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Volumn 45, Issue 6, 2009, Pages 546-553

Key role of a PtdIns-4,5P2 micro domain in ionic regulation of the mammalian heart Na+/Ca2+ exchanger

Author keywords

Mammalian heart; Membrane micro domains; Na+ Ca2+ exchanger; PtdIns 4,5P2; Transporter regulation

Indexed keywords

CALCIUM ION; CYCLIC AMP DEPENDENT PROTEIN KINASE; MARCKS PROTEIN; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE C; PROTON; SODIUM CALCIUM EXCHANGE PROTEIN; SODIUM ION;

EID: 67349114795     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2009.03.010     Document Type: Review
Times cited : (10)

References (70)
  • 1
    • 0032801648 scopus 로고    scopus 로고
    • Sodium/calcium exchange: its physiological implication
    • Blaustein M.P., and Lederer W.J. Sodium/calcium exchange: its physiological implication. Physiol. Rev. 79 (1999) 763-854
    • (1999) Physiol. Rev. , vol.79 , pp. 763-854
    • Blaustein, M.P.1    Lederer, W.J.2
  • 2
    • 33644838636 scopus 로고    scopus 로고
    • Sodium/calcium exchanger: influence of metabolic regulation on ion carrier interactions
    • DiPolo R., and Beaugé L. Sodium/calcium exchanger: influence of metabolic regulation on ion carrier interactions. Physiol. Rev. 86 (2006) 155-203
    • (2006) Physiol. Rev. , vol.86 , pp. 155-203
    • DiPolo, R.1    Beaugé, L.2
  • 7
    • 0035843910 scopus 로고    scopus 로고
    • 2+ exchange. Molecular and Pharmacological aspects
    • 2+ exchange. Molecular and Pharmacological aspects. Cir. Res. 88 (2001) 864-876
    • (2001) Cir. Res. , vol.88 , pp. 864-876
    • Shigekawa, M.1    Iwamoto, T.2
  • 10
    • 0033852625 scopus 로고    scopus 로고
    • Sodium-calcium exchange: a molecular perspective
    • Philipson K.D., and Nicoll D.A. Sodium-calcium exchange: a molecular perspective. Annu. Rev. Physiol. 62 (2000) 111-133
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 111-133
    • Philipson, K.D.1    Nicoll, D.A.2
  • 15
    • 0025233460 scopus 로고
    • 2+ exchange in giant excised sarcolemmal membrane patches
    • 2+ exchange in giant excised sarcolemmal membrane patches. Nature 344 (1990) 242-245
    • (1990) Nature , vol.344 , pp. 242-245
    • Hilgemann, D.W.1
  • 17
    • 0027218279 scopus 로고
    • The mechanism by which cytoplasmic protons inhibit the sodium-calcium exchanger in guinea-pig heart cells
    • Doering A.E., and Lederer W.J. The mechanism by which cytoplasmic protons inhibit the sodium-calcium exchanger in guinea-pig heart cells. J. Physiol. 466 (1993) 481-499
    • (1993) J. Physiol. , vol.466 , pp. 481-499
    • Doering, A.E.1    Lederer, W.J.2
  • 18
    • 0030899754 scopus 로고    scopus 로고
    • Cytoplasmic ATP-dependent regulation of ion transporters and channels: mechanisms and messengers
    • Hilgemann D.W. Cytoplasmic ATP-dependent regulation of ion transporters and channels: mechanisms and messengers. Annu. Rev. Physiol. 59 (1997) 193-220
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 193-220
    • Hilgemann, D.W.1
  • 25
    • 0027052783 scopus 로고
    • Steady-state and dynamic properties of cardiac sodium-calcium exchange. Sodium-dependent inactivation
    • Hilgemann D.W., Matsuoka S., Nagel G.A., and Collins A. Steady-state and dynamic properties of cardiac sodium-calcium exchange. Sodium-dependent inactivation. J. Gen. Physiol. 100 (1992) 905-932
    • (1992) J. Gen. Physiol. , vol.100 , pp. 905-932
    • Hilgemann, D.W.1    Matsuoka, S.2    Nagel, G.A.3    Collins, A.4
  • 27
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona O., and De Camilli P. Phosphoinositides in membrane traffic at the synapse. J. Cell Sci. 114 (2001) 1041-1052
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 29
    • 0033677862 scopus 로고    scopus 로고
    • 2 influences cytoskeletal protein activity at the plasma membrane
    • 2 influences cytoskeletal protein activity at the plasma membrane. J. Cell. Sci. 113 (2000) 13685-13695
    • (2000) J. Cell. Sci. , vol.113 , pp. 13685-13695
    • Sechi, A.S.1    Wehland, J.2
  • 33
    • 34547102486 scopus 로고    scopus 로고
    • Regulation of ion channels and transporters by phosphatidylinositol 4,5-bisphosphate
    • Robertson B. Regulation of ion channels and transporters by phosphatidylinositol 4,5-bisphosphate. J. Physiol. 582 (2007) 901-902
    • (2007) J. Physiol. , vol.582 , pp. 901-902
    • Robertson, B.1
  • 34
    • 0035424240 scopus 로고    scopus 로고
    • 2 regulation of surface membrane traffic
    • 2 regulation of surface membrane traffic. Curr. Opin. Cell. Biol. 13 (2001) 493-499
    • (2001) Curr. Opin. Cell. Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 35
    • 0032053708 scopus 로고    scopus 로고
    • The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate
    • Toker A. The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Cell. Biol. 10 (1998) 254-261
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 254-261
    • Toker, A.1
  • 37
    • 0028966081 scopus 로고
    • Inhibition of cardiac sarcolemmal sodium-calcium exchanger by glycerophosphoinositol 4-phosphate and glycerophosphoinositol 4-5-bisphosphate
    • Luciani S., Antonini M., Bova S., Cargnelli G., Cusinato F., Debetto P., Trevisi L., and Varotto R. Inhibition of cardiac sarcolemmal sodium-calcium exchanger by glycerophosphoinositol 4-phosphate and glycerophosphoinositol 4-5-bisphosphate. Biochem. Biophys. Res. Commun. 206 (1995) 674-680
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 674-680
    • Luciani, S.1    Antonini, M.2    Bova, S.3    Cargnelli, G.4    Cusinato, F.5    Debetto, P.6    Trevisi, L.7    Varotto, R.8
  • 39
    • 33748300740 scopus 로고    scopus 로고
    • Sodium-calcium exchange does not require allosteric calcium activation at high cytosolic sodium concentrations
    • Urbanczyk J., Chernysh O., Condrescu M., and Reeves J.P. Sodium-calcium exchange does not require allosteric calcium activation at high cytosolic sodium concentrations. J. Physiol. 575 (2006) 693-705
    • (2006) J. Physiol. , vol.575 , pp. 693-705
    • Urbanczyk, J.1    Chernysh, O.2    Condrescu, M.3    Reeves, J.P.4
  • 42
    • 0027964701 scopus 로고
    • Purification and characterization of polyphosphoinositede phosphatase from rat brain
    • Rath Hope H.M., and Pike L.J. Purification and characterization of polyphosphoinositede phosphatase from rat brain. J. Biol. Chem. 269 (1994) 23648-23654
    • (1994) J. Biol. Chem. , vol.269 , pp. 23648-23654
    • Rath Hope, H.M.1    Pike, L.J.2
  • 44
    • 34547110529 scopus 로고    scopus 로고
    • 2+ exchangers and K(ATP) channels: a long journey from membrane biophysics into cell biology
    • 2+ exchangers and K(ATP) channels: a long journey from membrane biophysics into cell biology. J. Physiol. 582 (2007) 903-909
    • (2007) J. Physiol. , vol.582 , pp. 903-909
    • Hilgemann, D.W.1
  • 45
    • 85047695896 scopus 로고    scopus 로고
    • 2+ exchanger displays a MgATP regulation similar to that of the exchange fluxes
    • 2+ exchanger displays a MgATP regulation similar to that of the exchange fluxes. Eur. J. Biochem. 268 (2001) 437-442
    • (2001) Eur. J. Biochem. , vol.268 , pp. 437-442
    • Asteggiano, C.1    Berberián, G.2    Beaugé, L.3
  • 49
    • 0020478960 scopus 로고
    • 2+ exchange in inside-out cardiac sarcolemmal vesicles
    • 2+ exchange in inside-out cardiac sarcolemmal vesicles. J. Biol. Chem. 257 (1982) 5111-5117
    • (1982) J. Biol. Chem. , vol.257 , pp. 5111-5117
    • Philipson, K.D.1    Nishimoto, A.Y.2
  • 50
    • 23944457745 scopus 로고    scopus 로고
    • Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase
    • Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J., Asami T., Yoshida S., Huber S.C., and Clouse S.D. Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17 (2005) 1685-1703
    • (2005) Plant Cell , vol.17 , pp. 1685-1703
    • Wang, X.1    Goshe, M.B.2    Soderblom, E.J.3    Phinney, B.S.4    Kuchar, J.A.5    Li, J.6    Asami, T.7    Yoshida, S.8    Huber, S.C.9    Clouse, S.D.10
  • 51
    • 0038343926 scopus 로고    scopus 로고
    • Localization of a highly active pool of type II phosphatidylinositol 4-kinase in a p97/valosin-containing-protein-rich fraction of the endoplasmic reticulum
    • Waugh M.G., Minogue S., Anderson J.S., Balinger A., Blumenkrantz D., Calnan D.P., Cramer R., and Hsuan J.J. Localization of a highly active pool of type II phosphatidylinositol 4-kinase in a p97/valosin-containing-protein-rich fraction of the endoplasmic reticulum. Biochem. J. 373 (2003) 57-63
    • (2003) Biochem. J. , vol.373 , pp. 57-63
    • Waugh, M.G.1    Minogue, S.2    Anderson, J.S.3    Balinger, A.4    Blumenkrantz, D.5    Calnan, D.P.6    Cramer, R.7    Hsuan, J.J.8
  • 52
  • 54
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa N., Homma Y., Yahara I., Sakai H., and Nishida E. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266 (1991) 17218-21721
    • (1991) J. Biol. Chem. , vol.266 , pp. 17218-21721
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 55
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profiling
    • Sohn R.H., Chen J., Koblan K.S., Bray P.F., and Goldschmidt-Clermont P.J. Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profiling. J. Biol. Chem. 270 (1995) 21114-21120
    • (1995) J. Biol. Chem. , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 57
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Yu F.X., Johnston P.A., Sudhof T.C., and Yin H.L. gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Science 250 (1990) 1413-1415
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4
  • 58
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey P.A., Lamb J., Allen P.G., and Matsudaira P.T. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267 (1992) 11818-11823
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 59
  • 60
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation
    • He H., Watanabe T., Zhan X., Huang C., Schuuring E., Fukami K., Takenawa T., Kumar C.C., Simpson R.J., and Maruta H. Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation. Mol. Cell. Biol. 18 (1998) 3829-3837
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 61
    • 16344372314 scopus 로고    scopus 로고
    • Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5-bisphosphate determined by site-directed spin labeling and high-resolution NMR
    • Ellena J.F., Wu J., Moulthrop J., Rauch M., Jaysinghne S., Castle J.D., and Cafiso D.S. Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5-bisphosphate determined by site-directed spin labeling and high-resolution NMR. Biophys. J. 87 (2004) 3221-3233
    • (2004) Biophys. J. , vol.87 , pp. 3221-3233
    • Ellena, J.F.1    Wu, J.2    Moulthrop, J.3    Rauch, M.4    Jaysinghne, S.5    Castle, J.D.6    Cafiso, D.S.7
  • 62
    • 37449027708 scopus 로고    scopus 로고
    • Structural insights into the PIP2 recognition by syntenin-1 PDZ domain
    • Sugi T., Oyama T., KMorikawa H., and Jingami. Structural insights into the PIP2 recognition by syntenin-1 PDZ domain. Biochem. Biophys. Res. Commun. 366 (2008) 373-378
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 373-378
    • Sugi, T.1    Oyama, T.2    KMorikawa, H.3    Jingami4
  • 63
    • 33947495167 scopus 로고    scopus 로고
    • 2+ exchangers: electrophysiological and optical characterization
    • 2+ exchangers: electrophysiological and optical characterization. J. Biol. Chem. 282 (2007) 3695-3701
    • (2007) J. Biol. Chem. , vol.282 , pp. 3695-3701
    • Ottolia, M.S.1    Ren, J.X.2    Philipson, K.D.3
  • 65
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22 (2006) 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 69
    • 40949088494 scopus 로고    scopus 로고
    • The sodium-calcium exchanger us a mechanosensitive transporter
    • Reeves J.P., Adellatif M., and Condrescu M. The sodium-calcium exchanger us a mechanosensitive transporter. J. Physiol. 586 (2008) 1549-1563
    • (2008) J. Physiol. , vol.586 , pp. 1549-1563
    • Reeves, J.P.1    Adellatif, M.2    Condrescu, M.3
  • 70
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on we: a case study the Phyre server
    • Kelly L.A., and Sternberg M.J.E. Protein structure prediction on we: a case study the Phyre server. Nat. Protocols 4 (2009) 363-371
    • (2009) Nat. Protocols , vol.4 , pp. 363-371
    • Kelly, L.A.1    Sternberg, M.J.E.2


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