메뉴 건너뛰기




Volumn 275, Issue 4 44-4, 1998, Pages

Cystic fibrosis transmembrane conductance regulator activation by cAMP- independent mechanisms

Author keywords

3 isobutyl 1 methylxanthine; Adenosine 3',5' cyclic monophosphate; Genistein; In vivo phosphorylation

Indexed keywords

1 (5 CHLORO 2 HYDROXYPHENYL) 5 TRIFLUOROMETHYL 2 BENZIMIDAZOLONE; 8 CYCLOPENTYL 1,3 DIPROPYLXANTHINE; CALYCULIN A; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; GENISTEIN; ISOBUTYLMETHYLXANTHINE; MILRINONE; PHOSPHATASE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0031723518     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.275.4.c958     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 0025931429 scopus 로고
    • Nucleoside triphosphates are required to open the CFTR chloride channel
    • Anderson, M. P., H. A. Berger, D. R. Rich, R. J. Gregory, A. E. Smith, and M. J. Welsh. Nucleoside triphosphates are required to open the CFTR chloride channel. Cell 67: 775-784, 1991.
    • (1991) Cell , vol.67 , pp. 775-784
    • Anderson, M.P.1    Berger, H.A.2    Rich, D.R.3    Gregory, R.J.4    Smith, A.E.5    Welsh, M.J.6
  • 2
    • 0032489513 scopus 로고    scopus 로고
    • Direct activation of cystic fibrosis transmembrane conductance regulator channels by 8-cyclopentyl-1,3-dipropylxanthine (CPX) and 1,3-diallyl-8-cyclohexylxanthine (DAX)
    • Arispe, N., J. Ma, K. A. Jacobson, and H. B. Pollard. Direct activation of cystic fibrosis transmembrane conductance regulator channels by 8-cyclopentyl-1,3-dipropylxanthine (CPX) and 1,3-diallyl-8-cyclohexylxanthine (DAX). J. Biol. Chem. 273: 5727-5734, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5727-5734
    • Arispe, N.1    Ma, J.2    Jacobson, K.A.3    Pollard, H.B.4
  • 4
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng, S. H., D. P. Rich, J. Marshall, R. J. Gregory, M. J. Welsh, and A. E. Smith. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 66: 1027-1036, 1991.
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 5
    • 0030943895 scopus 로고    scopus 로고
    • 8-Cyclopentyl-1,3-diproplyxanthine and other xanthines differentially bind to the first nucleotide binding fold (NBF-1) domains of the cystic fibrosis transmembrane conductance regulator
    • Cohen, B. E., G. Lee, K. A. Jacobson, Y.-C. Kim, Z. Huang, E. J. Sorscher, and H. B. Pollard. 8-Cyclopentyl-1,3-diproplyxanthine and other xanthines differentially bind to the first nucleotide binding fold (NBF-1) domains of the cystic fibrosis transmembrane conductance regulator. Biochemistry 36: 6455-6461, 1997.
    • (1997) Biochemistry , vol.36 , pp. 6455-6461
    • Cohen, B.E.1    Lee, G.2    Jacobson, K.A.3    Kim, Y.-C.4    Huang, Z.5    Sorscher, E.J.6    Pollard, H.B.7
  • 6
    • 0026620450 scopus 로고
    • 8-(4-Chlorophenyl)thio-cyclic AMP is a potent inhibitor of the cyclic GMP-specific phosphodiesterase (PDE VA)
    • Connolly, B. J., P. B. Willits, B. H. Warrington, and K. J. Murray. 8-(4-Chlorophenyl)thio-cyclic AMP is a potent inhibitor of the cyclic GMP-specific phosphodiesterase (PDE VA). Biochem. Pharmacol. 44: 2303-2306, 1992.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 2303-2306
    • Connolly, B.J.1    Willits, P.B.2    Warrington, B.H.3    Murray, K.J.4
  • 8
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G. M., M. P. Anderson, J. F. Amara, J. Marshall, A. E. Smith, and M. J. Welsh. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358: 761-764, 1992.
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 12
    • 0027938084 scopus 로고
    • Regulation of CFTR channel gating
    • Gadsby, D. C., and A. C. Nairn. Regulation of CFTR channel gating. Trends Biochem. Sci. 19: 513-518, 1994.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 513-518
    • Gadsby, D.C.1    Nairn, A.C.2
  • 13
    • 0028247368 scopus 로고
    • The substituted benzimidazolone NS004 is an opener of the cystic fibrosis chloride channel
    • Gribkoff, V., G. Champigny, P. Barbry, S. Dworetzky, N. Meanwell, and M. Lazdunski. The substituted benzimidazolone NS004 is an opener of the cystic fibrosis chloride channel. J. Biol. Chem. 269: 10983-10986, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10983-10986
    • Gribkoff, V.1    Champigny, G.2    Barbry, P.3    Dworetzky, S.4    Meanwell, N.5    Lazdunski, M.6
  • 16
    • 0030773897 scopus 로고    scopus 로고
    • Potentiation of ΔF508 channel function by genistein binding to CFTR
    • Cell Physiol. 42
    • Hwang, T.-C., F. Wang, S. Zeltwanger, I. C.-H. Yang, and W. W. Reenstra. Potentiation of ΔF508 channel function by genistein binding to CFTR. Am. J. Physiol. 273 (Cell Physiol. 42): C988-C998, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Hwang, T.-C.1    Wang, F.2    Zeltwanger, S.3    Yang, I.C.-H.4    Reenstra, W.W.5
  • 17
    • 0028928015 scopus 로고
    • cAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein
    • Cell Physiol. 37
    • Illek, B., H. Fischer, G. F. Santos, J. H. Widdicombe, T. E. Machen, and W. W. Reenstra. cAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein. Am. J. Physiol. 268 (Cell Physiol. 37): C886-C893, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Illek, B.1    Fischer, H.2    Santos, G.F.3    Widdicombe, J.H.4    Machen, T.E.5    Reenstra, W.W.6
  • 18
    • 0029665963 scopus 로고    scopus 로고
    • Activation of endogenous ΔF508 cystic fibrosis transmembrane conductance regulator by phosphodiesterase inhibition
    • Kelley, T. J., L. Al-Nakkash, C. U. Cotton, and M. L. Drumm. Activation of endogenous ΔF508 cystic fibrosis transmembrane conductance regulator by phosphodiesterase inhibition. J. Clin. Invest. 98: 513-520, 1996.
    • (1996) J. Clin. Invest. , vol.98 , pp. 513-520
    • Kelley, T.J.1    Al-Nakkash, L.2    Cotton, C.U.3    Drumm, M.L.4
  • 19
    • 0029556721 scopus 로고
    • CFTR-mediated chloride permeability is regulated by type III phosphodiesterases in airway epithelial cells
    • Kelley, T. J., L. Al-Nakkash, and M. L. Drumm. CFTR-mediated chloride permeability is regulated by type III phosphodiesterases in airway epithelial cells. Am. J. Respir. Cell. Mol. Biol. 13: 657-664, 1995.
    • (1995) Am. J. Respir. Cell. Mol. Biol. , vol.13 , pp. 657-664
    • Kelley, T.J.1    Al-Nakkash, L.2    Drumm, M.L.3
  • 21
    • 0028821773 scopus 로고
    • Tyrosine phosphorylation is a novel pathway for regulation of chloride secretion in shark rectal gland
    • Renal Fluid Electrolyte Physiol. 38
    • Lehrich, R. W., and J. N. Forrest, Jr. Tyrosine phosphorylation is a novel pathway for regulation of chloride secretion in shark rectal gland. Am. J. Physiol. 269 (Renal Fluid Electrolyte Physiol. 38): F594-F600, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Lehrich, R.W.1    Forrest Jr., J.N.2
  • 22
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • Picciotto, M. R., J. A. Cohn, G. Bertuzzi, P. Greengard, and A, C. Nairn. Phosphorylation of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 267: 12742-12752, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12742-12752
    • Picciotto, M.R.1    Cohn, J.A.2    Bertuzzi, G.3    Greengard, P.4    Nairn, A.C.5
  • 23
    • 0029759111 scopus 로고    scopus 로고
    • CFTR chloride channel activation by genistein: The role of serine/threonine protein phosphatases
    • Cell Physiol. 40
    • Reenstra, W. W., K. Yurko-Mauro, A. Dam, S. Raman, and S. Shorten. CFTR chloride channel activation by genistein: the role of serine/threonine protein phosphatases. Am. J. Physiol. 271 (Cell Physiol. 40): C650-C657, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Reenstra, W.W.1    Yurko-Mauro, K.2    Dam, A.3    Raman, S.4    Shorten, S.5
  • 25
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • Schweibert, E. M., M. E. Eagan, T. H. Hwang, S. B. Fulmer, S. S. Allen, G. R. Cutting, and W. B. Guggino. CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell 81: 1063-1073, 1995.
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schweibert, E.M.1    Eagan, M.E.2    Hwang, T.H.3    Fulmer, S.B.4    Allen, S.S.5    Cutting, G.R.6    Guggino, W.B.7
  • 28
    • 0025110836 scopus 로고
    • A simple assay for agonist-regulated Cl and K conductances in salt-secreting epithelial cells
    • Cell Physiol. 28
    • Venglarik, C. J., R. J. Bridges, and R. A. Frizzell. A simple assay for agonist-regulated Cl and K conductances in salt-secreting epithelial cells. Am. J. Physiol. 259 (Cell Physiol. 28): C358-C364, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Venglarik, C.J.1    Bridges, R.J.2    Frizzell, R.A.3
  • 29
    • 0031881489 scopus 로고    scopus 로고
    • Actions of genistein on cystic fibrosis transmembrane conductance regulator channel gating: Evidence for two binding sites with opposite effects
    • Wang, F., S. Zeltwanger, I. C.-H. Yang, A. C. Nairn, and T.-C. Hwang. 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.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 477-490
    • Wang, F.1    Zeltwanger, S.2    Yang, I.C.-H.3    Nairn, A.C.4    Hwang, T.-C.5
  • 31
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • Welsh, M. J., and A. E. Smith. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73: 1251-1254, 1993.
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 33
    • 0021077241 scopus 로고
    • Complex effects of inhibitors on cyclic GMP-stimulated cyclic nucleotide phosphodiesterase
    • Yamamoto, T., S. Yamamoto, J. C. Osborne, V. C. Manganiello, M. Vaughan, and H. Hikada. Complex effects of inhibitors on cyclic GMP-stimulated cyclic nucleotide phosphodiesterase. J. Biol. Chem. 258: 14173-14177, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14173-14177
    • Yamamoto, T.1    Yamamoto, S.2    Osborne, J.C.3    Manganiello, V.C.4    Vaughan, M.5    Hikada, H.6
  • 34
    • 0031028588 scopus 로고    scopus 로고
    • Modulation of CFTR chloride channels by calyculin a and genistein
    • Cell Physiol. 41
    • Yang, I. C.-H., T.-H. Cheng, F. Wang, E. M. Price, and T.-C. Hwang. Modulation of CFTR chloride channels by calyculin A and genistein. Am. J. Physiol. 272 (Cell Physiol. 41): C142-C155, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Yang, I.C.-H.1    Cheng, T.-H.2    Wang, F.3    Price, E.M.4    Hwang, T.-C.5
  • 35
    • 0032161340 scopus 로고    scopus 로고
    • 2aα stimulates CFTR activity by PKA- and PKC-dependent phosphorylation
    • Cell Physiol. 44
    • 2aα stimulates CFTR activity by PKA- and PKC-dependent phosphorylation. Am. J. Physiol 275 (Cell Physiol. 44): C653-C660, 1998.
    • (1998) Am. J. Physiol , vol.275
    • Yurko-Mauro, K.A.1    Reenstra, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.