메뉴 건너뛰기




Volumn 175, Issue 1, 2000, Pages 35-52

Direct comparison of NPPB and DPC as probes of CFTR expressed in Xenopus oocytes

Author keywords

Anion channel; Arylaminobenzoate; Chloride channel blocker; Cystic fibrosis; Cystic fibrosis transmembrane conductance regulator

Indexed keywords

AROMATIC AMINE; CHLORIDE CHANNEL; CHLORIDE CHANNEL BLOCKING AGENT; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0034192747     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002320001053     Document Type: Article
Times cited : (84)

References (69)
  • 1
    • 0032169499 scopus 로고    scopus 로고
    • Channel-lining residues in the M3 membrane-spanning segment of the cystic fibrosis transmembrane conductance regulator
    • 1. Akabas, M.A. 1998. Channel-lining residues in the M3 membrane-spanning segment of the cystic fibrosis transmembrane conductance regulator. Biochemistry 37:12233-12240
    • (1998) Biochemistry , vol.37 , pp. 12233-12240
    • Akabas, M.A.1
  • 2
    • 0026595919 scopus 로고
    • Proton transport mechanism in the cell membrane af Xenopus laevis oocytes
    • 2. Burckhardt, B.-C., Kroll, B., Frömter, E. 1992. Proton transport mechanism in the cell membrane af Xenopus laevis oocytes. Pfluegers. Arch. 420:78-82
    • (1992) Pfluegers. Arch. , vol.420 , pp. 78-82
    • Burckhardt, B.-C.1    Kroll, B.2    Frömter, E.3
  • 3
    • 0026572717 scopus 로고
    • Chemical probes for anion transporters of mammalian cell membranes
    • 3. Cabantchik, Z.I., Greger, R. 1992. Chemical probes for anion transporters of mammalian cell membranes. Am. J. Physiol. 262:C803-C827
    • (1992) Am. J. Physiol. , vol.262
    • Cabantchik, Z.I.1    Greger, R.2
  • 4
    • 0000410893 scopus 로고
    • The principles of the stochastic interpretations of ion-channel mechanisms
    • B. Sakmann and E. Neher, editors. Plenum Press, New York
    • 4. Colquhoun, D., Hawkes, A.G. 1995. The principles of the stochastic interpretations of ion-channel mechanisms. In: Single-Channel Recording. B. Sakmann and E. Neher, editors. pp. 397-482. Plenum Press, New York
    • (1995) Single-channel Recording , pp. 397-482
    • Colquhoun, D.1    Hawkes, A.G.2
  • 5
    • 0033605158 scopus 로고    scopus 로고
    • Cystic fibrosis-associated mutations at arginine 357 alter the pore architecture for CFTR: Evidence for disruption of a salt bridge
    • 5. Gotten, J.F., Welsh, M.J. 1999. Cystic fibrosis-associated mutations at arginine 357 alter the pore architecture for CFTR: Evidence for disruption of a salt bridge. J. Biol. Chem. 274:5429-5435
    • (1999) J. Biol. Chem. , vol.274 , pp. 5429-5435
    • Gotten, J.F.1    Welsh, M.J.2
  • 6
    • 0018673838 scopus 로고
    • Inhibition of anion permeability by amphiphilic compounds in human red cell: Evidence for an interaction of niflumic acid with the band 3 protein
    • 6. Cousin, J.L., Motais, R. 1979. Inhibition of anion permeability by amphiphilic compounds in human red cell: evidence for an interaction of niflumic acid with the band 3 protein. J. Membrane Biol. 46:125-153
    • (1979) J. Membrane Biol. , vol.46 , pp. 125-153
    • Cousin, J.L.1    Motais, R.2
  • 10
    • 0032032394 scopus 로고    scopus 로고
    • Nonspecificity of chloride channel blockers in rat cerebral arteries: Block of the L-type calcium channel
    • 10. Doughty, J.M., Miller, A.L., Langton, P.D. 1998. Nonspecificity of chloride channel blockers in rat cerebral arteries: block of the L-type calcium channel. J. Physiol. 507:433-439
    • (1998) J. Physiol. , vol.507 , pp. 433-439
    • Doughty, J.M.1    Miller, A.L.2    Langton, P.D.3
  • 13
    • 0020000227 scopus 로고
    • Sodium and calcium channels in bovine chromaffin cells
    • 13. Fenwick, E.M., Marty, A., Neher, E. 1982. Sodium and calcium channels in bovine chromaffin cells. J. Physiol. 331:599-635
    • (1982) J. Physiol. , vol.331 , pp. 599-635
    • Fenwick, E.M.1    Marty, A.2    Neher, E.3
  • 14
    • 0016227738 scopus 로고
    • Drugs which inhibit prostaglandin biosynthesis
    • 14. Flower, R.J. 1974. Drugs which inhibit prostaglandin biosynthesis. Pharmacol. Rev. 26:33-67
    • (1974) Pharmacol. Rev. , vol.26 , pp. 33-67
    • Flower, R.J.1
  • 15
    • 0027938084 scopus 로고    scopus 로고
    • Regulation of CFTR channel gating
    • 15. Gadsby, D.C., Nairn, A.C. 1997. Regulation of CFTR channel gating. Trends Biochem. Sci. 19:512-518
    • (1997) Trends Biochem. Sci. , vol.19 , pp. 512-518
    • Gadsby, D.C.1    Nairn, A.C.2
  • 16
    • 0025372566 scopus 로고
    • Flufenamic acid, mefenamic acid and niflumic acid inhibit single nonselective cation channels in the rat exocrine pancreas
    • 16. Gögelein, H., Dahlem, D., Englert, H.C., Lang, H.J. 1990. Flufenamic acid, mefenamic acid and niflumic acid inhibit single nonselective cation channels in the rat exocrine pancreas. FEBS Lett. 268:79-82
    • (1990) FEBS Lett. , vol.268 , pp. 79-82
    • Gögelein, H.1    Dahlem, D.2    Englert, H.C.3    Lang, H.J.4
  • 17
    • 0025670614 scopus 로고
    • Chloride channel blockers
    • 17. Greger, R. 1990. Chloride channel blockers. Methods Enzymol. 191:793-810
    • (1990) Methods Enzymol. , vol.191 , pp. 793-810
    • Greger, R.1
  • 18
    • 0025298982 scopus 로고
    • Inhibition of an outwardly rectifying anion channel by HEPES and related buffers
    • 18. Hanrahan, J.W., Tabcharani, J.A. 1990. Inhibition of an outwardly rectifying anion channel by HEPES and related buffers. J. Membrane Biol 116:65-77
    • (1990) J. Membrane Biol , vol.116 , pp. 65-77
    • Hanrahan, J.W.1    Tabcharani, J.A.2
  • 19
    • 0025755640 scopus 로고
    • Antagonists of epithelial chloride channels inhibit cAMP synthesis
    • 19. Heisler, S. 1991. Antagonists of epithelial chloride channels inhibit cAMP synthesis. Can. J. Physiol. Pharmacol. 69:501-506
    • (1991) Can. J. Physiol. Pharmacol. , vol.69 , pp. 501-506
    • Heisler, S.1
  • 20
  • 22
    • 0030668944 scopus 로고    scopus 로고
    • Block by MOPS reveals a conformational change in the CFTR pore produced by ATP hydrolysis
    • 22. Ishihara, H., Welsh, M.J. 1997. Block by MOPS reveals a conformational change in the CFTR pore produced by ATP hydrolysis. Am. J. Physiol. 273:C1278-C1289
    • (1997) Am. J. Physiol. , vol.273
    • Ishihara, H.1    Welsh, M.J.2
  • 24
    • 0026548697 scopus 로고
    • Chloride transport blockers prevent N-methyl-D-aspartate receptor-channel complex activation
    • 24. Lerma, J., Martín del Río, R. 1992. Chloride transport blockers prevent N-methyl-D-aspartate receptor-channel complex activation. Mol. Pharmacol. 41:217-222
    • (1992) Mol. Pharmacol. , vol.41 , pp. 217-222
    • Lerma, J.1    Martín Del Río, R.2
  • 25
    • 0025982125 scopus 로고
    • Strategies for studying permeation at voltagegated ion channels
    • 25. Lester, H.A. 1991. Strategies for studying permeation at voltagegated ion channels. Annu. Rev. Physiol. 53:477-496
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 477-496
    • Lester, H.A.1
  • 26
    • 0029861859 scopus 로고    scopus 로고
    • - channels expressed in a mammalian cell line, and its regulation by a critical pore residue
    • - channels expressed in a mammalian cell line, and its regulation by a critical pore residue J. Physiol. 496:687-693
    • (1996) J. Physiol. , vol.496 , pp. 687-693
    • Linsdell, P.1    Hanrahan, J.W.2
  • 27
    • 0030886246 scopus 로고    scopus 로고
    • Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel
    • 27. Linsdell, P., Tabcharani, J.A., Hanrahan, J.W. 1997. Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 110:365-377
    • (1997) J. Gen. Physiol. , vol.110 , pp. 365-377
    • Linsdell, P.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 30
    • 0030836234 scopus 로고    scopus 로고
    • Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel
    • 30. Ma, J., Zhao, J., Drumm, M.L., Xie, J., Davis, P.B. 1997. Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Biol. Chem. 272:28133-28141
    • (1997) J. Biol. Chem. , vol.272 , pp. 28133-28141
    • Ma, J.1    Zhao, J.2    Drumm, M.L.3    Xie, J.4    Davis, P.B.5
  • 31
    • 0024426645 scopus 로고
    • Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor
    • 31. MacKinnon, R., Miller, C. 1989. Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor. Science 245:1382-1385
    • (1989) Science , vol.245 , pp. 1382-1385
    • MacKinnon, R.1    Miller, C.2
  • 34
    • 4243284674 scopus 로고    scopus 로고
    • Residues near the extracellular end of TM6 and TM12 in CFTR contribute to anion selectivity
    • Abst.
    • 34. McCarty, N.A., Zhang, Z.-R. 1998. Residues near the extracellular end of TM6 and TM12 in CFTR contribute to anion selectivity. Biophys. J. 74:A395 (Abst.)
    • (1998) Biophys. J. , vol.74
    • McCarty, N.A.1    Zhang, Z.-R.2
  • 35
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open-channel block
    • 35. McDonough, S., Davidson, N., Lester, H.A., McCarty, N.A. 1994. Novel pore-lining residues in CFTR that govern permeation and open-channel block. Neuron 13:623-634
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    McCarty, N.A.4
  • 36
    • 0026609888 scopus 로고
    • 2+ release by flufenamic acid and other blockers of the non-selective cation channel
    • 2+ release by flufenamic acid and other blockers of the non-selective cation channel. FEBS Lett. 296:245-248
    • (1992) FEBS Lett. , vol.296 , pp. 245-248
    • Poronnik, P.1    Ward, M.C.2    Cook, D.I.3
  • 37
    • 0026782578 scopus 로고
    • Incubation with horse serum increases viability and decreases background neurotransmitter uptake in Xenopus oocytes
    • 37. Quick, M.W., Naeve, J., Davidson, N., Lester, H.A. 1992. Incubation with horse serum increases viability and decreases background neurotransmitter uptake in Xenopus oocytes. BioTechniques 13:358-362
    • (1992) BioTechniques , vol.13 , pp. 358-362
    • Quick, M.W.1    Naeve, J.2    Davidson, N.3    Lester, H.A.4
  • 38
    • 0025155528 scopus 로고
    • Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells
    • 38. Rich, D.P., Anderson, M.P., Gregory, R.J., Cheng, S.H., Paul, S., Jefferson, D.M., McCann, J.D., Klinger, K.W., Smith, A.E., Welsh, M.J. 1990. Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells. Nature 347:358-363
    • (1990) Nature , vol.347 , pp. 358-363
    • Rich, D.P.1    Anderson, M.P.2    Gregory, R.J.3    Cheng, S.H.4    Paul, S.5    Jefferson, D.M.6    McCann, J.D.7    Klinger, K.W.8    Smith, A.E.9    Welsh, M.J.10
  • 42
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity
    • 42. Seibert, F.S., Linsdell, P., Loo, T.P., Hanrahan, J.W., Clarke, D.M., Riordan, J.R. 1996. Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity. J. Biol. Chem. 271:15139-15145
    • (1996) J. Biol. Chem. , vol.271 , pp. 15139-15145
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.P.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordan, J.R.6
  • 43
    • 0029910820 scopus 로고    scopus 로고
    • Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity
    • 43. Seibert, F.S., Linsdell, P., Loo, T.W., Hanrahan, J.W., Riordan, J.R., Clarke, D.M. 1996. Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity. J. Biol. Chem. 271:27493-27499
    • (1996) J. Biol. Chem. , vol.271 , pp. 27493-27499
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Riordan, J.R.5    Clarke, D.M.6
  • 45
    • 0026759418 scopus 로고
    • + channel regulators on cystic fibrosis transmembrane conductance regulator chloride currents
    • + channel regulators on cystic fibrosis transmembrane conductance regulator chloride currents. J. Gen. Physiol. 100:573-592
    • (1992) J. Gen. Physiol. , vol.100 , pp. 573-592
    • Sheppard, D.N.1    Welsh, M.J.2
  • 46
    • 0032912589 scopus 로고    scopus 로고
    • Structure and function of the CFTR chloride channel
    • 46. Sheppard, D.N., Welsh, M.J. 1999. Structure and function of the CFTR chloride channel. Physiol. Rev. 79:S23-S45
    • (1999) Physiol. Rev. , vol.79
    • Sheppard, D.N.1    Welsh, M.J.2
  • 47
    • 0027364318 scopus 로고
    • Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator
    • 47. Smit, L.S., Wilkinson, D.J., Mansoura, M.K., Collins, F.S., Dawson, D.C. 1993. Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator. Proc. Natl. Acad. Sci. USA 90:9963-9967
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9963-9967
    • Smit, L.S.1    Wilkinson, D.J.2    Mansoura, M.K.3    Collins, F.S.4    Dawson, D.C.5
  • 50
    • 0030964656 scopus 로고    scopus 로고
    • Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels
    • 50. Tabcharani, J.A., Linsdell, P., Hanrahan, J.W. 1997. Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels. J. Gen. Physiol. 110:341-351
    • (1997) J. Gen. Physiol. , vol.110 , pp. 341-351
    • Tabcharani, J.A.1    Linsdell, P.2    Hanrahan, J.W.3
  • 51
    • 0015993232 scopus 로고
    • Structure-activity relationships of fenamic acids
    • 51. Terada, H., Muraoka, S., Fujita, T. 1974. Structure-activity relationships of fenamic acids. J. Med. Chem. 17:330-334
    • (1974) J. Med. Chem. , vol.17 , pp. 330-334
    • Terada, H.1    Muraoka, S.2    Fujita, T.3
  • 52
    • 0025766116 scopus 로고
    • Different types of blockers of the intermediate-conductance outwardly rectifying chloride channel in epithelia
    • 52. Tilmann, M., Kunzelmann, K., Fröbe, U., Cabantchik, I., Lang, H.J., Englert, H.C., Greger, R. 1991. Different types of blockers of the intermediate-conductance outwardly rectifying chloride channel in epithelia. Pfluegers. Arch. 418:556-563
    • (1991) Pfluegers. Arch. , vol.418 , pp. 556-563
    • Tilmann, M.1    Kunzelmann, K.2    Fröbe, U.3    Cabantchik, I.4    Lang, H.J.5    Englert, H.C.6    Greger, R.7
  • 56
    • 0032986798 scopus 로고    scopus 로고
    • Structural and ionic determinants of 5-nitro-2-(3-phenylpropylamino)-benzoic acid block of the CFTR chloride channel
    • 56. Walsh, K.B., Long, K.J., Shen, X. 1999. Structural and ionic determinants of 5-nitro-2-(3-phenylpropylamino)-benzoic acid block of the CFTR chloride channel. Br. J. Pharmacol. 127:369-376
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 369-376
    • Walsh, K.B.1    Long, K.J.2    Shen, X.3
  • 57
    • 0030222239 scopus 로고    scopus 로고
    • Effect of chloride channel blockers on the cardiac CFTR chloride and L-type calcium currents
    • 57. Walsh, K.B., Wang, C. 1996. Effect of chloride channel blockers on the cardiac CFTR chloride and L-type calcium currents. Cardiovasc. Res. 32:391-399
    • (1996) Cardiovasc. Res. , vol.32 , pp. 391-399
    • Walsh, K.B.1    Wang, C.2
  • 58
    • 0031977182 scopus 로고    scopus 로고
    • Arylaminobenzoate block of the cardiac cyclic AMP-dependent chloride current
    • 58. Walsh, K.B., Wang, C. 1998. Arylaminobenzoate block of the cardiac cyclic AMP-dependent chloride current. Mol. Pharmacol. 53:539-546
    • (1998) Mol. Pharmacol. , vol.53 , pp. 539-546
    • Walsh, K.B.1    Wang, C.2
  • 59
    • 0031881489 scopus 로고    scopus 로고
    • Actions of genistein on cystic fibrosis transmembrane conductance regulator channel gating: Evidence for two binding sites with opposite effects
    • 59. Wang, F., Zeltwanger, S., Yang, I.C., Nairn, A.C., Hwang, T.-C. 1998. Actions of genistein on cystic fibrosis transmembrane conductance regulator channel gating: Evidence for two binding sites with opposite effects. J. Gen. Physiol. 111:477-490
    • (1998) J. Gen. Physiol. , vol.111 , pp. 477-490
    • Wang, F.1    Zeltwanger, S.2    Yang, I.C.3    Nairn, A.C.4    Hwang, T.-C.5
  • 62
    • 0030045751 scopus 로고    scopus 로고
    • CFTR: The nucleotide binding folds regulate the accessibility and stability of the activated state
    • 62. Wilkinson, D.J., Mansoura, M.K., Watson, P.Y., Smit, L.S., Collins, F.S., Dawson, D.C. 1996. CFTR: the nucleotide binding folds regulate the accessibility and stability of the activated state. J. Gen. Physiol. 107:103-119
    • (1996) J. Gen. Physiol. , vol.107 , pp. 103-119
    • Wilkinson, D.J.1    Mansoura, M.K.2    Watson, P.Y.3    Smit, L.S.4    Lins, F.S.5    Dawson, D.C.6
  • 63
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • 63. Woodhull, A.M. 1973. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61:687-708
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 65
    • 0029770050 scopus 로고    scopus 로고
    • Human epithelial cystic fibrosis transmembrane conductance regulator without exon 5 maintains partial chloride channel function in intracellular membranes
    • 65. Xie, J., Drumm, M.L., Zhao, J., Ma, J., Davis, P.B. 1996. Human epithelial cystic fibrosis transmembrane conductance regulator without exon 5 maintains partial chloride channel function in intracellular membranes. Biophys. J. 71:3148-3156
    • (1996) Biophys. J. , vol.71 , pp. 3148-3156
    • Xie, J.1    Drumm, M.L.2    Zhao, J.3    Ma, J.4    Davis, P.B.5
  • 67
    • 0032954806 scopus 로고    scopus 로고
    • Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis: Quantitative analysis of a cyclic gating scheme
    • 67. Zeltwanger, S., Wang, F., Wang, G.-T., Gillis, K.D., Hwang, T.-C. 1999. Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis: Quantitative analysis of a cyclic gating scheme. J. Gen. Physiol. 113:541-554
    • (1999) J. Gen. Physiol. , vol.113 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.-T.3    Gillis, K.D.4    Hwang, T.-C.5
  • 68
    • 0013646972 scopus 로고    scopus 로고
    • A comparison of probes for structure/function experiments in CFTR
    • Abstr.
    • 68. Zhang, Z.-R., McCarty, N.A. 1998. A comparison of probes for structure/function experiments in CFTR. Ped. Pulmonol. 17:224-225 (Abstr.)
    • (1998) Ped. Pulmonol. , vol.17 , pp. 224-225
    • Zhang, Z.-R.1    McCarty, N.A.2
  • 69
    • 0013648825 scopus 로고    scopus 로고
    • Interaction between permeation and gating in a putative pore-domain mutant in CFTR
    • in press
    • 69. Zhang, Z.-R., McDonough, S.I., McCarty, N.A. 2000. Interaction between permeation and gating in a putative pore-domain mutant in CFTR. Biophys. J. (in press)
    • (2000) Biophys. J.
    • Zhang, Z.-R.1    McDonough, S.I.2    McCarty, N.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.