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Volumn 106, Issue 2, 2000, Pages 283-292

Characterization of cyclic AMP phosphodiesterases in Leishmania mexicana and purification of a soluble form

Author keywords

cAMP; Leishmania; Phosphodiesterase; Purification

Indexed keywords

CAFFEINE; CYCLIC AMP PHOSPHODIESTERASE; CYCLIC GMP; ISOBUTYLMETHYLXANTHINE; MAGNESIUM; N CYCLOHEXYL 4 (1,2 DIHYDRO 2 OXO 6 QUINOLYLOXY) N (2 HYDROXYETHYL)BUTYRAMIDE; ROLIPRAM; THEOPHYLLINE; ZAPRINAST;

EID: 0034049859     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00224-8     Document Type: Article
Times cited : (24)

References (41)
  • 2
    • 0029009878 scopus 로고
    • Recent progress in understanding the hormonal regulation of phosphodiesterases
    • Conti M., Nemoz G., Sette C., Vicini E. Recent progress in understanding the hormonal regulation of phosphodiesterases. Endocr. Rev. 16:1995;370-389.
    • (1995) Endocr. Rev. , vol.16 , pp. 370-389
    • Conti, M.1    Nemoz, G.2    Sette, C.3    Vicini, E.4
  • 3
    • 33847612208 scopus 로고
    • Adenosine 3′-5′ phosphate in biological materials
    • Butcher R.W., Sutherland E.W. Adenosine 3′-5′ phosphate in biological materials. J. Biol. Chem. 237:1962;1244-1250.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1244-1250
    • Butcher, R.W.1    Sutherland, E.W.2
  • 4
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • Thompson W.J., Appleman M.M. Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry. 10:1971;311-316.
    • (1971) Biochemistry , vol.10 , pp. 311-316
    • Thompson, W.J.1    Appleman, M.M.2
  • 5
    • 0015239529 scopus 로고
    • Characterization of cyclic nucleotide phosphodiesterases of rat tissues
    • Thompson W.J., Appleman M.M. Characterization of cyclic nucleotide phosphodiesterases of rat tissues. J. Biol. Chem. 246:1971;3145-3150.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3145-3150
    • Thompson, W.J.1    Appleman, M.M.2
  • 6
    • 0032555138 scopus 로고    scopus 로고
    • Cloning and characterization of a cAMP-specific cyclic nucleotide phosphodiesterase
    • Soderling S.H., Bayuga S.J., Beavo J.A. Cloning and characterization of a cAMP-specific cyclic nucleotide phosphodiesterase. Proc. Nat. Acad. Sci. USA. 9:1998;8991-8996.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.9 , pp. 8991-8996
    • Soderling, S.H.1    Bayuga, S.J.2    Beavo, J.A.3
  • 7
    • 0032546924 scopus 로고    scopus 로고
    • Identification and characterization of a novel family of cyclic nucleotide phosphodiesterases
    • Soderling S.H., Bayuga S.J., Beavo J.A. Identification and characterization of a novel family of cyclic nucleotide phosphodiesterases. J. Biol. Chem. 273(25):1998;15553-15558.
    • (1998) J. Biol. Chem. , vol.273 , Issue.25 , pp. 15553-15558
    • Soderling, S.H.1    Bayuga, S.J.2    Beavo, J.A.3
  • 8
    • 0033536020 scopus 로고    scopus 로고
    • Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE 10A
    • Soderling S.H., Bayuga S.J., Beavo J.A. Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE 10A. Proc. Natl. Acad. Sci. USA. 96:1999;7071-7076.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7071-7076
    • Soderling, S.H.1    Bayuga, S.J.2    Beavo, J.A.3
  • 9
    • 0023427567 scopus 로고
    • Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae
    • Nikawa J., Sass P., Wigler M. Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1987;3629-3636.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3629-3636
    • Nikawa, J.1    Sass, P.2    Wigler, M.3
  • 10
    • 0023007633 scopus 로고
    • Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum
    • Lacombe M.L., Podgorski G.J., Franke J, Kessin R.H. Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum. J. Biol. Chem. 261:1986;16811-16817.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16811-16817
    • Lacombe, M.L.1    Podgorski, G.J.2    Franke, J.3    Kessin, R.H.4
  • 11
    • 0027219228 scopus 로고
    • Characterization of a periplasmic 3′:5′-cyclic nucleotide phosphodiesterase gene, cpdP, from the marine symbiotic bacterium Vibrio fischeri
    • Dunlap P.V., Callahan S.M. Characterization of a periplasmic 3′:5′-cyclic nucleotide phosphodiesterase gene, cpdP, from the marine symbiotic bacterium Vibrio fischeri. J. Bacteriol. 175:1993;4615-4624.
    • (1993) J. Bacteriol. , vol.175 , pp. 4615-4624
    • Dunlap, P.V.1    Callahan, S.M.2
  • 12
    • 0028037682 scopus 로고
    • A Candida albicans cyclic nucleotide phosphodiesterase: Cloning and expression in Saccharomyces cerevisiae and biochemical characterization of the enzyme
    • Hoyer L.L., Cieslinsky L.B., McLaughlin M.M., Thorphy T.J., Shatzman A.R., Livi G.P. A Candida albicans cyclic nucleotide phosphodiesterase: cloning and expression in Saccharomyces cerevisiae and biochemical characterization of the enzyme. Microbiology. 140:1994;1533-1542.
    • (1994) Microbiology , vol.140 , pp. 1533-1542
    • Hoyer, L.L.1    Cieslinsky, L.B.2    McLaughlin, M.M.3    Thorphy, T.J.4    Shatzman, A.R.5    Livi, G.P.6
  • 13
    • 0018078641 scopus 로고
    • Adenylate cyclase in bloodstream forms of Trypanosoma brucei brucei
    • Martin B.R., Voorheis H.P., Kennedy E.L. Adenylate cyclase in bloodstream forms of Trypanosoma brucei brucei. Biochem. J. 175:1978;207-212.
    • (1978) Biochem. J. , vol.175 , pp. 207-212
    • Martin, B.R.1    Voorheis, H.P.2    Kennedy, E.L.3
  • 14
    • 0019571794 scopus 로고
    • Cyclic 3′, 5′-adenosine monophosphate levels during developmental cycle of Trypanosoma brucei brucei in the rat
    • Mancini P.E., Patton C.L. Cyclic 3′, 5′-adenosine monophosphate levels during developmental cycle of Trypanosoma brucei brucei in the rat. Mol. Biochem. Parasitol. 3:1981;19-31.
    • (1981) Mol. Biochem. Parasitol. , vol.3 , pp. 19-31
    • Mancini, P.E.1    Patton, C.L.2
  • 15
    • 0020352579 scopus 로고
    • Subcellular distribution of adenylate cyclase, cAMP phosphodiesterase, protein kinase and phosphoprotein phosphatase in Trypanosoma brucei
    • Walter R.D., Opperdoes F.R. Subcellular distribution of adenylate cyclase, cAMP phosphodiesterase, protein kinase and phosphoprotein phosphatase in Trypanosoma brucei. Mol. Biochem. Parasitol. 6:1982;287-295.
    • (1982) Mol. Biochem. Parasitol. , vol.6 , pp. 287-295
    • Walter, R.D.1    Opperdoes, F.R.2
  • 16
    • 0021099659 scopus 로고
    • The cAMP receptor protein of Trypanosoma cruzi
    • Rangel-Aldao R., Tovar G., de Ruiz M.L. The cAMP receptor protein of Trypanosoma cruzi. J. Biol. Chem. 258:1983;6976-6983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6976-6983
    • Rangel-Aldao, R.1    Tovar, G.2    De Ruiz, M.L.3
  • 17
    • 0023475546 scopus 로고
    • Trypanosoma cruzi: Adrenergic modulation of cAMP role in proliferation and differentiation in vitro
    • De Castro S.L., Meirelles M.N.L., Oliveira M.M. Trypanosoma cruzi: adrenergic modulation of cAMP role in proliferation and differentiation in vitro. Exp. Parasitol. 64:1987;368-375.
    • (1987) Exp. Parasitol. , vol.64 , pp. 368-375
    • De Castro, S.L.1    Meirelles, M.N.L.2    Oliveira, M.M.3
  • 19
    • 0023927842 scopus 로고
    • Effects of α- And β-adrenergic agonists on Trypanosoma cruzi interaction with host cells
    • Connely M.C., Ayala A., Kierszenbaum F. Effects of α- and β-adrenergic agonists on Trypanosoma cruzi interaction with host cells. J. Parasitol. 74:1988;379-386.
    • (1988) J. Parasitol. , vol.74 , pp. 379-386
    • Connely, M.C.1    Ayala, A.2    Kierszenbaum, F.3
  • 20
    • 0026673477 scopus 로고
    • Characterization of a G-protein form Trypanosoma cruzi epimastigote membranes
    • Coso O.A., Diaz Anel A., Martinetto H. et al. Characterization of a G-protein form Trypanosoma cruzi epimastigote membranes. Biochem. J. 287:1992;443-446.
    • (1992) Biochem. J. , vol.287 , pp. 443-446
    • Coso, O.A.1    Diaz Anel, A.2    Martinetto, H.3
  • 21
    • 0029954373 scopus 로고    scopus 로고
    • Cloning from Leishmania major of a developmentally regulated gene, c-lpk2, for the catalytic subunit of the cAMP-dependant protein kinase
    • Siman-Tov M.M., Aly R., Shapira M., Jaffe C.L. Cloning from Leishmania major of a developmentally regulated gene, c-lpk2, for the catalytic subunit of the cAMP-dependant protein kinase. Mol. Biochem. Parasitol. 77:1996;201-215.
    • (1996) Mol. Biochem. Parasitol. , vol.77 , pp. 201-215
    • Siman-Tov, M.M.1    Aly, R.2    Shapira, M.3    Jaffe, C.L.4
  • 22
    • 0033574724 scopus 로고    scopus 로고
    • A novel gene encoding a ras-like GTP-binding protein from Trypanosoma brucei: An evolutionary ancestor of the ras and rap genes of higher eukayotes
    • Sowa M.P.K., Coulter L.J., Tait A., Hide G. A novel gene encoding a ras-like GTP-binding protein from Trypanosoma brucei: an evolutionary ancestor of the ras and rap genes of higher eukayotes. Gene. 230:1999;155-161.
    • (1999) Gene , vol.230 , pp. 155-161
    • Sowa, M.P.K.1    Coulter, L.J.2    Tait, A.3    Hide, G.4
  • 23
    • 0018158805 scopus 로고
    • Effect of cAMP on transformation and proliferation of Leishmania cells
    • Walter R.D., Buse E., Ebert F. Effect of cAMP on transformation and proliferation of Leishmania cells. Tropenmed. Parasit. 29:1978;439-447.
    • (1978) Tropenmed. Parasit. , vol.29 , pp. 439-447
    • Walter, R.D.1    Buse, E.2    Ebert, F.3
  • 24
    • 0039282082 scopus 로고
    • Regulation of cAMP metabolism in Leishmania promastigotes and amastigotes
    • D. Slutzky. Oxford: Pergamon Press
    • Walter R.D. Regulation of cAMP metabolism in Leishmania promastigotes and amastigotes. Slutzky D. The Biochemistry of Parasites. 1981;151-167 Pergamon Press, Oxford.
    • (1981) The Biochemistry of Parasites , pp. 151-167
    • Walter, R.D.1
  • 25
    • 0016702153 scopus 로고
    • Adenosine 3′, 5′-monophosphate in reproducing and differentiated Trypanosomes
    • Strickler J.E., Patton C.L. Adenosine 3′, 5′-monophosphate in reproducing and differentiated Trypanosomes. Science. 190:1975;1110-1112.
    • (1975) Science , vol.190 , pp. 1110-1112
    • Strickler, J.E.1    Patton, C.L.2
  • 26
    • 0030696101 scopus 로고    scopus 로고
    • Differentiation of African trypanosomes is controlled by a density sensing mechanism which signals cell cycle arrest via cAMP pathway
    • Vassella E., Reuner B., Yutzy B., Boshart M. Differentiation of African trypanosomes is controlled by a density sensing mechanism which signals cell cycle arrest via cAMP pathway. J. Cell. Sci. 110:1997;2661-2671.
    • (1997) J. Cell. Sci. , vol.110 , pp. 2661-2671
    • Vassella, E.1    Reuner, B.2    Yutzy, B.3    Boshart, M.4
  • 27
    • 0023795507 scopus 로고
    • Assay of cyclic nucleotide phosphodiesterase using radiolabeled and fluorescent substrates
    • Kincaid R.L., Manganiello V.C. Assay of cyclic nucleotide phosphodiesterase using radiolabeled and fluorescent substrates. Adv. Enzymol. 159:1988;457-470.
    • (1988) Adv. Enzymol. , vol.159 , pp. 457-470
    • Kincaid, R.L.1    Manganiello, V.C.2
  • 28
    • 0031686647 scopus 로고    scopus 로고
    • Comparative phosphorylation of calmodulin from trypanosomatids and bovine brain by calmodulin-binding protein kinases
    • Benaim G., Cervino V., Villalobo A. Comparative phosphorylation of calmodulin from trypanosomatids and bovine brain by calmodulin-binding protein kinases. Comp. Biochem. Physiol. 120:1998;57-65.
    • (1998) Comp. Biochem. Physiol. , vol.120 , pp. 57-65
    • Benaim, G.1    Cervino, V.2    Villalobo, A.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 78651153791 scopus 로고
    • Disc-electrophoresis-II method and application to human serum
    • Davis B. Disc-electrophoresis-II method and application to human serum. Ann. NY. Acad. Sci. 2:1964;404-427.
    • (1964) Ann. NY. Acad. Sci. , vol.2 , pp. 404-427
    • Davis, B.1
  • 32
    • 0026531771 scopus 로고
    • Purification and properties of the cGMP-inhibited cAMP phosphodiesterase from bovine aortic smooth muscle
    • Rascón A., Lindgren S., Stavenow L. et al. Purification and properties of the cGMP-inhibited cAMP phosphodiesterase from bovine aortic smooth muscle. Biochim. Biophys. Acta. 1134:1992;149-156.
    • (1992) Biochim. Biophys. Acta , vol.1134 , pp. 149-156
    • Rascón, A.1    Lindgren, S.2    Stavenow, L.3
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1972;680-685.
    • (1972) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0023878613 scopus 로고
    • Improvement and simplification of low-background silver staining of proteins by using sodium dithionite
    • Rabilloud T., Carpentier G., Tarroux P. Improvement and simplification of low-background silver staining of proteins by using sodium dithionite. Electrophoresis. 9:1988;288-291.
    • (1988) Electrophoresis , vol.9 , pp. 288-291
    • Rabilloud, T.1    Carpentier, G.2    Tarroux, P.3
  • 35
    • 0019489914 scopus 로고
    • The extracellular cyclic nucleotide phosphodiesterase of Dictyostelium discoideum: Purification and characterization
    • Orlow S.J., Shapiro R.L., Franke J., Kessin R.H. The extracellular cyclic nucleotide phosphodiesterase of Dictyostelium discoideum: purification and characterization. J. Biol. Chem. 256:1981;7620-7627.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7620-7627
    • Orlow, S.J.1    Shapiro, R.L.2    Franke, J.3    Kessin, R.H.4
  • 36
    • 0029089518 scopus 로고
    • Purification and properties of periplasmic 3′:5′-cyclic nucleotide phosphodiesterase
    • Callahan S.M., Cornell N.W., Dunlap P.V Purification and properties of periplasmic 3′:5′-cyclic nucleotide phosphodiesterase. J. Biol. Chem. 270:1995;17627-17632.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17627-17632
    • Callahan, S.M.1    Cornell, N.W.2    Dunlap, P.V.3
  • 37
    • 0020569144 scopus 로고
    • m cyclic nucleotide phosphodiesterase of bakers' yeast
    • m cyclic nucleotide phosphodiesterase of bakers' yeast. J. Biol. Chem. 258:1983;2966-2972.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2966-2972
    • Londesborough, J.1    Suoranta, K.2
  • 38
    • 0031719432 scopus 로고    scopus 로고
    • Critical role of conserved histidine pairs HNXXH and HDXXH in recombinant human phosphodiesterase 4A
    • Omburo G.A., Jacobitz S., Torphy T.J., Colman R.W. Critical role of conserved histidine pairs HNXXH and HDXXH in recombinant human phosphodiesterase 4A. Cell Sign. 10:1998;491-497.
    • (1998) Cell Sign. , vol.10 , pp. 491-497
    • Omburo, G.A.1    Jacobitz, S.2    Torphy, T.J.3    Colman, R.W.4
  • 39
    • 0028070403 scopus 로고
    • Zinc interactions of the cGMP binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase
    • Francis S.H., Colbran J.L., McAllister-Lucas L.M., Corbin J.D. Zinc interactions of the cGMP binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase. J. Biol. Chem. 269:1994;22477-22480.
    • (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
  • 40
    • 0016313001 scopus 로고
    • 3′,5′ cyclic AMP phosphodiesterase from Trypanosoma gambiense
    • Walter R.D. 3′,5′ cyclic AMP phosphodiesterase from Trypanosoma gambiense. Hoppe-Seylers Z. Physiol. Chem. 355:1974;1443-1450.
    • (1974) Hoppe-Seylers Z. Physiol. Chem. , vol.355 , pp. 1443-1450
    • Walter, R.D.1
  • 41
    • 0028268356 scopus 로고
    • Single-step purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase
    • Degerman E., Moos M., Rascón A. et al. Single-step purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase. Biochim. Biophys. Acta. 1205:1994;189-198.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 189-198
    • Degerman, E.1    Moos, M.2    Rascón, A.3


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