메뉴 건너뛰기




Volumn 51, Issue 6, 1997, Pages 999-1006

Role of conserved histidines in catalytic activity and inhibitor binding of human recombinant phosphodiesterase 4A

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; HISTIDINE; PHOSPHODIESTERASE INHIBITOR; PHOSPHODIESTERASE IV; PICLAMILAST; RECOMBINANT PROTEIN; ROLIPRAM;

EID: 0030981608     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.51.6.999     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0025215525 scopus 로고
    • Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors
    • Beavo, J. A., and D. H. Reifsnyder. Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors. Trends Pharmacol. Sci. 11:150-155 (1990).
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 150-155
    • Beavo, J.A.1    Reifsnyder, D.H.2
  • 2
    • 0026844552 scopus 로고
    • Regulation and function of cyclic nucleotides
    • Bentley, J. K., and J. A. Beavo. Regulation and function of cyclic nucleotides. Curr. Opin. Cell Biol. 4:233-240 (1992).
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 233-240
    • Bentley, J.K.1    Beavo, J.A.2
  • 3
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • Beavo, J. A., Conti, M., and R. J. Heaslip. Multiple cyclic nucleotide phosphodiesterases. Mol. Pharmacol. 46:399-405 (1994).
    • (1994) Mol. Pharmacol. , vol.46 , pp. 399-405
    • Beavo, J.A.1    Conti, M.2    Heaslip, R.J.3
  • 5
    • 0027454556 scopus 로고
    • A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs
    • Bolger, G., T. Michaeli, T. Martins, T. St. John, B. Steiner, L. Rodgers, M. Riggs, M. Wigler, and K. Ferguson. A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol. Cell. Biol. 13:6558-6571 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6558-6571
    • Bolger, G.1    Michaeli, T.2    Martins, T.3    St. John, T.4    Steiner, B.5    Rodgers, L.6    Riggs, M.7    Wigler, M.8    Ferguson, K.9
  • 6
    • 0024405251 scopus 로고
    • Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: Evidence for a family of genes
    • Swinnen, J. V., D. R. Josef, and M. Conti. Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: evidence for a family of genes. Proc. Natl. Acad. Sci. USA 86:5325-5329 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5325-5329
    • Swinnen, J.V.1    Josef, D.R.2    Conti, M.3
  • 9
    • 0027339578 scopus 로고
    • m, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain: Cloning and expression of cDNA, biochemical characterization of recombinant protein and tissue distribution of mRNA
    • m, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain: cloning and expression of cDNA, biochemical characterization of recombinant protein and tissue distribution of mRNA. J. Biol. Chem. 268:6470-6476 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 6470-6476
    • McLaughlin, M.M.1    Cieslinski, L.B.2    Burman, M.3    Torphy, T.J.4    Livi, G.P.5
  • 10
    • 0027244894 scopus 로고
    • The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family
    • Obernolte, R., S. Bhakta, R. Alvarez, C. Bach, P. Zuppan, M. Mulkins, K. Jarnagin, and E. R. Shelton. The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family. Gene 129:239-247 (1993).
    • (1993) Gene , vol.129 , pp. 239-247
    • Obernolte, R.1    Bhakta, S.2    Alvarez, R.3    Bach, C.4    Zuppan, P.5    Mulkins, M.6    Jarnagin, K.7    Shelton, E.R.8
  • 11
    • 0028033778 scopus 로고
    • Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases
    • Bolger, G. B., L. Rodgers, and M. Riggs. Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases. Gene 149:237-244 (1994).
    • (1994) Gene , vol.149 , pp. 237-244
    • Bolger, G.B.1    Rodgers, L.2    Riggs, M.3
  • 12
    • 0028140251 scopus 로고
    • Structure of two rat genes coding for closely related rolipram-sensitive cAMP phosphodiesterases
    • Monaco, L., E. Vicini, and M. Conti. Structure of two rat genes coding for closely related rolipram-sensitive cAMP phosphodiesterases. J. Biol. Chem. 269:347-357 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 347-357
    • Monaco, L.1    Vicini, E.2    Conti, M.3
  • 14
    • 0025868447 scopus 로고
    • Phosphodiesterase inhibitors: New opportunities for the treatment of asthma
    • Torphy, T. J., and B. J. Undem. Phosphodiesterase inhibitors: new opportunities for the treatment of asthma. Thorax 46:512-524 (1991).
    • (1991) Thorax , vol.46 , pp. 512-524
    • Torphy, T.J.1    Undem, B.J.2
  • 15
    • 0028228233 scopus 로고
    • Selective type IV phosphodiesterase inhibitors as antiasthmatic agents: The syntheses and biological activities of 3-(cyclopentyloxy)-4 methoxybenzamides and analogues
    • Ashton, M. J., D. C. Cook, G. Fenton, J.-A. Karlsson, M. N. Palfreyman, D. Raeburn, A. J. Ratcliffe, J. E. Souness, S. Thurairatnam, and N. Vicker. Selective type IV phosphodiesterase inhibitors as antiasthmatic agents: the syntheses and biological activities of 3-(cyclopentyloxy)-4 methoxybenzamides and analogues. J. Med. Chem. 37:1696-1703 (1994).
    • (1994) J. Med. Chem. , vol.37 , pp. 1696-1703
    • Ashton, M.J.1    Cook, D.C.2    Fenton, G.3    Karlsson, J.-A.4    Palfreyman, M.N.5    Raeburn, D.6    Ratcliffe, A.J.7    Souness, J.E.8    Thurairatnam, S.9    Vicker, N.10
  • 17
    • 0029036931 scopus 로고
    • Suppression of eosinophil function by RP 73401, a potent and selective inhibitor of cyclic AMP-specific phosphodiesterase: Comparison with rolipram
    • Souness, J. E., C. Maslen, S. Webber, M. Foster, D. Raeburn, M. N. Palfreyman, M. J. Ashton, and J.-A. Karlsson. Suppression of eosinophil function by RP 73401, a potent and selective inhibitor of cyclic AMP-specific phosphodiesterase: comparison with rolipram. Br. J. Pharmacol. 115:39-46 (1995).
    • (1995) Br. J. Pharmacol. , vol.115 , pp. 39-46
    • Souness, J.E.1    Maslen, C.2    Webber, S.3    Foster, M.4    Raeburn, D.5    Palfreyman, M.N.6    Ashton, M.J.7    Karlsson, J.-A.8
  • 18
    • 0026551071 scopus 로고
    • Effects of solubilization and vanadate/glutathione complex on inhibitor potencies against eosinophil cyclic AMP-specific phosphodiesterase
    • Souness, J. E., C. Maslen, and L. C. Scott. Effects of solubilization and vanadate/glutathione complex on inhibitor potencies against eosinophil cyclic AMP-specific phosphodiesterase. FEBS Lett. 302:181-184 (1992).
    • (1992) FEBS Lett. , vol.302 , pp. 181-184
    • Souness, J.E.1    Maslen, C.2    Scott, L.C.3
  • 19
    • 0029979738 scopus 로고    scopus 로고
    • Mapping the functional domains of human recombinant phosphodiesterase 4A: Structural requirements for catalytic activity and rolipram binding
    • Jacobitz, S., M. M. McLaughlin, G. P. Livi, M. Burman, and T. J. Torphy. Mapping the functional domains of human recombinant phosphodiesterase 4A: structural requirements for catalytic activity and rolipram binding. Mol. Pharmacol. 50:891-899 (1996).
    • (1996) Mol. Pharmacol. , vol.50 , pp. 891-899
    • Jacobitz, S.1    McLaughlin, M.M.2    Livi, G.P.3    Burman, M.4    Torphy, T.J.5
  • 20
    • 0022459284 scopus 로고
    • Stereospecific binding of the antidepressant rolipram to brain protein structures
    • Schneider, H. H., R. Schmiechen, M. Brezenski, and J. Seidler. Stereospecific binding of the antidepressant rolipram to brain protein structures. Eur. J. Pharmacol. 127:105-115 (1986).
    • (1986) Eur. J. Pharmacol. , vol.127 , pp. 105-115
    • Schneider, H.H.1    Schmiechen, R.2    Brezenski, M.3    Seidler, J.4
  • 21
    • 0026528829 scopus 로고
    • Coexpression of human cAMP-specific phosphodiesterase activity and high affinity rolipram binding in yeast
    • Torphy, T. J., J. M. Stadel, M. Burman, L. B. Cieslinski, M. M. McLaughlin, J. R. White, and G. P. Livi. Coexpression of human cAMP-specific phosphodiesterase activity and high affinity rolipram binding in yeast. J. Biol. Chem. 267:1798-1804 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 1798-1804
    • Torphy, T.J.1    Stadel, J.M.2    Burman, M.3    Cieslinski, L.B.4    McLaughlin, M.M.5    White, J.R.6    Livi, G.P.7
  • 22
    • 0027138677 scopus 로고
    • Use of a yeast expression system for the isolation and analysis of drug-resistant mutants of a mammalian phosphodiesterase
    • Pillai, R., K. Kytle, A. Reyes, and J. Colicelli. Use of a yeast expression system for the isolation and analysis of drug-resistant mutants of a mammalian phosphodiesterase. Proc. Natl. Acad. Sci. USA 90:11970-11974 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11970-11974
    • Pillai, R.1    Kytle, K.2    Reyes, A.3    Colicelli, J.4
  • 23
    • 0025967117 scopus 로고
    • Expression of human recombinant cAMP phosphodiesterase isozyme IV reverses growth arrest phenotypes in phosphodiesterase-deficient yeast
    • T. J.
    • McHale, M. M., L. B. Cieslinski, W.-K. Eng, R. K. Johnson, T. J. Torphy, T. J., and G. P. Livi. Expression of human recombinant cAMP phosphodiesterase isozyme IV reverses growth arrest phenotypes in phosphodiesterase-deficient yeast. Mol. Pharmacol. 39:109-113 (1991).
    • (1991) Mol. Pharmacol. , vol.39 , pp. 109-113
    • McHale, M.M.1    Cieslinski, L.B.2    Eng, W.-K.3    Johnson, R.K.4    Torphy, T.J.5    Livi, G.P.6
  • 24
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction
    • Mullis, K. B., and F. A. Faloona. Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol. 155:335-350 (1987).
    • (1987) Methods Enzymol. , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 27
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168 (1983).
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 28
    • 0025092063 scopus 로고
    • Characterization and selective inhibition of cyclic nucleotide phosphodiesterase isozymes in canine tracheal smooth muscle
    • Torphy, T. J., and L. B. Cieslinski. Characterization and selective inhibition of cyclic nucleotide phosphodiesterase isozymes in canine tracheal smooth muscle. Mol. Pharmacol. 37:206-214 (1990).
    • (1990) Mol. Pharmacol. , vol.37 , pp. 206-214
    • Torphy, T.J.1    Cieslinski, L.B.2
  • 29
    • 0343751890 scopus 로고
    • Phosphodiesterase isozymes in airways
    • (K. F. Chung and P. J. Barnes, eds.). Marcel Dekker Inc., New York
    • Torphy, T. J., and G. P. Livi. Phosphodiesterase isozymes in airways, in Pharmacology of the Respiratory Tract (K. F. Chung and P. J. Barnes, eds.). Marcel Dekker Inc., New York, 177-222 (1993).
    • (1993) Pharmacology of the Respiratory Tract , pp. 177-222
    • Torphy, T.J.1    Livi, G.P.2
  • 30
    • 0020505453 scopus 로고
    • Substrate specificity of cyclic nucleotide phosphodiesterase from beef heart and from Dictyostelium discoideum
    • Van Haastert, P. J. M., P. A. M. Dijkgraaf, T. M. Konijn, E. G. Abbad, G. Petridis, and B. Jastorff. Substrate specificity of cyclic nucleotide phosphodiesterase from beef heart and from Dictyostelium discoideum. Eur. J. Biochem. 131:659-666 (1983).
    • (1983) Eur. J. Biochem. , vol.131 , pp. 659-666
    • Van Haastert, P.J.M.1    Dijkgraaf, P.A.M.2    Konijn, T.M.3    Abbad, E.G.4    Petridis, G.5    Jastorff, B.6
  • 32
    • 0028923797 scopus 로고
    • Characterization of cyclic nucleotide phosphodiesterases with cyclic AMP analogs: Topology of the catalytic sites and comparison with other cyclic AMP-binding proteins
    • Butt, E., J. Beltman, D. E. Becker, G. S. Jensen, S. D. Rybalkin, B. Jastorff, and J. A. Beavo. Characterization of cyclic nucleotide phosphodiesterases with cyclic AMP analogs: topology of the catalytic sites and comparison with other cyclic AMP-binding proteins. Mol. Pharmacol. 47: 340-347 (1995).
    • (1995) Mol. Pharmacol. , vol.47 , pp. 340-347
    • Butt, E.1    Beltman, J.2    Becker, D.E.3    Jensen, G.S.4    Rybalkin, S.D.5    Jastorff, B.6    Beavo, J.A.7
  • 33
    • 0027290657 scopus 로고
    • Biochemical characteristics and cellular regulation of phosphodiesterase IV
    • Torphy, T. J., W. E. DeWolf, Jr., D. W. Green, and G. P. Livi. Biochemical characteristics and cellular regulation of phosphodiesterase IV. Agents Actions 43:51-71 (1993).
    • (1993) Agents Actions , vol.43 , pp. 51-71
    • Torphy, T.J.1    DeWolf Jr., W.E.2    Green, D.W.3    Livi, G.P.4
  • 35
    • 0025181849 scopus 로고
    • Rat homologues of the Drosophila dunce gene code for cyclic AMP phosphodiesterases sensitive to rolipram and Ro 20-1724
    • Henkel-Tigges, J., and R. L. Davis. Rat homologues of the Drosophila dunce gene code for cyclic AMP phosphodiesterases sensitive to rolipram and Ro 20-1724. Mol. Pharmacol. 37:7-10 (1990).
    • (1990) Mol. Pharmacol. , vol.37 , pp. 7-10
    • Henkel-Tigges, J.1    Davis, R.L.2
  • 36
    • 0022961581 scopus 로고
    • Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species
    • Charbonneau, H., N. Beier, K. A. Walsh, and J. A. Beavo. Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species. Proc. Natl. Acad. Sci. USA 83:9308-9312 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9308-9312
    • Charbonneau, H.1    Beier, N.2    Walsh, K.A.3    Beavo, J.A.4
  • 37
    • 0028070403 scopus 로고
    • Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase
    • Francis, S. H., J. L. Colbran, L. M. McAllister-Lucas, and J. D. Corbin. Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase. J. Biol. Chem. 269:22477-22480 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22477-22480
    • Francis, S.H.1    Colbran, J.L.2    McAllister-Lucas, L.M.3    Corbin, J.D.4
  • 38
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution
    • Weber, I. T., and T. A. Steitz. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198:311-326 (1987).
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 39
    • 1842411601 scopus 로고
    • Competitive inhibition (simple intersecting linear competitive inhibition)
    • John Wiley & Sons, New York
    • Segel, I. H. Competitive inhibition (simple intersecting linear competitive inhibition), in Enzyme Kinetics. John Wiley & Sons, New York, 107-109 (1975).
    • (1975) Enzyme Kinetics , pp. 107-109
    • Segel, I.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.