메뉴 건너뛰기




Volumn 123, Issue 6, 2004, Pages 743-757

Antagonistic regulation of native Ca2+- and ATP-sensitive cation channels in brain capillaries by nucleotides and decavanadate

Author keywords

Blood brain barrier; Competitive binding; Kinetic model; Microscopic reversibility; Trp channels

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM ION; CATION CHANNEL; DECAVANADIC ACID; NUCLEOTIDE DERIVATIVE; PHOSPHATE; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 2942678754     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200309008     Document Type: Article
Times cited : (11)

References (60)
  • 1
    • 0014675819 scopus 로고
    • Intracellular organic phosphates as regulators of oxygen release by haemoglobin
    • Benesch, R., and R.E. Benesch. 1969. Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature. 221:618-622.
    • (1969) Nature , vol.221 , pp. 618-622
    • Benesch, R.1    Benesch, R.E.2
  • 2
    • 0022038808 scopus 로고
    • Do vanadate polyanions inhibit phosphotransferase enzymes?
    • Boyd, D.W., K. Kustin, and M. Niwa. 1985. Do vanadate polyanions inhibit phosphotransferase enzymes? Biochim. Biophys. Acta. 827: 472-475.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 472-475
    • Boyd, D.W.1    Kustin, K.2    Niwa, M.3
  • 3
    • 0000805140 scopus 로고
    • Fitting curves to data. The simplex algorithm is the answer
    • Caceci, M.S., and W.P. Cacheris. 1984. Fitting curves to data. The simplex algorithm is the answer. Byte. May:340-348.
    • (1984) Byte , vol.MAY , pp. 340-348
    • Caceci, M.S.1    Cacheris, W.P.2
  • 4
    • 0141456728 scopus 로고    scopus 로고
    • Functional coupling between sulfonylurea receptor type 1 and a nonselective cation channel in reactive astrocytes from adult rat brain
    • Chen, M., Y. Dong, and J.M. Simard. 2003. Functional coupling between sulfonylurea receptor type 1 and a nonselective cation channel in reactive astrocytes from adult rat brain. J Neurosci. 23: 8568-8577.
    • (2003) J. Neurosci. , vol.23 , pp. 8568-8577
    • Chen, M.1    Dong, Y.2    Simard, J.M.3
  • 5
    • 0035449886 scopus 로고    scopus 로고
    • 2+ and ATP in native reactive astrocytes from adult rat brain
    • 2+ and ATP in native reactive astrocytes from adult rat brain. J. Neurosci. 21:6512-6521.
    • (2001) J. Neurosci. , vol.21 , pp. 6512-6521
    • Chen, M.1    Simard, J.M.2
  • 6
    • 0042377364 scopus 로고    scopus 로고
    • Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels
    • Chen, M.F., and T.Y. Chen. 2003. Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels. J. Gen. Physiol. 122:133-145.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 133-145
    • Chen, M.F.1    Chen, T.Y.2
  • 7
    • 0018577178 scopus 로고
    • Studies on heart phosphofructokinase. Decavanadate as a potent allosteric inhibitor at alkaline and acidic pH
    • Choate, G., and T.E. Mansour. 1979. Studies on heart phosphofructokinase. Decavanadate as a potent allosteric inhibitor at alkaline and acidic pH. J. Biol. Chem. 254:11457-11462.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11457-11462
    • Choate, G.1    Mansour, T.E.2
  • 8
    • 0022830347 scopus 로고
    • Oligovanadate binding to sarcoplasmic reticulum ATPase. Evidence for substrate analogue behavior
    • Coan, C., DJ. Scales, and AJ. Murphy. 1986. Oligovanadate binding to sarcoplasmic reticulum ATPase. Evidence for substrate analogue behavior. J. Biol. Chem. 261:10394-10403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10394-10403
    • Coan, C.1    Scales, D.J.2    Murphy, A.J.3
  • 9
    • 0019776473 scopus 로고
    • Inward current channels activated by intracellular Ca in cultured cardiac cells
    • Colquhoun, D., E. Neher, H. Reuter, and C.F. Stevens. 1981. Inward current channels activated by intracellular Ca in cultured cardiac cells. Nature. 294:752-754.
    • (1981) Nature , vol.294 , pp. 752-754
    • Colquhoun, D.1    Neher, E.2    Reuter, H.3    Stevens, C.F.4
  • 10
    • 17144456826 scopus 로고    scopus 로고
    • Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms
    • Csanády, L. 2000. Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms. Biophys. J. 78:785-799.
    • (2000) Biophys. J. , vol.78 , pp. 785-799
    • Csanády, L.1
  • 11
    • 0038480003 scopus 로고    scopus 로고
    • 2+- and ATP-sensitive cationic channels in brain capillary endothelium
    • 2+- and ATP-sensitive cationic channels in brain capillary endothelium. Biophys. J. 85:313-327.
    • (2003) Biophys. J. , vol.85 , pp. 313-327
    • Csanády, L.1    Adam-Vizi, V.2
  • 12
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • Csanády, L., K.W. Chan, D. Seto-Young, D.C. Kopsco, A.C. Nairn, and D.C. Gadsby. 2000. Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J. Gen. Physiol. 116:477-500.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 477-500
    • Csanády, L.1    Chan, K.W.2    Seto-Young, D.3    Kopsco, D.C.4    Nairn, A.C.5    Gadsby, D.C.6
  • 14
    • 0032458043 scopus 로고    scopus 로고
    • Improved growth of cultured brain microvascular endothelial cells on glass coated with a biological matrix
    • Dömötör, E., I. Sipos, A. Kittel, N.J. Abbott, and V. Adam-Vizi. 1998. Improved growth of cultured brain microvascular endothelial cells on glass coated with a biological matrix. Neurochem. Int. 33: 473-478.
    • (1998) Neurochem. Int. , vol.33 , pp. 473-478
    • Dömötör, E.1    Sipos, I.2    Kittel, A.3    Abbott, N.J.4    Adam-Vizi, V.5
  • 15
    • 0025003121 scopus 로고
    • Quinine inhibits chloride and nonselective cation channels in isolated rat distal colon cells
    • Gögelein, H., and K. Capek. 1990. Quinine inhibits chloride and nonselective cation channels in isolated rat distal colon cells. Biochim. Biophys. Acta. 1027:191-198.
    • (1990) Biochim. Biophys. Acta , vol.1027 , pp. 191-198
    • Gögelein, H.1    Capek, K.2
  • 16
    • 0025104274 scopus 로고
    • Non-selective cation channel on pancreatic duct cells
    • Gray, M.A., and B.E. Argent. 1990. Non-selective cation channel on pancreatic duct cells. Biochim. Biophys. Acta. 1029:33-42.
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 33-42
    • Gray, M.A.1    Argent, B.E.2
  • 17
    • 0037098880 scopus 로고    scopus 로고
    • 2+-activated nonselective cation channel during dedifferentiation of cultured rat ventricular cardiomyocytes
    • 2+-activated nonselective cation channel during dedifferentiation of cultured rat ventricular cardiomyocytes. J. Membr. Biol. 188:127-135.
    • (2002) J. Membr. Biol. , vol.188 , pp. 127-135
    • Guinamard, R.1    Rahmati, M.2    Lenfant, J.3    Bois, P.4
  • 18
    • 0036668296 scopus 로고    scopus 로고
    • Adenosine 5′-monophosphate is a selective inhibitor of the brown adipocyte nonselective cation channel
    • Halonen, J., and J. Nedergaard. 2002. Adenosine 5′-monophosphate is a selective inhibitor of the brown adipocyte nonselective cation channel. J. Membr. Biol. 188:183-197.
    • (2002) J. Membr. Biol. , vol.188 , pp. 183-197
    • Halonen, J.1    Nedergaard, J.2
  • 19
    • 0034177642 scopus 로고    scopus 로고
    • From worm to man: Three subfamilies of TRP channels
    • Harteneck, C., T.D. Plant, and G. Schultz. 2000. From worm to man: three subfamilies of TRP channels. Trends Neurosci. 23:159-166.
    • (2000) Trends Neurosci. , vol.23 , pp. 159-166
    • Harteneck, C.1    Plant, T.D.2    Schultz, G.3
  • 21
    • 0034730656 scopus 로고    scopus 로고
    • Distinct topologies of mono- and decavanadate binding and photo-oxidative cleavage in the sarcoplasmic reticulum ATPase
    • Hua, S., G. Inesi, and C. Toyoshima. 2000. Distinct topologies of mono- and decavanadate binding and photo-oxidative cleavage in the sarcoplasmic reticulum ATPase. J. Biol. Chem. 275:30546-30550.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30546-30550
    • Hua, S.1    Inesi, G.2    Toyoshima, C.3
  • 22
    • 0026633526 scopus 로고
    • Blockers of platelet-derived growth factor-activated nonselective cation channel inhibit cell proliferation
    • Jung, F., S. Selvaraj, and J.J. Gargus. 1992. Blockers of platelet-derived growth factor-activated nonselective cation channel inhibit cell proliferation. Am. J. Physiol. 262:C1464-C1470.
    • (1992) Am. J. Physiol. , vol.262
    • Jung, F.1    Selvaraj, S.2    Gargus, J.J.3
  • 23
    • 0032947989 scopus 로고    scopus 로고
    • Non-selective cation channels in endothelial cells derived from human umbilical vein
    • Kamouchi, M., A. Mamin, G. Droogmans, and B. Nilius. 1999. Non-selective cation channels in endothelial cells derived from human umbilical vein. J. Membr. Biol. 169:29-38.
    • (1999) J. Membr. Biol. , vol.169 , pp. 29-38
    • Kamouchi, M.1    Mamin, A.2    Droogmans, G.3    Nilius, B.4
  • 24
    • 0033673710 scopus 로고    scopus 로고
    • Norepinephrine-induced sustained inward current in brown fat cells: α(1)-mediated by nonselective cation channels
    • Koivisto, A., D. Siemen, and J. Nedergaard. 2000. Norepinephrine-induced sustained inward current in brown fat cells: α(1)-mediated by nonselective cation channels. Am. J. Physiol. Endocrinol. Metab. 279:E963-E977.
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.279
    • Koivisto, A.1    Siemen, D.2    Nedergaard, J.3
  • 25
    • 0028335890 scopus 로고
    • Effect of vanadium ions on ATP citrate lyase
    • Krivanek, J. 1994. Effect of vanadium ions on ATP citrate lyase. Gen. Physiol. Biophys. 13:43-55.
    • (1994) Gen. Physiol. Biophys. , vol.13 , pp. 43-55
    • Krivanek, J.1
  • 27
    • 0037648699 scopus 로고    scopus 로고
    • 2+- activated cation channel from hamster vomeronasal sensory neurons
    • 2+-activated cation channel from hamster vomeronasal sensory neurons. J. Physiol. 548:777-787.
    • (2003) J. Physiol. , vol.548 , pp. 777-787
    • Liman, E.R.1
  • 28
    • 0344149569 scopus 로고    scopus 로고
    • 2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5
    • 2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5. Proc. Natl. Acad. Sci. USA. 100:15160-15165.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15160-15165
    • Liu, D.1    Liman, E.R.2
  • 32
    • 0021646385 scopus 로고
    • Three types of calcium-dependent channel in rat lacrimal glands
    • Marty, A., Y.P. Tan, and A. Trautmann. 1984. Three types of calcium-dependent channel in rat lacrimal glands. J. Physiol. 357: 293-325.
    • (1984) J. Physiol. , vol.357 , pp. 293-325
    • Marty, A.1    Tan, Y.P.2    Trautmann, A.3
  • 33
    • 0019920766 scopus 로고
    • Cholecystokinin activation of single-channel currents is mediated by internal messenger in pancreatic acinar cells
    • Maruyama, Y., and O.H. Petersen. 1982. Cholecystokinin activation of single-channel currents is mediated by internal messenger in pancreatic acinar cells. Nature. 300:61-63.
    • (1982) Nature , vol.300 , pp. 61-63
    • Maruyama, Y.1    Petersen, O.H.2
  • 34
    • 0023645767 scopus 로고
    • Binding of nucleotides to the ATP-dependent protease La from Escherichia coli
    • Menon, A.S., and A.L. Goldberg. 1987. Binding of nucleotides to the ATP-dependent protease La from Escherichia coli. J. Biol. Chem. 262:14921-14928.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14921-14928
    • Menon, A.S.1    Goldberg, A.L.2
  • 35
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a ClC-type chloride ion channel
    • Middleton, R.E., DJ. Pheasant, and C. Miller. 1996. Homodimeric architecture of a ClC-type chloride ion channel. Nature. 383:337-340.
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 38
    • 0043074453 scopus 로고    scopus 로고
    • Electrostatic tuning of ion conductance in potassium channels
    • Nimigean, C.M., J.S. Chappie, and C. Miller. 2003. Electrostatic tuning of ion conductance in potassium channels. Biochemistry. 42:9263-9268.
    • (2003) Biochemistry , vol.42 , pp. 9263-9268
    • Nimigean, C.M.1    Chappie, J.S.2    Miller, C.3
  • 39
    • 0017381166 scopus 로고
    • Substrate positions and induced-fit in crystalline adenylate kinase
    • Pai, E.F., W. Sachsenheimer, R.H. Schirmer, and G.E. Schulz. 1977. Substrate positions and induced-fit in crystalline adenylate kinase. J. Mol. Biol. 114:37-45.
    • (1977) J. Mol. Biol. , vol.114 , pp. 37-45
    • Pai, E.F.1    Sachsenheimer, W.2    Schirmer, R.H.3    Schulz, G.E.4
  • 40
    • 0024327136 scopus 로고
    • A cation channel in the thick ascending limb of Henle's loop of the mouse kidney: Inhibition by adenine nucleotides
    • Paulais, M., and J. Teulon. 1989. A cation channel in the thick ascending limb of Henle's loop of the mouse kidney: inhibition by adenine nucleotides. J. Physiol. 413:315-327.
    • (1989) J. Physiol. , vol.413 , pp. 315-327
    • Paulais, M.1    Teulon, J.2
  • 43
    • 0037031319 scopus 로고    scopus 로고
    • Cation channels: Homing in on the elusive CAN channels
    • Petersen, O.H. 2002. Cation channels: homing in on the elusive CAN channels. Curr. Biol. 12:R520-R522.
    • (2002) Curr. Biol. , vol.12
    • Petersen, O.H.1
  • 44
    • 0036849354 scopus 로고    scopus 로고
    • Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif
    • Pezza, R.J., M.A. Villarreal, G.G. Montich, and C.E. Argarana. 2002. Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif. Nucleic Acids Res. 30:4700-4708.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4700-4708
    • Pezza, R.J.1    Villarreal, M.A.2    Montich, G.G.3    Argarana, C.E.4
  • 45
    • 0026637681 scopus 로고
    • A calcium and ATP sensitive non-selective cation channel in the antiluminal membrane of rat cerebral capillary endothelial cells
    • Popp, R., and H. Gögelein. 1992. A calcium and ATP sensitive non-selective cation channel in the antiluminal membrane of rat cerebral capillary endothelial cells. Biochim. Biophys. Acta. 1108:59-66.
    • (1992) Biochim. Biophys. Acta , vol.1108 , pp. 59-66
    • Popp, R.1    Gögelein, H.2
  • 47
    • 0037799198 scopus 로고    scopus 로고
    • A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity
    • Prescott, E.D., and D. Julius. 2003. A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity. Science. 300:1284-1288.
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 48
    • 0033520290 scopus 로고    scopus 로고
    • Interaction of vanadate with the cloned beta cell K(ATP) channel
    • Proks, P., R. Ashfield, and EM. Ashcroft. 1999. Interaction of vanadate with the cloned beta cell K(ATP) channel. J. Biol. Chem. 274: 25393-25397.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25393-25397
    • Proks, P.1    Ashfield, R.2    Ashcroft, E.M.3
  • 49
    • 0034693148 scopus 로고    scopus 로고
    • Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase
    • Reichard, P., R. Eliasson, R. Ingemarson, and L. Thelander. 2000. Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase. J. Biol. Chem. 275:33021-33026.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33021-33026
    • Reichard, P.1    Eliasson, R.2    Ingemarson, R.3    Thelander, L.4
  • 51
    • 0023664954 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P
    • 2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P. J. Biol. Chem. 262:12977-12983.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12977-12983
    • Ross, D.C.1    McIntosh, D.B.2
  • 53
    • 0021101207 scopus 로고
    • Effect of oxyanions of the early transition metals on rabbit skeletal muscle phosphorylase
    • Soman, G., Y.C. Chang, and D.J. Graves. 1983. Effect of oxyanions of the early transition metals on rabbit skeletal muscle phosphorylase. Biochemistry. 22:4994-5000.
    • (1983) Biochemistry , vol.22 , pp. 4994-5000
    • Soman, G.1    Chang, Y.C.2    Graves, D.J.3
  • 54
    • 0023025149 scopus 로고
    • Inhibition of a calcium-activated, non-selective cation channel, in a rat insulinoma cell line, by adenine derivatives
    • Sturgess, N.C., C.N. Hales, and M.L. Ashford. 1986. Inhibition of a calcium-activated, non-selective cation channel, in a rat insulinoma cell line, by adenine derivatives. FEBS Lett. 208:397-400.
    • (1986) FEBS Lett. , vol.208 , pp. 397-400
    • Sturgess, N.C.1    Hales, C.N.2    Ashford, M.L.3
  • 56
  • 57
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima, C., M. Nakasako, H. Nomura, and H. Ogawa. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature. 405:647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 59
    • 0021869073 scopus 로고
    • The binding of vanadium (V) oligoanions to sarcoplasmic reticulum
    • Varga, S., P. Csermely, and A. Martonosi. 1985. The binding of vanadium (V) oligoanions to sarcoplasmic reticulum. Eur. J. Biochem. 148:119-126.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 119-126
    • Varga, S.1    Csermely, P.2    Martonosi, A.3
  • 60
    • 0020003935 scopus 로고
    • 2+-activated nonselective cation channels in neuroblastoma
    • 2+-activated nonselective cation channels in neuroblastoma. Nature. 296:357-359.
    • (1982) Nature , vol.296 , pp. 357-359
    • Yellen, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.