Gen. Physiol. , vol.106 , pp. 393-414
    • Hartzell, H.C.1    Hirayama, Y.2    Petit-Jacques, J.3
  • 19
    • 0025994342 scopus 로고
    • Cytosolic free magnesium in stimulated, hypoxic, and underperfused rat heart
    • Headrick, J.P., and R.J. Willis. 1991. Cytosolic free magnesium in stimulated, hypoxic, and underperfused rat heart. J. Mol. Cell. Cardiol. 23:991-999. http://dx.doi.org/10.1016/0022-2828(91)91635-5
    • (1991) J. Mol. Cell. Cardiol. , vol.23 , pp. 991-999
    • Headrick, J.P.1    Willis, R.J.2
  • 22
    • 17044424577 scopus 로고    scopus 로고
    • Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle
    • USA
    • Hulme, J.T., K. Konoki, T.W. Lin, M.A. Gritsenko, D.G. Camp II, D.J. Bigelow, and W.A. Catterall. 2005. Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle. Proc. Natl. Acad. Sci. USA. 102:5274-5279. http://dx.doi.org/10.1073/pnas.0409885102
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 5274-5279
    • Hulme, J.T.1    Konoki, K.2    Lin, T.W.3    Gritsenko, M.A.4    Camp II, D.G.5    Bigelow, D.J.6    Catterall, W.A.7
  • 25
    • 0031044250 scopus 로고    scopus 로고
    • The adenylyl cyclases as integrators of transmembrane signal transduction
    • Ishikawa, Y., and C.J. Homcy. 1997. The adenylyl cyclases as integrators of transmembrane signal transduction. Circ. Res. 80:297-304. http://dx.doi.org/10.1161/01.RES.80.3.297
    • (1997) Circ. Res. , vol.80 , pp. 297-304
    • Ishikawa, Y.1    Homcy, C.J.2
  • 26
    • 0019924660 scopus 로고
    • 2+ and enhancing its extent of activation by gua-nine nucleotides
    • USA
    • 2+ and enhancing its extent of activation by gua-nine nucleotides. Proc. Natl. Acad. Sci. USA. 79:5179-5183. http:// dx.doi.org/10.1073/pnas.79.17.5179
    • (1982) Proc. Natl. Acad. Sci. , vol.79 , pp. 5179-5183
    • Iyengar, R.1    Birnbaumer, L.2
  • 27
    • 0022381201 scopus 로고
    • On the mechanism of β-adrenergic regulation of the Ca channel in the guinea-pig heart
    • Kameyama, M., F. Hofmann, and W. Trautwein. 1985. On the mechanism of β-adrenergic regulation of the Ca channel in the guinea-pig heart. Pflugers Arch. 405:285-293. http://dx.doi.org/10.1007/ BF00582573
    • (1985) Pflugers Arch. , vol.405 , pp. 285-293
    • Kameyama, M.1    Hofmann, F.2    Trautwein, W.3
  • 28
    • 0022474217 scopus 로고
    • Modulation of Ca current during the phosphorylation cycle in the guinea pig heart
    • Kameyama, M., J. Hescheler, F. Hofmann, and W. Trautwein. 1986. Modulation of Ca current during the phosphorylation cycle in the guinea pig heart. Pflugers Arch. 407:123-128. http://dx.doi.org/10.1007/BF00580662
    • (1986) Pflugers Arch. , vol.407 , pp. 123-128
    • Kameyama, M.1    Hescheler, J.2    Hofmann, F.3    Trautwein, W.4
  • 29
    • 0034623827 scopus 로고    scopus 로고
    • Regulation of cardiac L-type calcium channels by protein kinase A and protein kinase C
    • Kamp, T.J., and J.W. Hell. 2000. Regulation of cardiac L-type calcium channels by protein kinase A and protein kinase C. Circ. Res. 87:1095-1102. http://dx.doi.org/10.1161/01.RES.87.12.1095
    • (2000) Circ. Res. , vol.87 , pp. 1095-1102
    • Kamp, T.J.1    Hell, J.W.2
  • 30
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • Krebs, E.G., and J.A. Beavo. 1979. Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48:923-959. http://dx.doi.org/10.1146/annurev.bi.48.070179.004423
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 923-953
    • Krebs, E.G.1    Beavo, J.A.2
  • 33
    • 0032875356 scopus 로고    scopus 로고
    • Physiological regulation of G protein-linked signaling
    • Morris, A.J., and C.C. Malbon. 1999. Physiological regulation of G protein-linked signaling. Physiol. Rev. 79:1373-1430.
    • (1999) Physiol. Rev. , vol.79 , pp. 1373-1430
    • Morris, A.J.1    Malbon, C.C.2
  • 34
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth
    • Mumby, M.C., and G. Walter. 1993. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73:673-699.
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 38
    • 0034791590 scopus 로고    scopus 로고
    • Phosphorylation-dependent modulation of cardiac calcium current by intracellular free magnesium
    • Pelzer, S., C. La, and D.J. Pelzer. 2001. Phosphorylation-dependent modulation of cardiac calcium current by intracellular free magnesium. Am. J. Physiol. Heart Circ. Physiol. 281:H1532-H1544.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Pelzer, S.1    La, C.2    Pelzer, D.J.3
  • 39
  • 40
    • 0031750463 scopus 로고    scopus 로고
    • The sympathetic nervous system and ischaemic heart disease
    • Remme, W.J. 1998. The sympathetic nervous system and ischaemic heart disease. Eur. Heart J. 19:F62-F71.
    • (1998) Eur. Heart J. , vol.19
    • Remme, W.J.1
  • 41
    • 0020693764 scopus 로고
    • Calcium channel modulation by neurotransmitters, enzymes and drugs
    • Reuter, H. 1983. Calcium channel modulation by neurotransmitters, enzymes and drugs. Nature. 301:569-574. http://dx.doi.org/10.1038/301569a0
    • (1983) Nature , vol.301 , pp. 569-574
    • Reuter, H.1
  • 42
    • 0033609051 scopus 로고    scopus 로고
    • ATP-linked structural change in protein kinase A precedes phosphoryl transfer under physiological magnesium concentrations
    • Shaffer, J., and J.A. Adams. 1999. An ATP-linked structural change in protein kinase A precedes phosphoryl transfer under physiological magnesium concentrations. Biochemistry. 38:5572-5581. http://dx.doi.org/10.1021/bi982768q
    • (1999) Biochemistry , vol.38 , pp. 5572-5581
    • Shaffer, J.1    Adams, J.A.2
  • 44
    • 0028838122 scopus 로고
    • Mammalian membrane-bound adenylyl cyclases
    • Taussig, R., and A.G. Gilman. 1995. Mammalian membrane-bound adenylyl cyclases. J. Biol. Chem. 270:1-4. http://dx.doi.org/10.1074/ jbc.270.1.1
    • (1995) J. Biol. Chem. , vol.270 , pp. 1-4
    • Taussig, R.1    Gilman, A.G.2
  • 45
    • 0015496308 scopus 로고
    • Cyclic AMP mediates the effects of adrenaline on cardiac purkinje fibres
    • Tsien, R.W., W. Giles, and P. Greengard. 1972. Cyclic AMP mediates the effects of adrenaline on cardiac purkinje fibres. Nat. New Biol. 240:181-183.
    • (1972) Nat. New Biol. , vol.240 , pp. 181-183
    • Tsien, R.W.1    Giles, W.2    Greengard, P.3
  • 47
    • 0346368252 scopus 로고    scopus 로고
    • 2+ current to protein kinase A: role of calmodulin
    • 2+ current to protein kinase A: role of calmodulin. Am. J. Physiol. Heart Circ. Physiol. 286:H186-H194. http://dx.doi.org/10.1152/ajpheart.00272.2003
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.286
    • Walsh, K.B.1    Cheng, Q.2
  • 48
    • 1642348821 scopus 로고    scopus 로고
    • Regulation of L-type calcium current by intracellular magnesium in rat cardiac myocytes
    • Wang, M., M. Tashiro, and J.R. Berlin. 2004. Regulation of L-type calcium current by intracellular magnesium in rat cardiac myocytes. J. Physiol. 555:383-396. http://dx.doi.org/10.1113/jphysiol.2003.048538
    • (2004) J. Physiol. , vol.555 , pp. 383-396
    • Wang, M.1    Tashiro, M.2    Berlin, J.R.3
  • 49
    • 0023882141 scopus 로고
    • Effects of intracellular free magnesium on calcium current in isolated cardiac myocytes
    • White, R.E., and H.C. Hartzell. 1988. Effects of intracellular free magnesium on calcium current in isolated cardiac myocytes. Science. 239:778-780. http://dx.doi.org/10.1126/science.2448878
    • (1988) Science , vol.239 , pp. 778-780
    • White, R.E.1    Hartzell, H.C.2
  • 50
    • 0024505252 scopus 로고
    • Magnesium ions in cardiac function. Regulator of ion channels and second messengers
    • White, R.E., and H.C. Hartzell. 1989. Magnesium ions in cardiac function. Regulator of ion channels and second messengers. Biochem. Pharmacol. 38:859-867. http://dx.doi.org/10.1016/ 0006-2952(89)90272-4
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 859-867
    • White, R.E.1    Hartzell, H.C.2
  • 52
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., D.R. Knighton, L.F. ten Eyck, R. Karlsson, N. Xuong, S.S. Taylor, and J.M. Sowadski. 1993a. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry. 32:2154-2161. http://dx.doi.org/10.1021/bi00060a005
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.5    Taylor, S.S.6    Sowadski, J.M.7
  • 53
    • 0000127673 scopus 로고
    • 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng, J., E.A. Trafny, D.R. Knighton, N.H. Xuong, S.S. Taylor, L.F. Ten Eyck, and J.M. Sowadski. 1993b. 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr. D Biol. Crystallogr. 49:362-365. http://dx.doi.org/10.1107/ S0907444993000423
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 362-365
    • Zheng, J.1    Trafny, E.A.2    Knighton, D.R.3    Xuong, N.H.4    Taylor, S.S.5    Ten Eyck, L.F.6    Sowadski, J.M.7
  • 54
    • 70349449921 scopus 로고    scopus 로고
    • Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development
    • USA
    • Zhou, H., and D.E. Clapham. 2009. Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development. Proc. Natl. Acad. Sci. USA. 106:15750-15755. http://dx.doi.org/10.1073/pnas.0908332106
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 15750-15755
    • Zhou, H.1    Clapham, D.E.2
  • 55
    • 46249120772 scopus 로고    scopus 로고
    • Effect of metal ions on high-affinity binding of pseudosubstrate inhibitors to PKA.
    • Zimmermann, B., S. Schweinsberg, S. Drewianka, and F.W. Herberg. 2008. Effect of metal ions on high-affinity binding of pseudosubstrate inhibitors to PKA. Biochem. J. 413:93-101. http://dx.doi.org/10.1042/BJ20071665
    • (2008) Biochem. J. , vol.413 , pp. 93-101
    • Zimmermann, B.1    Schweinsberg, S.2    Drewianka, S.3    Herberg, F.W.4
  • 56
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type calcium channels
    • Zühlke, R.D., G.S. Pitt, K. Deisseroth, R.W. Tsien, and H. Reuter. 1999. Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature. 399:159-162. http://dx.doi.org/10.1038/20200
    • (1999) Nature , vol.399 , pp. 159-162
    • Zuhlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5

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