메뉴 건너뛰기




Volumn 88, Issue 4, 1996, Pages 1321-1329

Human platelet cGI-PDE: Expression in yeast and localization of the catalytic domain by deletion mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC GMP PHOSPHODIESTERASE;

EID: 0029797257     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v88.4.1321.bloodjournal8841321     Document Type: Article
Times cited : (43)

References (55)
  • 1
    • 0027973543 scopus 로고
    • Goals for signal transduction pathways: Linking up with transcriptional regulation
    • Sassone-Corsi P: Goals for signal transduction pathways: Linking up with transcriptional regulation (review). EMBO J 13:4717, 1994
    • (1994) EMBO J , vol.13 , pp. 4717
    • Sassone-Corsi, P.1
  • 2
    • 0027964862 scopus 로고
    • Estrogen action via the cAMP signaling pathway: Stimulation of adenylate cyclase and cAMP-regulated gene transcription
    • Aronica SM, Kraus WL, Katzenellenbogen BS: Estrogen action via the cAMP signaling pathway: Stimulation of adenylate cyclase and cAMP-regulated gene transcription. Proc Natl Acad Sci USA 91:8517, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8517
    • Aronica, S.M.1    Kraus, W.L.2    Katzenellenbogen, B.S.3
  • 3
    • 0028050688 scopus 로고
    • Evidence for participation of calcineurin in potentiation of agonist-stimulated cyclic AMP formation by the calcium-mobilizing hormone, angiotensin II
    • Baukal AJ, Hunyady L, Catt KJ, Balla T: Evidence for participation of calcineurin in potentiation of agonist-stimulated cyclic AMP formation by the calcium-mobilizing hormone, angiotensin II. J Biol Chem 269:24546, 1994
    • (1994) J Biol Chem , vol.269 , pp. 24546
    • Baukal, A.J.1    Hunyady, L.2    Catt, K.J.3    Balla, T.4
  • 4
    • 0028171317 scopus 로고
    • Adenosine A1 receptors mediate chronic ethanol-induced increases in receptor-stimulated cyclic AMP in cultured hepatocytes
    • Nagy LE, DeSilva SE: Adenosine A1 receptors mediate chronic ethanol-induced increases in receptor-stimulated cyclic AMP in cultured hepatocytes. Biochem J 304:205, 1994
    • (1994) Biochem J , vol.304 , pp. 205
    • Nagy, L.E.1    DeSilva, S.E.2
  • 5
    • 0026321604 scopus 로고
    • Mutating protein kinase cAMP-binding sites into cGMP-binding sites. Mechanism of cGMP selectivity
    • Shabb JB, Buzzeo BD, Ng L, Corbin JD: Mutating protein kinase cAMP-binding sites into cGMP-binding sites. Mechanism of cGMP selectivity. J Biol Chem 266:24320, 1991
    • (1991) J Biol Chem , vol.266 , pp. 24320
    • Shabb, J.B.1    Buzzeo, B.D.2    Ng, L.3    Corbin, J.D.4
  • 8
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • Beavo JA, Conti M, Heaslip RJ: Multiple cyclic nucleotide phosphodiesterases. Mol Pharmacol 46:399, 1994
    • (1994) Mol Pharmacol , vol.46 , pp. 399
    • Beavo, J.A.1    Conti, M.2    Heaslip, R.J.3
  • 10
    • 0019518111 scopus 로고
    • Regulation of cyclic AMP metabolism in human platelets. Sequential activation of adenylate cyclase and cyclic AMP phosphodiesterase by prostaglandins
    • Alvarez R, Taylor A, Fazzari JJ, Jacobs JR: Regulation of cyclic AMP metabolism in human platelets. Sequential activation of adenylate cyclase and cyclic AMP phosphodiesterase by prostaglandins. Mol Pharmacol 20:302, 1981
    • (1981) Mol Pharmacol , vol.20 , pp. 302
    • Alvarez, R.1    Taylor, A.2    Fazzari, J.J.3    Jacobs, J.R.4
  • 11
    • 0023679813 scopus 로고
    • Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets
    • Macphee CH, Reifsnyder DH, Moore TA, Lerea KM, Beavo JA: Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets. J Biol Chem 263:10353, 1988
    • (1988) J Biol Chem , vol.263 , pp. 10353
    • Macphee, C.H.1    Reifsnyder, D.H.2    Moore, T.A.3    Lerea, K.M.4    Beavo, J.A.5
  • 12
    • 2142854957 scopus 로고
    • cAMP-mediated phosphorylation of the low-Km cAMP phosphodiesterase markedly stimulates its catalytic activity
    • Grant PG, Mannarino AF, Colman RW: cAMP-mediated phosphorylation of the low-Km cAMP phosphodiesterase markedly stimulates its catalytic activity. Proc Natl Acad Sci USA 85:9071, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9071
    • Grant, P.G.1    Mannarino, A.F.2    Colman, R.W.3
  • 13
    • 0023677847 scopus 로고
    • Activation of the particulate low Km phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinase
    • Gettys TW, Vine AJ, Simonds MF, Corbin JD: Activation of the particulate low Km phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinase. J Biol Chem 263:10359, 1988
    • (1988) J Biol Chem , vol.263 , pp. 10359
    • Gettys, T.W.1    Vine, A.J.2    Simonds, M.F.3    Corbin, J.D.4
  • 14
    • 0024253227 scopus 로고
    • Multiple isozymes of cyclic nucleotide phosphodiesterase
    • Beavo JA: Multiple isozymes of cyclic nucleotide phosphodiesterase [review]. Adv Second Messenger Phosphoprotein Res 22:1, 1988
    • (1988) Adv Second Messenger Phosphoprotein Res , vol.22 , pp. 1
    • Beavo, J.A.1
  • 15
    • 0025012986 scopus 로고
    • Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterases
    • Charbonneau H, Prusti RK, LeTrong H, Sonnenburg WK, Mullaney PJ, Walsh KA, Beavo JA: Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterases. Proc Natl Acad Sci USA 87:288, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 288
    • Charbonneau, H.1    Prusti, R.K.2    LeTrong, H.3    Sonnenburg, W.K.4    Mullaney, P.J.5    Walsh, K.A.6    Beavo, J.A.7
  • 16
    • 0025179687 scopus 로고
    • Purification and characterization of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from the cytosol of human platelets
    • Grant PG, Mannarino AF, Colman RW: Purification and characterization of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from the cytosol of human platelets. Thromb Res 59:105, 1990
    • (1990) Thromb Res , vol.59 , pp. 105
    • Grant, P.G.1    Mannarino, A.F.2    Colman, R.W.3
  • 18
    • 0023921455 scopus 로고
    • Effects of SK&F 94120, an inhibitor of cyclic nucleotide phosphodiesterase type III, on human platelets
    • Simpson AW, Reeves ML, Rink TJ: Effects of SK&F 94120, an inhibitor of cyclic nucleotide phosphodiesterase type III, on human platelets. Biochem Pharmacol 37:2315, 1988
    • (1988) Biochem Pharmacol , vol.37 , pp. 2315
    • Simpson, A.W.1    Reeves, M.L.2    Rink, T.J.3
  • 19
    • 0025215525 scopus 로고
    • Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors
    • Beavo JA, Reifsnyder DH: Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors [review]. Trends Pharmacol Sci 11:150, 1990
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 150
    • Beavo, J.A.1    Reifsnyder, D.H.2
  • 20
    • 0027469344 scopus 로고
    • Isoenzyme selective phosphodiesterase inhibitors: Potential clinical uses
    • Hall IP: Isoenzyme selective phosphodiesterase inhibitors: Potential clinical uses [review], Br J Clin Pharmacol 35:1, 1993
    • (1993) Br J Clin Pharmacol , vol.35 , pp. 1
    • Hall, I.P.1
  • 21
    • 0026586838 scopus 로고
    • Inhibitors of cyclic nucleotide phosphodiesterases as therapeutic agents
    • Murray KJ, England PJ: Inhibitors of cyclic nucleotide phosphodiesterases as therapeutic agents [review]. Biochem Soc Trans 20:460, 1992
    • (1992) Biochem Soc Trans , vol.20 , pp. 460
    • Murray, K.J.1    England, P.J.2
  • 22
    • 0027468538 scopus 로고
    • Cilostazol, a novel cyclic AMP phosphodiesterase inhibitor, prevents reocclusion after coronary arterial thrombolysis with recombinant tissue-type plasminogen activator
    • Saitoh S, Saito T, Otake A, Owada T, Mitsugi M, Hashimoto H, Maruyama Y: Cilostazol, a novel cyclic AMP phosphodiesterase inhibitor, prevents reocclusion after coronary arterial thrombolysis with recombinant tissue-type plasminogen activator. Arterioscler Thromb 13:563, 1993
    • (1993) Arterioscler Thromb , vol.13 , pp. 563
    • Saitoh, S.1    Saito, T.2    Otake, A.3    Owada, T.4    Mitsugi, M.5    Hashimoto, H.6    Maruyama, Y.7
  • 23
    • 0023921455 scopus 로고
    • Effects of SK&F 94120, an inhibitor of cyclic nucleotide phosphodiesterase type III, on human platelets
    • Simpson AW, Reeves ML, Rink TJ: Effects of SK&F 94120, an inhibitor of cyclic nucleotide phosphodiesterase type III, on human platelets. Biochem Pharmacol 37:2315, 1988
    • (1988) Biochem Pharmacol , vol.37 , pp. 2315
    • Simpson, A.W.1    Reeves, M.L.2    Rink, T.J.3
  • 25
    • 0027219034 scopus 로고
    • Two isoforms of cGMP-inhibited cyclic nucleotide phosphodiesterases in human tissues distinguished by their responses to vesnarinone, a new cardiotonic agent
    • Masuoka H, Ito M, Sugioka M, Kozeki H, Konishi T, Tanaka T, Nakano T: Two isoforms of cGMP-inhibited cyclic nucleotide phosphodiesterases in human tissues distinguished by their responses to vesnarinone, a new cardiotonic agent. Biochem Biophys Res Commun 190:412, 1993
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 412
    • Masuoka, H.1    Ito, M.2    Sugioka, M.3    Kozeki, H.4    Konishi, T.5    Tanaka, T.6    Nakano, T.7
  • 26
    • 0021359546 scopus 로고
    • Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase
    • Grant PG, Colman RW: Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase. Biochemistry 23:1801, 1984
    • (1984) Biochemistry , vol.23 , pp. 1801
    • Grant, P.G.1    Colman, R.W.2
  • 27
    • 0028097556 scopus 로고
    • Mutational mapping of kinetic and pharmacological properties of a human cardiac cAMP phosphodiesterase
    • Pillai R, Staub SF, Colicelli J: Mutational mapping of kinetic and pharmacological properties of a human cardiac cAMP phosphodiesterase. J Biol Chem 269:30676, 1994
    • (1994) J Biol Chem , vol.269 , pp. 30676
    • Pillai, R.1    Staub, S.F.2    Colicelli, J.3
  • 28
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 29
    • 0003474640 scopus 로고
    • Hybridization in the analysis of RNA
    • Hanes BD, Higgins SJ (eds): Washington, DC, IRL
    • Williams JG, Mason PJ: Hybridization in the analysis of RNA, in Hanes BD, Higgins SJ (eds): Nucleic Acid Hybridization. Washington, DC, IRL, 1987, 139
    • (1987) Nucleic Acid Hybridization , pp. 139
    • Williams, J.G.1    Mason, P.J.2
  • 30
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg AP, Vogelstein B: A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132:6, 1983
    • (1983) Anal Biochem , vol.132 , pp. 6
    • Feinberg, A.P.1    Vogelstein, B.2
  • 31
    • 0001903367 scopus 로고
    • Construction and screening cDNA libraries in λgt10 and λgt11
    • Glover DM (ed): Washington, DC, IRL
    • Huynh TV, Young RA, Davis RW: Construction and screening cDNA libraries in λgt10 and λgt11, in Glover DM (ed): DNA Cloning: A Practical Approach. Washington, DC, IRL, 1985, 49
    • (1985) DNA Cloning: A Practical Approach , pp. 49
    • Huynh, T.V.1    Young, R.A.2    Davis, R.W.3
  • 32
    • 0025967117 scopus 로고
    • Expression of human recombinant cAMP phosphodiesterase isozyme IV reverses growth arrest phenotypes in phosphodiesterase-deficient yeast
    • McHale MM, Cieslinski LB, Eng WK, Johnson RK, Torphy TJ, Livi GP: Expression of human recombinant cAMP phosphodiesterase isozyme IV reverses growth arrest phenotypes in phosphodiesterase-deficient yeast. Mol Pharmacol 39:109, 1991
    • (1991) Mol Pharmacol , vol.39 , pp. 109
    • McHale, M.M.1    Cieslinski, L.B.2    Eng, W.K.3    Johnson, R.K.4    Torphy, T.J.5    Livi, G.P.6
  • 33
    • 0027339578 scopus 로고
    • A low-km rolipram-sensitive, cAMP-specific phosphodiesterase form human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA
    • McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-km rolipram-sensitive, cAMP-specific phosphodiesterase form human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem 268:6470, 1993
    • (1993) J Biol Chem , vol.268 , pp. 6470
    • McLaughlin, M.M.1    Cieslinski, L.B.2    Burman, M.3    Torphy, T.J.4    Livi, G.P.5
  • 34
    • 0017240112 scopus 로고
    • Evidence for a new diffusible element of mating pheromones in yeast
    • Hicks JB, Herskowitz I: Evidence for a new diffusible element of mating pheromones in yeast. Nature 260:246, 1976
    • (1976) Nature , vol.260 , pp. 246
    • Hicks, J.B.1    Herskowitz, I.2
  • 35
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A: Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153:163, 1983
    • (1983) J Bacteriol , vol.153 , pp. 163
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 36
    • 0017378834 scopus 로고
    • Cyclic AMP metabolism in cholesterol-rich platelets
    • Sinha AK, Shattil SJ, Colman RW: Cyclic AMP metabolism in cholesterol-rich platelets. J Biol Chem 252:3310, 1977
    • (1977) J Biol Chem , vol.252 , pp. 3310
    • Sinha, A.K.1    Shattil, S.J.2    Colman, R.W.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 39
    • 0020321974 scopus 로고
    • HEL cells: A new human erythroleukemia cell line with spontaneous and induced globin expression
    • Martin P, Papayannopoulou T: HEL cells: A new human erythroleukemia cell line with spontaneous and induced globin expression. Science 216:1233, 1982
    • (1982) Science , vol.216 , pp. 1233
    • Martin, P.1    Papayannopoulou, T.2
  • 41
    • 0025283678 scopus 로고
    • Enhanced expression of thrombomodulin by intracellular cyclic AMP-increasing agents in two human megakaryoblastic leukemia cell lines
    • Ito T, Ogura M, Morishita Y, Takamatsu J, Maruyama I, Yamamoto S, Ogawa K, Saito H: Enhanced expression of thrombomodulin by intracellular cyclic AMP-increasing agents in two human megakaryoblastic leukemia cell lines. Thromb Res 58:615, 1990
    • (1990) Thromb Res , vol.58 , pp. 615
    • Ito, T.1    Ogura, M.2    Morishita, Y.3    Takamatsu, J.4    Maruyama, I.5    Yamamoto, S.6    Ogawa, K.7    Saito, H.8
  • 42
    • 0028888001 scopus 로고
    • Human erythroleukemic (HEL) cells express a platelet P2T-like ADP receptor
    • Shi XP, Yin KC, Gardell SJ: Human erythroleukemic (HEL) cells express a platelet P2T-like ADP receptor. Thromb Res 77:235, 1995
    • (1995) Thromb Res , vol.77 , pp. 235
    • Shi, X.P.1    Yin, K.C.2    Gardell, S.J.3
  • 43
    • 0023131421 scopus 로고
    • Cloning and characterization of platelet factor 4 cDNA derived from a human erythroleukemic cell line
    • Poncz M, Surrey S, LaRocco P, Weiss MJ, Rappaport EF, Conway TM, Schwartz E: Cloning and characterization of platelet factor 4 cDNA derived from a human erythroleukemic cell line. Blood 69:219, 1987
    • (1987) Blood , vol.69 , pp. 219
    • Poncz, M.1    Surrey, S.2    LaRocco, P.3    Weiss, M.J.4    Rappaport, E.F.5    Conway, T.M.6    Schwartz, E.7
  • 44
    • 0024601850 scopus 로고
    • Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library
    • Wenger RH, Wicki AN, Walz A, Kieffer N, Clemetson KJ: Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library. Blood 73:1498, 1989
    • (1989) Blood , vol.73 , pp. 1498
    • Wenger, R.H.1    Wicki, A.N.2    Walz, A.3    Kieffer, N.4    Clemetson, K.J.5
  • 45
    • 0029000706 scopus 로고
    • Multiple transcripts for the human cardiac form of the cGMP-inhibited cAMP phosphodiesterase
    • Kasuya J, Goko H, Fujita-Yamaguchi Y: Multiple transcripts for the human cardiac form of the cGMP-inhibited cAMP phosphodiesterase. J Biol Chem 270:14305, 1995
    • (1995) J Biol Chem , vol.270 , pp. 14305
    • Kasuya, J.1    Goko, H.2    Fujita-Yamaguchi, Y.3
  • 47
    • 0023696370 scopus 로고
    • Purification of cAMP phosphodiesterase from platelets
    • Grant PG, Colman RW: Purification of cAMP phosphodiesterase from platelets. Methods Enzymol 159:772, 1988
    • (1988) Methods Enzymol , vol.159 , pp. 772
    • Grant, P.G.1    Colman, R.W.2
  • 48
    • 0024514081 scopus 로고
    • A hypervariable microsatellite revealed by in vitro amplification of a dinucleotide repeat within the cardiac muscle actin gene
    • Litt M, Luty JA: A hypervariable microsatellite revealed by in vitro amplification of a dinucleotide repeat within the cardiac muscle actin gene. Am J Hum Genet 44:397, 1989
    • (1989) Am J Hum Genet , vol.44 , pp. 397
    • Litt, M.1    Luty, J.A.2
  • 50
    • 0026753496 scopus 로고
    • Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain
    • Jin SL, Swinnen JV, Conti M: Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain. J Biol Chem 267:18929, 1992
    • (1992) J Biol Chem , vol.267 , pp. 18929
    • Jin, S.L.1    Swinnen, J.V.2    Conti, M.3
  • 51
    • 0027283557 scopus 로고
    • Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase
    • Taira M, Hockman SC, Calvo JC, Belfrage P, Manganiello VC: Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase. J Biol Chem 268:18573, 1993
    • (1993) J Biol Chem , vol.268 , pp. 18573
    • Taira, M.1    Hockman, S.C.2    Calvo, J.C.3    Belfrage, P.4    Manganiello, V.C.5
  • 52
    • 0022961581 scopus 로고
    • Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species
    • Charbonneau H, Beier N, Walsh KA, Beavo JA: Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species. Proc Natl Acad Sci USA 83:9308, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9308
    • Charbonneau, H.1    Beier, N.2    Walsh, K.A.3    Beavo, J.A.4
  • 54
    • 0028788430 scopus 로고
    • Divalent metal cation requirement and possible classification of cGMP-inhibited phosphodiesterase as a metallohydrolase
    • Omburo GA, Brickus T, Ghazaleh FA, Colman RW: Divalent metal cation requirement and possible classification of cGMP-inhibited phosphodiesterase as a metallohydrolase. Arch Biochem Biophys 323:1, 1995
    • (1995) Arch Biochem Biophys , vol.323 , pp. 1
    • Omburo, G.A.1    Brickus, T.2    Ghazaleh, F.A.3    Colman, R.W.4
  • 55
    • 0028070403 scopus 로고
    • Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase
    • Francis SH, Colbran JL, McAllister-Lucas LM, Corbin JD: Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase. J Biol Chem 269:22477, 1994
    • (1994) J Biol Chem , vol.269 , pp. 22477
    • Francis, S.H.1    Colbran, J.L.2    McAllister-Lucas, L.M.3    Corbin, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.