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Volumn 273, Issue 5277, 1996, Pages 956-959

Regulation of cardiac Na+,Ca2+ exchange and K(ATP) potassium channels by PIP2

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; POTASSIUM CHANNEL;

EID: 0029831984     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5277.956     Document Type: Article
Times cited : (581)

References (62)
  • 1
    • 0024294230 scopus 로고
    • R. Vemuri and K. D. Philipson, Biochim. Biophys. Acta 937, 258 (1988); S. Luciani, S. Bova, G. Cargnelli, F. Cusinato, P. Debetto, Ann. N.Y. Acad. Sci. 639, 156 (1993).
    • (1988) Biochim. Biophys. Acta , vol.937 , pp. 258
    • Vemuri, R.1    Philipson, K.D.2
  • 6
    • 0001505065 scopus 로고
    • M. Seigneuret and Pl. F. Devaux, Proc. Natl. Acad. Sci. U.S.A. 81, 3751 (1984); J. Conner and A. J. Schroit, Biochemistry 27, 848 (1988); X. Tang, M. S. Halleck, R. A. Schlegel, P. Williamson, Science 272, 1495 (1996).
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3751
    • Seigneuret, M.1    Devaux, Pl.F.2
  • 7
    • 0023860020 scopus 로고
    • M. Seigneuret and Pl. F. Devaux, Proc. Natl. Acad. Sci. U.S.A. 81, 3751 (1984); J. Conner and A. J. Schroit, Biochemistry 27, 848 (1988); X. Tang, M. S. Halleck, R. A. Schlegel, P. Williamson, Science 272, 1495 (1996).
    • (1988) Biochemistry , vol.27 , pp. 848
    • Conner, J.1    Schroit, A.J.2
  • 8
    • 0029992825 scopus 로고    scopus 로고
    • M. Seigneuret and Pl. F. Devaux, Proc. Natl. Acad. Sci. U.S.A. 81, 3751 (1984); J. Conner and A. J. Schroit, Biochemistry 27, 848 (1988); X. Tang, M. S. Halleck, R. A. Schlegel, P. Williamson, Science 272, 1495 (1996).
    • (1996) Science , vol.272 , pp. 1495
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 9
    • 0027503866 scopus 로고
    • H. Kanoh, F. Sakane, S. Imai, I. Wada, Cell. Signalling 5, 495 (1993); C. Redman, J. Lefevre, M. L. McDonald, Biochem. Pharmacol. 50, 235 (1995); K. Goto, M. Funayama, H. Kondo, Proc. Natl. Acad. Sci. U.S.A. 50, 235 (1995).
    • (1993) Cell. Signalling , vol.5 , pp. 495
    • Kanoh, H.1    Sakane, F.2    Imai, S.3    Wada, I.4
  • 10
    • 0028981944 scopus 로고
    • H. Kanoh, F. Sakane, S. Imai, I. Wada, Cell. Signalling 5, 495 (1993); C. Redman, J. Lefevre, M. L. McDonald, Biochem. Pharmacol. 50, 235 (1995); K. Goto, M. Funayama, H. Kondo, Proc. Natl. Acad. Sci. U.S.A. 50, 235 (1995).
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 235
    • Redman, C.1    Lefevre, J.2    McDonald, M.L.3
  • 11
    • 0027503866 scopus 로고
    • H. Kanoh, F. Sakane, S. Imai, I. Wada, Cell. Signalling 5, 495 (1993); C. Redman, J. Lefevre, M. L. McDonald, Biochem. Pharmacol. 50, 235 (1995); K. Goto, M. Funayama, H. Kondo, Proc. Natl. Acad. Sci. U.S.A. 50, 235 (1995).
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.50 , pp. 235
    • Goto, K.1    Funayama, M.2    Kondo, H.3
  • 13
    • 0028986998 scopus 로고
    • L. Stephens, T. Jackson, P. T. Hawkins, Biochim. Biophys. Acta 1179, 27 (1993); S. B. Lee and S. G. Rhee, Curr. Opin. Cell Biol. 7, 183 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 183
    • Lee, S.B.1    Rhee, S.G.2
  • 14
    • 0001180854 scopus 로고
    • B. Sakmann and E. Neher, Eds. Plenum, New York
    • D. W. Hilgemann, in Single Channel Recording, B. Sakmann and E. Neher, Eds. (Plenum, New York, 1995), pp. 307-327.
    • (1995) Single Channel Recording , pp. 307-327
    • Hilgemann, D.W.1
  • 15
    • 9444261086 scopus 로고    scopus 로고
    • note
    • 2 was from Calbiochem, and all other phospholipids were from Avanti Polar Lipids (Alabaster, AL). PI-PLC (from Bacillus cereus) was from Calbiochem.
  • 17
    • 0000749232 scopus 로고
    • H. Ikezawa, M. Yamanegi, R. Tagushi, T. Miyashita, T. Ohyabu, Biochim. Biophys. Acta 450, 154 (1976); H. Ikezawa and R. Taguchi, Methods. Enzymol. 71, 731 (1981); J. J Volwerk, M. S. Shashidhar, A. Kuppe, O. H. Griffith, Biochemistry 29, 8056 (1990)
    • (1981) Methods. Enzymol. , vol.71 , pp. 731
    • Ikezawa, H.1    Taguchi, R.2
  • 18
    • 0025109107 scopus 로고
    • H. Ikezawa, M. Yamanegi, R. Tagushi, T. Miyashita, T. Ohyabu, Biochim. Biophys. Acta 450, 154 (1976); H. Ikezawa and R. Taguchi, Methods. Enzymol. 71, 731 (1981); J. J Volwerk, M. S. Shashidhar, A. Kuppe, O. H. Griffith, Biochemistry 29, 8056 (1990)
    • (1990) Biochemistry , vol.29 , pp. 8056
    • Volwerk, J.J.1    Shashidhar, M.S.2    Kuppe, A.3    Griffith, O.H.4
  • 19
    • 9444290890 scopus 로고    scopus 로고
    • note
    • Exchange current was recorded in 22 excised patches, 7 of which disrupted before completion of the experiment. Results from the nine stable control patches and six stable PI-PLC-treated patches were compared by Student's t tests. The average peak current after 4 min of recording was 67 ± 7 pA (SEM) in control patches and 51 ± 9 pA in PI-PLC treated patches. The difference was not significant (P > 0.1). During application of ATP, exchange current increased by 4.7 ± 0.9 times in control patches to 88 ± 14 pA and by 0.19 ± 0.05 times in treated patches to 14 ± 2 pA. The differences were highly significant (P < 0.001).
  • 20
  • 22
    • 0027102580 scopus 로고
    • D. W. Hilgemann, A. Collins, S. Matsuoka. J. Gen. Physiol. 100, 933 (1992); S. Matsuoka et al., ibid. 105, 403 (1995); D. O. Levitsky, D. A. Nicoll, K. D. Philipson, J. Biol. Chem. 269, 22847 (1994).
    • (1992) J. Gen. Physiol. , vol.100 , pp. 933
    • Hilgemann, D.W.1    Collins, A.2    Matsuoka, S.3
  • 23
    • 0028965584 scopus 로고
    • D. W. Hilgemann, A. Collins, S. Matsuoka. J. Gen. Physiol. 100, 933 (1992); S. Matsuoka et al., ibid. 105, 403 (1995); D. O. Levitsky, D. A. Nicoll, K. D. Philipson, J. Biol. Chem. 269, 22847 (1994).
    • (1995) J. Gen. Physiol. , vol.105 , pp. 403
    • Matsuoka, S.1
  • 24
    • 0028038204 scopus 로고
    • D. W. Hilgemann, A. Collins, S. Matsuoka. J. Gen. Physiol. 100, 933 (1992); S. Matsuoka et al., ibid. 105, 403 (1995); D. O. Levitsky, D. A. Nicoll, K. D. Philipson, J. Biol. Chem. 269, 22847 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22847
    • Levitsky, D.O.1    Nicoll, D.A.2    Philipson, K.D.3
  • 25
    • 9444290052 scopus 로고    scopus 로고
    • note
    • 2+ were small or absent. ATP effects were restored by PI.
  • 26
    • 9444245179 scopus 로고    scopus 로고
    • note
    • 2+.
  • 27
    • 0003421978 scopus 로고
    • Plenum, New York
    • Fast reversal was blocked by EDTA (0.5 mM), fluoride (0.2 mM), 5 mM phosphate, and 5′-adenylimidodiphosphate (2 mM), which all bind polyvalent cations (18, 19). 18. A. E. Martell and R. M. Smith, Critical Stability Constants, vol. 3, (Plenum, New York, 1977).
    • (1977) Critical Stability Constants , vol.3
    • Martell, A.E.1    Smith, R.M.2
  • 28
    • 0023783850 scopus 로고
    • R. B. Martin, Biochem. Biophys. Res. Commun. 155, 1194 (1988). EDTA (2 mM) only partially reversed the aluminum effect. Usually, exchange current could be fully restimulated by second and third applications of ATP after brief applications of aluminum.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 1194
    • Martin, R.B.1
  • 29
  • 30
    • 0023832149 scopus 로고
    • L. J. McDonald and M. D. Mamrack, J. Lipid Mediat. Cell Signal. 11, 81 (1995); J. D. Birchall and J. S. Chappell, Clin. Chem. 34, 265 (1988); C. Schofl et al., Biochem. J. 269, 547 (1990).
    • (1988) Clin. Chem. , vol.34 , pp. 265
    • Birchall, J.D.1    Chappell, J.S.2
  • 31
    • 0025356584 scopus 로고
    • L. J. McDonald and M. D. Mamrack, J. Lipid Mediat. Cell Signal. 11, 81 (1995); J. D. Birchall and J. S. Chappell, Clin. Chem. 34, 265 (1988); C. Schofl et al., Biochem. J. 269, 547 (1990).
    • (1990) Biochem. J. , vol.269 , pp. 547
    • Schofl, C.1
  • 32
    • 9444296686 scopus 로고    scopus 로고
    • note
    • 2+-activated PI hydrolysis in our assays, but inhibition has been reported for higher free aluminum concentrations, probably by aluminum binding to PI (20). As was consistent with a PI-aluminum interaction in cardiac patches, high concentrations of aluminum (100 to 500 μM with 10 mM EGTA) slowed development of the ATP effect and decreased its magnitude (12).
  • 34
    • 9444272389 scopus 로고    scopus 로고
    • note
    • 3 was added with twofold NaOH to compensate for protons released from EGTA. Fluorescence of ANEPPS increased in response to aluminum; fluorescence of rhodamine-labeled hexalysine decreased upon binding to vesicles, and the decrease was reversed by aluminum.
  • 38
    • 0028972501 scopus 로고
    • C. G. Nicholsand W. J. Lederer, Am. J. Physiol. 261, H1675 (1991); N. Inagaki et al., Science 270, 1166 (1995).
    • (1995) Science , vol.270 , pp. 1166
    • Inagaki, N.1
  • 39
    • 9444231288 scopus 로고
    • T. Ohno-Shosaku, B. J. Zuenkler, G. Trube, Pflügers Arch. 40, 133 (1987); R. Ribalet, S. Ciani, G. T. Eddlestone, J. Gen. Physiol. 94, 693 (1989); M. Takano, D. Qin, A. Noma, Am. J. Physiol. 58, H45 (1990).
    • (1987) Pflügers Arch. , vol.40 , pp. 133
    • Ohno-Shosaku, T.1    Zuenkler, B.J.2    Trube, G.3
  • 40
    • 0024434321 scopus 로고
    • T. Ohno-Shosaku, B. J. Zuenkler, G. Trube, Pflügers Arch. 40, 133 (1987); R. Ribalet, S. Ciani, G. T. Eddlestone, J. Gen. Physiol. 94, 693 (1989); M. Takano, D. Qin, A. Noma, Am. J. Physiol. 58, H45 (1990).
    • (1989) J. Gen. Physiol. , vol.94 , pp. 693
    • Ribalet, R.1    Ciani, S.2    Eddlestone, G.T.3
  • 41
    • 9444261085 scopus 로고
    • T. Ohno-Shosaku, B. J. Zuenkler, G. Trube, Pflügers Arch. 40, 133 (1987); R. Ribalet, S. Ciani, G. T. Eddlestone, J. Gen. Physiol. 94, 693 (1989); M. Takano, D. Qin, A. Noma, Am. J. Physiol. 58, H45 (1990).
    • (1990) Am. J. Physiol. , vol.58
    • Takano, M.1    Qin, D.2    Noma, A.3
  • 42
    • 9444268847 scopus 로고    scopus 로고
    • note
    • 2.
  • 43
    • 0028274104 scopus 로고    scopus 로고
    • P. A. Janmey, Annu. Rev. Physiol. 56, 169 (1994); A. Hall, Ann. Rev. Cell Biol. 10, 31 (1994); J. H. Hartwig et al., Cell 82, 643 (1995); A. P. Gilmore and K. Burridge, Nature 381, 5311 (1996).
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169
    • Janmey, P.A.1
  • 44
    • 0028170820 scopus 로고
    • P. A. Janmey, Annu. Rev. Physiol. 56, 169 (1994); A. Hall, Ann. Rev. Cell Biol. 10, 31 (1994); J. H. Hartwig et al., Cell 82, 643 (1995); A. P. Gilmore and K. Burridge, Nature 381, 5311 (1996).
    • (1994) Ann. Rev. Cell Biol. , vol.10 , pp. 31
    • Hall, A.1
  • 45
    • 0029117595 scopus 로고
    • P. A. Janmey, Annu. Rev. Physiol. 56, 169 (1994); A. Hall, Ann. Rev. Cell Biol. 10, 31 (1994); J. H. Hartwig et al., Cell 82, 643 (1995); A. P. Gilmore and K. Burridge, Nature 381, 5311 (1996).
    • (1995) Cell , vol.82 , pp. 643
    • Hartwig, J.H.1
  • 46
    • 0028274104 scopus 로고    scopus 로고
    • P. A. Janmey, Annu. Rev. Physiol. 56, 169 (1994); A. Hall, Ann. Rev. Cell Biol. 10, 31 (1994); J. H. Hartwig et al., Cell 82, 643 (1995); A. P. Gilmore and K. Burridge, Nature 381, 5311 (1996).
    • (1996) Nature , vol.381 , pp. 5311
    • Gilmore, A.P.1    Burridge, K.2
  • 49
    • 0027336147 scopus 로고
    • 2+ exchanger may be linked to the cytoskeleton by ankyrin [Z. P. Li, E. P. Burke, F. W. Frank, V. Bennett, K. D. Philipson, J. Biol. Chem. 268, 11489 (1993)], and disruption of the actin cytoskeleton inhibits exchange activity in a transfected cell line [M. Condrescu et al., ibid. 270, 9137 (1995)]. However, 10 μM cytochalasin D, 0.5 μM deoxyribonuclease, gelsolin, and G-actin were all without any evident influence on the effect of ATP on exchange current in giant patches, its reversal, or a series of ATP responses using aluminum (10 μM) to reverse the ATP effect (12). Gelsolin and actin were gifts of H. Yin.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11489
    • Li, Z.P.1    Burke, E.P.2    Frank, F.W.3    Bennett, V.4    Philipson, K.D.5
  • 50
    • 0028899965 scopus 로고
    • 2+ exchanger may be linked to the cytoskeleton by ankyrin [Z. P. Li, E. P. Burke, F. W. Frank, V. Bennett, K. D. Philipson, J. Biol. Chem. 268, 11489 (1993)], and disruption of the actin cytoskeleton inhibits exchange activity in a transfected cell line [M. Condrescu et al., ibid. 270, 9137 (1995)]. However, 10 μM cytochalasin D, 0.5 μM deoxyribonuclease, gelsolin, and G-actin were all without any evident influence on the effect of ATP on exchange current in giant patches, its reversal, or a series of ATP responses using aluminum (10 μM) to reverse the ATP effect (12). Gelsolin and actin were gifts of H. Yin.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9137
    • Condrescu, M.1
  • 51
    • 0021734626 scopus 로고
    • D. Choquette et al., Biochem. Biophys. Res. Commun. 125, 908 (1984); A. G. Filoteo, A. Enyedi, J. T. Penniston, J. Biol. Chem. 267, 11800 (1992)
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 908
    • Choquette, D.1
  • 54
    • 0029943112 scopus 로고    scopus 로고
    • M. Liscovitch, V. Chalifa, P. Pertile, C.-S. Chen, L. C. Cantley, J. Biol. Chem. 269, 21403 (1994); A. P. Gilmore and K. Burridge, Nature 381, 531 (1996).
    • (1996) Nature , vol.381 , pp. 531
    • Gilmore, A.P.1    Burridge, K.2
  • 57
    • 0026693943 scopus 로고
    • H. Ito et al., J. Gen. Physiol. 99, 961 (1992); R. Ribalet and S. Ciani, J. Memb. Biol. 142, 395 (1994).
    • (1992) J. Gen. Physiol. , vol.99 , pp. 961
    • Ito, H.1
  • 58
    • 0028670808 scopus 로고
    • H. Ito et al., J. Gen. Physiol. 99, 961 (1992); R. Ribalet and S. Ciani, J. Memb. Biol. 142, 395 (1994).
    • (1994) J. Memb. Biol. , vol.142 , pp. 395
    • Ribalet, R.1    Ciani, S.2
  • 61
    • 0024262551 scopus 로고
    • R. W. Tsien, Adv. Cyclic Nucleotide Res. 8, 363 (1977); M. Reiter, Pharmacol. Rev. 40, 189 (1988).
    • (1988) Pharmacol. Rev. , vol.40 , pp. 189
    • Reiter, M.1
  • 62
    • 9444227788 scopus 로고    scopus 로고
    • note
    • We thank P. C. Sternweis, S. Muallem, and H. L. Yin for insightful discussions, encouragement, and reagents; and S. Feng and X. Xu for technical help. Supported by grants from NIH (5-R1-HL51323-03) and the American Heart Association (95014830) to D.W.H. and from NIH (GM49993) to P.C. Sternweis.


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