Negative regulation of γ-globin gene expression by cyclic AMP-dependent pathway in erythroid cells

Experimental Hematology

Volumn 32, Issue 3, 2004, Pages 244-253

  Inoue, Akio ^a   Kuroyanagi, Yuichi ^a   Terui, Kiminori ^a   Moi, Paolo ^b   Ikuta, Tohru ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Regional Thalassemia Hospital   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

1H 1,2,4 OXADIAZOLO[4,3 A]QUINOXALIN 1 ONE; 8 BROMO CYCLIC AMP; 9 (TETRAHYDRO 2 FURYL)ADENINE; ADENYLATE CYCLASE ACTIVATOR; ALPHA GLOBIN; ARGININE; BUTYRIC ACID; CYCLIC AMP; FORSKOLIN; HEMIN; HYDROXYUREA; KT 5720; KT 5823; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHODIESTERASE III; PROSTAGLANDIN E1;

ARTICLE; CELL STRAIN K 562; CONTROLLED STUDY; DRUG EFFECT; ENZYME PHOSPHORYLATION; ERYTHROID CELL; GENE EXPRESSION REGULATION; GENETIC ANALYSIS; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; REPORTER GENE; SIGNAL TRANSDUCTION; TRANSCRIPTION INITIATION;

3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; 8-BROMO CYCLIC ADENOSINE MONOPHOSPHATE; ADENINE; ADENYLATE CYCLASE; CYCLIC AMP; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYCLIC GMP; ERYTHROID PROGENITOR CELLS; FORSKOLIN; GENE EXPRESSION REGULATION; GLOBINS; HEMIN; HUMANS; K562 CELLS; MAP KINASE SIGNALING SYSTEM; PHOSPHORYLATION; PROMOTER REGIONS (GENETICS); RNA, MESSENGER; SIGNAL TRANSDUCTION; TRANSCRIPTION, GENETIC;

EID: 1542267418     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exphem.2003.12.006     Document Type: Article

References (72)

1. May C., Rivella S., Callegari J., et al. Therapeutic haemoglobin synthesis in beta-thalassaemic mice expressing lentivirus-encoded human beta-globin. Nature. 406:2000;82-86.
2. Pawliuk R., Westerman K.A., Fabry M.E., et al. Correction of sickle cell disease in transgenic mouse models by gene therapy. Science. 294:2001;2368-2371.
3. Walters M.C., Storb R., Patience M., et al. Impact of bone marrow transplantation for symptomatic sickle cell disease: an interim report. Blood. 95:2000;1918-1924.
4. Dover G.J., Charache S. Hydroxyurea induction of fetal hemoglobin synthesis in sickle-cell disease. Semin Oncol. 19:1992;61-66.
5. Steinberg M.H. Sickle cell anemia and fetal hemoglobin. Am J Med Sci. 308:1994;259-265.
6. Powars D.R., Chan L., Schroeder W.A. Beta S-gene-cluster haplotypes in sickle cell anemia: clinical implications. Am J Pediatr Hematol Oncol. 12:1990;367-374.
7. Nagel R.L., Erlingsson S., Fabry M.E., et al. The Senegal DNA haplotype is associated with the amelioration of anemia in African-American sickle cell anemia patients. Blood. 77:1991;1371-1375.
8. Weatherall D.J. The Thalassemias. Stamatoyannopoulos G., Majerus P.W., Perlmutter R.M., Varmus H. The Molecular Basis of Blood Diseases. 3rd ed. 2001;183-226 WB Saunders, Philadelphia.
9. Jane S.M., Ney P.A., Vanin E.F., Gumucio D.L., Nienhuis A.W. Identification of a stage selector element in the human gamma-globin gene promoter that fosters preferential interaction with the 5′ HS2 enhancer when in competition with the beta-promoter. EMBO J. 11:1992;2961-2969.
10. Cunningham J.M., Purucker M.E., Jane S.M., et al. The regulatory element 3′ to the A gamma-globin gene binds to the nuclear matrix and interacts with special A-T-rich binding protein 1 (SATB1), an SAR/MAR-associating region DNA binding protein. Blood. 84:1994;1298-1308.
11. Navas P.A., Peterson K.R., Li Q., et al. Developmental specificity of the interaction between the locus control region and embryonic or fetal globin genes in transgenic mice with an HS3 core deletion. Mol Cell Biol. 18:1998;4188-4196.
12. Liu Q., Tanimoto K., Bungert J., Engel J.D. The A gamma-globin 3′ element provides no unique function(s) for human beta-globin locus gene regulation. Proc Natl Acad Sci USA. 95:1998;9944-9949.
13. Holmes M.L., Haley J.D., Cerruti L., et al. Identification of Id2 as a globin regulatory protein by representational difference analysis of K562 cells induced to express gamma-globin with a fungal compound. Mol Cell Biol. 19:1999;4182-4190.
14. Asano H., Li X.S., Stamatoyannopoulos G. FKLF, a novel Kruppel-like factor that activates human embryonic and fetal beta-like globin genes. Mol Cell Biol. 19:1999;3571-3579.
15. Pace B.S., Li Q., Stamatoyannopoulos G. In vivo search for butyrate responsive sequences using transgenic mice carrying A gamma gene promoter mutants. Blood. 88:1996;1079-1083.
16. Ikuta T., Atweh G., Boosalis V., et al. Cellular and molecular effects of a pulse butyrate regimen and new inducers of globin gene expression and hematopoiesis. Ann N Y Acad Sci. 850:1998;87-99.
17. Ikuta T., Kan Y.W., Swerdlow P.S., Faller D.V., Perrine S.P. Alterations in protein-DNA interactions in the gamma-globin gene promoter in response to butyrate therapy. Blood. 92:1998;2924-2933.
18. Pace B.S., Chen Y.R., Thompson A., Goodman S.R. Butyrate-inducible elements in the human gamma-globin promoter. Exp Hematol. 28:2000;283-293.
19. Kruh J. Effects of sodium butyrate, a new pharmacological agent, on cells in culture. Mol Cell Biochem. 42:1982;65-82.
20. Ikuta T., Ausenda S., Cappellini M.D. Mechanism for fetal globin gene expression: role of the soluble guanylate cyclase-cyclic GMP-dependent protein kinase pathway. Proc Natl Acad Sci USA. 98:2001;1847-1852.
21. Cokic V.P., Smith R.D., Beleslin-Cokic B.B., et al. Hydroxyurea induces fetal hemoglobin by the nitric oxide-dependent activation of soluble guanylyl cyclase. J Clin Invest. 111:2003;231-239.
22. Beavo J.A., Hansen R.S., Harrison S.A., et al. Identification and properties of cyclic nucleotide phosphodiesterases. Mol Cell Endocrinol. 28:1982;387-410.
23. Ikuta T., Kan Y.W. In vivo protein-DNA interactions at the beta-globin gene locus. Proc Natl Acad Sci USA. 88:1991;10188-10192.
24. Sievers G., Hakli H., Luhtala J., Tenhunen R. Optical and EPR spectroscopy studies on haem arginate, a new compound used for treatment of porphyria. Chem Biol Interact. 63:1987;105-114.
25. Yamamoto K.K., Gonzalez G.A., Menzel P., Rivier J., Montminy M.R. Characterization of a bipartite activator domain in transcription factor CREB. Cell. 60:1990;611-617.
26. Klingmüller U., Lorenz U., Cantley L.C., Neel B.G., Lodish H.F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell. 80:1995;729-738.
27. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 162:1987;156-159.
28. Andrews N.C., Faller D.V. A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells. Nucleic Acids Res. 19:1991;2499.
29. Locker J., Buzard G. A dictionary of transcription control sequences. DNA Seq. 1:1990;3-11.
30. Montminy M.R., Bilezikjian L.M. Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene. Nature. 328:1987;175-178.
31. Ikuta T., Papayannopoulou T., Stamatoyannopoulos G., Kan Y.W. Globin gene switching. In vivo protein-DNA interactions of the human beta-globin locus in erythroid cells expressing the fetal or the adult globin gene program. J Biol Chem. 271:1996;14082-14091.
32. Groudine M., Peretz M., Weintraub H. Transcriptional regulation of hemoglobin switching in chicken embryos. Mol Cell Biol. 1:1981;281-288.
33. Moi P., Kan Y.W. Synergistic enhancement of globin gene expression by activator protein-1-like proteins. Proc Natl Acad Sci USA. 87:1990;9000-9004.
34. Denamur E., Chehab F.F. Analysis of the mouse and rat CFTR promoter regions. Hum Mol Genet. 3:1994;1089-1094.
35. Wechsler J., Choi Y.H., Krall J., et al. Isoforms of cyclic nucleotide phosphodiesterase PDE3A in cardiac myocytes. J Biol Chem. 277:2002;38072-38078.
36. Beavo J.A. Cyclic nucleotide phosphodiesterases: functional implications of multiple isoforms. Physiol Rev. 75:1995;725-748.
37. Yamamoto K.K., Gonzalez G.A., Biggs W.H.D., Montminy M.R. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature. 334:1988;494-498.
38. Lamph W.W., Dwarki V.J., Ofir R., Montminy M., Verma I.M. Negative and positive regulation by transcription factor cAMP response element-binding protein is modulated by phosphorylation. Proc Natl Acad Sci USA. 87:1990;4320-4324.
39. Beckman B., Mirand E., Fisher J.W. Effects of beta adrenergic agents and prostaglandin E1 on erythroid colony (CFU-E) growth and cyclic AMP formation in Friend erythroleukemic cells. J Cell Physiol. 105:1980;355-361.
40. Ignarro L.J. Regulation of cytosolic guanylyl cyclase by porphyrins and metalloporphyrins. Adv Pharmacol. 26:1994;35-65.
41. Garthwaite J., Southam E., Boulton C.L., et al. Potent and selective inhibition of nitric oxide-sensitive guanylyl cyclase by 1H-[1,2,4]oxadiazolo[4, 3-a]quinoxalin-1-one. Mol Pharmacol. 48:1995;184-188.
42. Gadbois D.M., Crissman H.A., Tobey R.A., Bradbury E.M. Multiple kinase arrest points in the G1 phase of nontransformed mammalian cells are absent in transformed cells. Proc Natl Acad Sci USA. 89:1992;8626-8630.
43. Harris D.N., Asaad M.M., Phillips M.B., Goldenberg H.J., Antonaccio M.J. Inhibition of adenylate cyclase in human blood platelets by 9-substituted adenine derivatives. J Cyclic Nucleotide Res. 5:1979;125-134.
44. Rivero J.A., Adunyah S.E. Sodium butyrate induces tyrosine phosphorylation and activation of MAP kinase (ERK-1) in human K562 cells. Biochem Biophys Res Commun. 224:1996;796-801.
45. Witt O., Sand K., Pekrun A. Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways. Blood. 95:2000;2391-2396.
46. Park J.I., Choi H.S., Jeong J.S., Han J.Y., Kim I.H. Involvement of p38 kinase in hydroxyurea-induced differentiation of K562 cells. Cell Growth Differ. 12:2001;481-486.
47. Woessmann W., Mivechi N.F. Role of ERK activation in growth and erythroid differentiation of K562 cells. Exp Cell Res. 264:2001;193-200.
48. Deak M., Clifton A.D., Lucocq L.M., Alessi D.R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17:1998;4426-4441.
49. Leonard W.J., O'Shea J.J. Jaks and STATs: biological implications. Annu Rev Immunol. 16:1998;293-322.
50. Cobb M.H. MAP kinase pathways. Prog Biophys Mol Biol. 71:1999;479-500.
51. Ihle J.N. The Stat family in cytokine signaling. Curr Opin Cell Biol. 13:2001;211-217.
52. Nichols M., Weih F., Schmid W., et al. Phosphorylation of CREB affects its binding to high and low affinity sites: implications for cAMP induced gene transcription. EMBO J. 11:1992;3337-3346.
53. Weinberg R.S., Ji X., Sutton M., et al. The rapid increase in gamma-globin chain synthesis in butyate responsive sickle cell (SCD) patients may be mediated by translational mechanisms. Blood. 98:2001;751. Abstract 3126.
54. Witt O., Monkemeyer S., Ronndahl G., et al. Induction of fetal hemoglobin expression by the histone deacetylase inhibitor apicidin. Blood. 101:2003;2001-2007.
55. Bhanu N.V., Trice T.A., Lee Y.T., Miller J.L. Stem cell factor increases fetal hemoglobin production through activation of MEK and p44 MAPK. Blood. 100:2002;118. Abstract 438.
56. Ben-Neriah Y., Daley G.Q., Mes-Masson A.M., Witte O.N., Baltimore D. The chronic myelogenous leukemia-specific P210 protein is the product of the bcr/ abl hybrid gene. Science. 233:1986;212-214.
57. Wong S., McLaughlin J., Cheng D., Witte O.N. Cell context-specific effects of the BCR-ABL oncogene monitored in hematopoietic progenitors. Blood. 101:2003;4088-4097.
58. de Rooij J., Zwartkruis F.J., Verheijen M.H., et al. Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature. 396:1998;474-477.
59. Li X., Zarinetchi F., Schrier R.W., Nemenoff R.A. Inhibition of MAP kinase by prostaglandin E2 and forskolin in rat renal mesangial cells. Am J Physiol. 269:1995;C986-C991.
60. Rao K.M. MAP kinase activation in macrophages. J Leukoc Biol. 69:2001;3-10.
61. Rincon M. MAP-kinase signaling pathways in T cells. Curr Opin Immunol. 13:2001;339-345.
62. Nahavandi M., Tavakkoli F., Wyche M.Q., et al. Nitric oxide and cyclic GMP levels in sickle cell patients receiving hydroxyurea. Br J Haematol. 119:2002;855-857.
63. Costa F.F., Conran N., Acosta H.C., Fattori A., Saad S.T.O. Sickle red blood cells possess elevated levels of cGMP: a possible mechanism for fetal hemoglobin production? Blood. 100:2002;665. Abstract 2615.
64. Polson J.B., Strada S.J. Cyclic nucleotide phosphodiesterases and vascular smooth muscle. Annu Rev Pharmacol. 36:1996;403-427.
65. Longmore G.D., Pharr P.N., Lodish H.F. A constitutively activated erythropoietin receptor stimulates proliferation and contributes to transformation of multipotent, committed nonerythroid and erythroid progenitor cells. Mol Cell Biol. 14:1994;2266-2277.
66. Suhasini M., Boss G.R., Pascual F.E., Pilz R.B. Nitric oxide-releasing agents and cGMP analogues inhibit murine erythroleukemia cell differentiation and suppress erythroid-specific gene expression: correlation with decreased DNA binding of NF-E2 and altered c-myb mRNA expression. Cell Growth Differ. 6:1995;1559-1566.
67. Tabuse Y., Furusawa M., Eisen H., Shibata K. Prostaglandin E1, an inducer of erythroid differentiation of Friend erythroleukemia cells. Exp Cell Res. 108:1977;41-45.
68. Taxman D.J., Wojchowski D.M. Erythropoietin-induced transcription at the murine beta maj-globin promoter. A central role for GATA-1. J Biol Chem. 270:1995;6619-6627.
69. Pilz R.B., Eigenthaler M., Boss G.R. Chemically induced murine erythroleukemia cell differentiation is severely impaired when cAMP-dependent protein kinase activity is repressed by transfected genes. J Biol Chem. 267:1992;16161-16167.
70. Pilz R.B. Impaired erythroid-specific gene expression in cAMP-dependent protein kinase-deficient murine erythroleukemia cells. J Biol Chem. 268:1993;20252-20258.
71. O'Dorisio M.S., Fertel R., Finkler E., Brooks R., Vassalo L. Characterization of cyclic nucleotide metabolism during human monocyte differentiation. J Leukoc Biol. 35:1984;617-630.
72. Ledbetter J.A., Parsons M., Martin P.J., et al. Antibody binding to CD5 (Tp67) and Tp44 T cell surface molecules: effects on cyclic nucleotides, cytoplasmic free calcium, and cAMP-mediated suppression. J Immunol. 137:1986;3299-3305.