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Volumn 51, Issue 2, 1997, Pages 242-249

Selective activation of rolipram-sensitive, cAMP-specific phosphodiesterase isoforms by phosphatidic acid

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; ISOENZYME; PHOSPHODIESTERASE; PROTEIN KINASE INHIBITOR; RECOMBINANT PROTEIN; ROLIPRAM; STAUROSPORINE;

EID: 0039181708     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.51.2.242     Document Type: Article
Times cited : (59)

References (45)
  • 1
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton, J. H. Phosphatidylcholine breakdown and signal transduction. Biochim. Biophys. Acta 1212:26-42 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 2
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar, W. H. Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270:12949-12952 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 3
    • 0026725673 scopus 로고
    • Phosphatidic acid that accumulates in platelet-derived growth factor-stimulated Balb/c3T3 cells is a potential mitogenic signal
    • Fukami, K., and T. Takenawa. Phosphatidic acid that accumulates in platelet-derived growth factor-stimulated Balb/c3T3 cells is a potential mitogenic signal. J. Biol. Chem. 267:10988-10993 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 10988-10993
    • Fukami, K.1    Takenawa, T.2
  • 4
    • 0026049696 scopus 로고
    • Sphingosine-1-phosphate, a novel lipid, involved in cellular proliferation
    • Zhang, H., N. N. Desai, A. Olivera, T. Seki, G. Brooker, and S. Spiegel. Sphingosine-1-phosphate, a novel lipid, involved in cellular proliferation. J. Cell Biol. 114:155-167 (1991).
    • (1991) J. Cell Biol. , vol.114 , pp. 155-167
    • Zhang, H.1    Desai, N.N.2    Olivera, A.3    Seki, T.4    Brooker, G.5    Spiegel, S.6
  • 5
    • 0026457994 scopus 로고
    • Sphingosine-1-phosphate, a metabolite of sphingosine, increases phosphatidic acid levels by phospholipase D activation
    • Desai, N. N., H. Zhang, A. Olivera, M. E. Mattie, and S. Spiegel. Sphingosine-1-phosphate, a metabolite of sphingosine, increases phosphatidic acid levels by phospholipase D activation. J. Biol. Chem. 267:23122-23128 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 23122-23128
    • Desai, N.N.1    Zhang, H.2    Olivera, A.3    Mattie, M.E.4    Spiegel, S.5
  • 7
    • 0025831191 scopus 로고
    • A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells
    • Breittmayer, J.-P., C. Aussel, D. Farahifar, J. L. Cousin, and M. Fehlman. A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells. Immunology 73:134-139 (1991).
    • (1991) Immunology , vol.73 , pp. 134-139
    • Breittmayer, J.-P.1    Aussel, C.2    Farahifar, D.3    Cousin, J.L.4    Fehlman, M.5
  • 8
    • 0026458730 scopus 로고
    • Activation of NADPH oxidase and phospholipase D in permeabilized human neutrophils
    • Bauldry, S. A., K. L. Elsey, and D. A. Bass. Activation of NADPH oxidase and phospholipase D in permeabilized human neutrophils. J. Biol. Chem. 267:25141-25152 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25141-25152
    • Bauldry, S.A.1    Elsey, K.L.2    Bass, D.A.3
  • 9
    • 0027244275 scopus 로고
    • Phosphatidic acid induces the respiratory burst of electropermeabilized human neutrophils by acting on downstream step of protein kinase C
    • Mitsuyama, T., K. Takeshige, and S. Minakami. Phosphatidic acid induces the respiratory burst of electropermeabilized human neutrophils by acting on downstream step of protein kinase C. FEBS Lett. 328:67-70 (1993).
    • (1993) FEBS Lett. , vol.328 , pp. 67-70
    • Mitsuyama, T.1    Takeshige, K.2    Minakami, S.3
  • 10
    • 0025274039 scopus 로고
    • Phosphatidic acid and not diacylglycerol generated by phospholipase D is functionally linked to the activation of the NADPH oxidase by FMLP in human neutrophils
    • Rossi, F., M. Grzeskowiak, V. Della Bianca, F. Calzetti, and G. Gandini. Phosphatidic acid and not diacylglycerol generated by phospholipase D is functionally linked to the activation of the NADPH oxidase by FMLP in human neutrophils. Biochem. Biophys. Res. Commun. 168:320-327 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 320-327
    • Rossi, F.1    Grzeskowiak, M.2    Della Bianca, V.3    Calzetti, F.4    Gandini, G.5
  • 11
    • 0027262361 scopus 로고
    • Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains
    • Zhao, Z., S. H. Shen, and E. H. Fischer. Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains. Proc. Natl. Acad. Sci. USA 90:4251-4255 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4251-4255
    • Zhao, Z.1    Shen, S.H.2    Fischer, E.H.3
  • 12
    • 0029151931 scopus 로고
    • Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells
    • Tomic, S., U. Greiser, R. Lammers, A. Kharitonenkov, E. Imyanitov, A. Ullrich, and F. D. Böhmer. Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. J. Biol. Chem. 270:21277-21284 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21277-21284
    • Tomic, S.1    Greiser, U.2    Lammers, R.3    Kharitonenkov, A.4    Imyanitov, E.5    Ullrich, A.6    Böhmer, F.D.7
  • 13
    • 0028567280 scopus 로고
    • Phosphatidic acid activation of protein kinase C-ζ overexpressed in COS cells: Comparison with other protein kinase C isotypes and other acidic lipids
    • Limatola, C., D. Schaap, W. H. Moolenaar, and W. J. van Blitterswijk. Phosphatidic acid activation of protein kinase C-ζ overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids. Biochem. J. 304:1001-1008 (1994).
    • (1994) Biochem. J. , vol.304 , pp. 1001-1008
    • Limatola, C.1    Schaap, D.2    Moolenaar, W.H.3    Van Blitterswijk, W.J.4
  • 14
    • 0027495890 scopus 로고
    • The regulation of phospholipase C-γ1 by phosphatidic acid
    • Jones, G. A., and G. Carpenter. The regulation of phospholipase C-γ1 by phosphatidic acid. J. Biol. Chem. 268:20845-20850 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 20845-20850
    • Jones, G.A.1    Carpenter, G.2
  • 15
    • 0026744154 scopus 로고
    • Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase
    • Moritz, A., P. N. E. De Graan, W. H. Gispen, and K. W. A. Wirtz. Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase. J. Biol. Chem. 267:7207-7210 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 7207-7210
    • Moritz, A.1    De Graan, P.N.E.2    Gispen, W.H.3    Wirtz, K.W.A.4
  • 16
    • 0025296217 scopus 로고
    • Concanavalin A stimulates the rolipram-sensitive isoforms of cyclic nucleotide phosphodiesterase in rat thymic lymphocytes
    • Valette, L., A. F. Prigent, G. Némoz, G. Anker, O. Macovschi, and M. Lagarde. Concanavalin A stimulates the rolipram-sensitive isoforms of cyclic nucleotide phosphodiesterase in rat thymic lymphocytes. Biochem. Biophys. Res. Commun. 169:864-872 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 864-872
    • Valette, L.1    Prigent, A.F.2    Némoz, G.3    Anker, G.4    Macovschi, O.5    Lagarde, M.6
  • 17
    • 0027398917 scopus 로고
    • Phosphatidic acid stimulates the rolipram-sensitive cyclic nucleotide phosphodiesterase from rat thymocytes
    • Marcoz, P., G. Némoz, A. F. Prigent, and M. Lagarde. Phosphatidic acid stimulates the rolipram-sensitive cyclic nucleotide phosphodiesterase from rat thymocytes. Biochim. Biophys. Acta 1176:129-136 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1176 , pp. 129-136
    • Marcoz, P.1    Némoz, G.2    Prigent, A.F.3    Lagarde, M.4
  • 18
    • 0023938335 scopus 로고
    • The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response
    • Kammer, J. M. The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response. Immunol. Today 9:222-229 (1988).
    • (1988) Immunol. Today , vol.9 , pp. 222-229
    • Kammer, J.M.1
  • 19
    • 0028132624 scopus 로고
    • Role of phospholipase-D and phosphatidic acid in mediating gonadotropin-releasing hormone-induced inhibition of preantral granulosa cell differentiation
    • Amsterdam, A., A. Dantes, and M. Liscovitch. Role of phospholipase-D and phosphatidic acid in mediating gonadotropin-releasing hormone-induced inhibition of preantral granulosa cell differentiation. Endocrinology 135: 1205-1211 (1994).
    • (1994) Endocrinology , vol.135 , pp. 1205-1211
    • Amsterdam, A.1    Dantes, A.2    Liscovitch, M.3
  • 20
    • 0029009878 scopus 로고
    • Recent progress in understanding the hormonal regulation of phosphodiesterases
    • Conti, M., G. Némoz, C. Sette, and E. Vicini. Recent progress in understanding the hormonal regulation of phosphodiesterases. Endocr. Rev. 16:370-389 (1995).
    • (1995) Endocr. Rev. , vol.16 , pp. 370-389
    • Conti, M.1    Némoz, G.2    Sette, C.3    Vicini, E.4
  • 21
    • 0024405251 scopus 로고
    • Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: Evidence for a family of genes
    • M.
    • Swinnen, J. V., D. R. Joseph, and M. Conti. M. 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    Joseph, D.R.2    Conti, M.3
  • 22
  • 23
    • 0024670166 scopus 로고
    • Cloning and characterization of mammalian homologs of the Drosophila dunce gene
    • Davis, R. L., H. Takayasu, M. Eberwine, and J. Myres. Cloning and characterization of mammalian homologs of the Drosophila dunce gene. Proc. Natl. Acad. Sci. USA 86:3604-3608 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3604-3608
    • Davis, R.L.1    Takayasu, H.2    Eberwine, M.3    Myres, J.4
  • 24
    • 0026667380 scopus 로고
    • A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs: Molecular cloning of the 63-kDa calmodulin-dependent phosphodiesterase
    • Repaske, D. R., J. V. Swinnen, S. L. C. Jin, J. J. Van Wick, and M. Conti. A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs: molecular cloning of the 63-kDa calmodulin-dependent phosphodiesterase. J. Biol. Chem. 267:18683-18688 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18683-18688
    • Repaske, D.R.1    Swinnen, J.V.2    Jin, S.L.C.3    Van Wick, J.J.4    Conti, M.5
  • 25
    • 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. Janargin, 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    Janargin, K.7    Shelton, E.R.8
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0028360098 scopus 로고
    • The rat PDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase
    • Sette, C., E. Vicini, and M. Conti. The rat PDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase. J. Biol. Chem. 269:18271-18274 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18271-18274
    • Sette, C.1    Vicini, E.2    Conti, M.3
  • 29
    • 0026010201 scopus 로고
    • Properties and hormonal regulation of two structurally related cAMP phosphodiesterases from the rat Sertoli cells
    • Swinnen, J. V., K. E. Tsikalas, and M. Conti. Properties and hormonal regulation of two structurally related cAMP phosphodiesterases from the rat Sertoli cells. J. Biol. Chem. 266:18370-18377 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 18370-18377
    • Swinnen, J.V.1    Tsikalas, K.E.2    Conti, M.3
  • 30
    • 0028243837 scopus 로고
    • The short-term activation of a rolipramsensitive, cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells is mediated by a cAMP-dependent phosphorylation
    • Sette, C., S. Iona, and M. Conti. The short-term activation of a rolipramsensitive, cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells is mediated by a cAMP-dependent phosphorylation. J. Biol. Chem. 269:9245-9252 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 9245-9252
    • Sette, C.1    Iona, S.2    Conti, M.3
  • 31
    • 0028198615 scopus 로고
    • Modulation of cellular responses by hormones: Role of cAMP specific, rolipram-sensitive phosphodiesterases
    • Sette, C., E. Vicini, and M. Conti. Modulation of cellular responses by hormones: role of cAMP specific, rolipram-sensitive phosphodiesterases. Mol. Cell. Endocrinol. 100:75-79 (1994).
    • (1994) Mol. Cell. Endocrinol. , vol.100 , pp. 75-79
    • Sette, C.1    Vicini, E.2    Conti, M.3
  • 33
    • 0026753496 scopus 로고
    • Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase: Mapping of the catalytic domain
    • Jin, S. L. C., J. V. Swinnen, and M. Conti. Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase: mapping of the catalytic domain. J. Biol. Chern. 267:18929-18939 (1992).
    • (1992) J. Biol. Chern. , vol.267 , pp. 18929-18939
    • Jin, S.L.C.1    Swinnen, J.V.2    Conti, M.3
  • 34
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • Thompson, W. J., and M. M. Appleman. Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry 10:311-316 (1971).
    • (1971) Biochemistry , vol.10 , pp. 311-316
    • Thompson, W.J.1    Appleman, M.M.2
  • 36
    • 0029096745 scopus 로고
    • Structural and thermotropic properties of calcium-dimyristoylphosphatidic acid complexes at acidic and neutral pH conditions
    • Takahashi, H., T. Yasue, K. Ohki, and I. Hatta. Structural and thermotropic properties of calcium-dimyristoylphosphatidic acid complexes at acidic and neutral pH conditions. Biophys. J. 69:1464-1472 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 1464-1472
    • Takahashi, H.1    Yasue, T.2    Ohki, K.3    Hatta, I.4
  • 37
    • 0028865692 scopus 로고
    • A novel phosphatidylserine-binding peptide motif defined by an anti- Idiotypic monoclonal antibody
    • Igarashi, K., M. Kaneda, A. Yamaji, T. C. Saido, U. Kikkawa, Y. Ono, K. Inoue, and M. Umeda. A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody. J. Biol. Chem. 270: 29075-29078 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 29075-29078
    • Igarashi, K.1    Kaneda, M.2    Yamaji, A.3    Saido, T.C.4    Kikkawa, U.5    Ono, Y.6    Inoue, K.7    Umeda, M.8
  • 38
    • 0029003452 scopus 로고
    • Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase
    • Venema, R. C., H. S. Sayegh, J. F. Arnal, and D. G. Harrison. Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase. J. Biol. Chem. 270:14705-14711 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14705-14711
    • Venema, R.C.1    Sayegh, H.S.2    Arnal, J.F.3    Harrison, D.G.4
  • 39
    • 0017120832 scopus 로고
    • Calcium-dependent cyclic nucleotide phosphodiesterase from brain: Identification of phospholipids as calcium-independent activators
    • Wolff, D. J., and C. O. Brostrom. Calcium-dependent cyclic nucleotide phosphodiesterase from brain: identification of phospholipids as calcium-independent activators. Arch. Biochem. Biophys. 173:720-731 (1976).
    • (1976) Arch. Biochem. Biophys. , vol.173 , pp. 720-731
    • Wolff, D.J.1    Brostrom, C.O.2
  • 40
    • 0017647184 scopus 로고
    • Cyclic nucleotide phosphodiesterase: Stimulation of bovine brain cytoplasmic enzyme by lysophosphatidylcholine
    • Pichard, A. L., and W. Y. Cheung. Cyclic nucleotide phosphodiesterase: stimulation of bovine brain cytoplasmic enzyme by lysophosphatidylcholine. J. Biol. Chem. 252:4872-4875 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 4872-4875
    • Pichard, A.L.1    Cheung, W.Y.2
  • 41
    • 0021079778 scopus 로고
    • Comparison of phospholipid effects on insulin-sensitive low Km cyclic AMP phosphodiesterase in adipocyte plasma membranes and microsomes
    • Macaulay, S. L., F. L. Kiechle, and L. Jarett. Comparison of phospholipid effects on insulin-sensitive low Km cyclic AMP phosphodiesterase in adipocyte plasma membranes and microsomes. Biochim. Biophys. Acta 760: 293-299 (1983).
    • (1983) Biochim. Biophys. Acta , vol.760 , pp. 293-299
    • Macaulay, S.L.1    Kiechle, F.L.2    Jarett, L.3
  • 42
    • 0028787790 scopus 로고
    • Phospholipid regulation of a cyclic AMP-specific phosphodiesterase (PDE4) from U937 cells
    • Di Santo, M. E., K. B. Glaser, and R. J. Heaslip. Phospholipid regulation of a cyclic AMP-specific phosphodiesterase (PDE4) from U937 cells. Cell. Signalling 7:827-835 (1995).
    • (1995) Cell. Signalling , vol.7 , pp. 827-835
    • Di Santo, M.E.1    Glaser, K.B.2    Heaslip, R.J.3
  • 43
    • 0030006920 scopus 로고    scopus 로고
    • Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase: Involvement of serine 54 in the activation
    • Sette, C., and M. Conti. Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase: involvement of serine 54 in the activation. J. Biol. Chem. 271:16526-16534 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16526-16534
    • Sette, C.1    Conti, M.2
  • 44
    • 0028952293 scopus 로고
    • Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C
    • Yang, L., and M. Glaser. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry 34:1500-1506 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1500-1506
    • Yang, L.1    Glaser, M.2
  • 45
    • 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 46:512-523 (1991).
    • (1991) Thorax , vol.46 , pp. 512-523
    • Torphy, T.J.1    Undem, B.J.2


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