Regulation of IRF and STAT Gene Expression by Retinoic Acid

References

• Lotan R. Retinoids in cancer chemoprevention. FASEB J. 1996; 10.: 1031–1039
   PubMed Web of Science ®Google Scholar
• Borden E. C. Interferons-expanding therapeutic roles. N. Engl. J. Med. 1992; 326: 1491–1493
   PubMed Web of Science ®Google Scholar
• Cirelli R., Tyring S. Major therapeutic uses of interferons. Clin. Immunother. 1995; 3: 27–87
   Google Scholar
• Eisenhauer E. A., Lippman S. M., Cavanagh J. J., Parades-Espinoza M., Arnold A., Hong W. K., Massimini G., Schleuniger U., Bollag W., Holdener E. E., Krakoff I. Combination of 13-cis-retinoic acid and interferon α-2a in therapy of solid tumors. Leukemia 1993; 8: 1622–1625
   Web of Science ®Google Scholar
• Chambon P. A decade of molecular biology of retinoic acid receptors. FASEB J. 1996; 10: 940–954
   PubMed Web of Science ®Google Scholar
• De The H. Altered retinoic acid receptors. FASEB J. 1996; 10: 955–960
   PubMed Web of Science ®Google Scholar
• Chomienne C., Fenaux P., Degos L. Retinoid differentiation therapy in promyelocytic leukemia. FASEB J. 1996; 10: 1025–1030
   PubMed Web of Science ®Google Scholar
• Grignani F., Fermcci P. F., Testa U., Talamo G., Fagioli M., Alcalay M., Mencarelli A., Grignani F., Peschle C., Nicoletti I., Pelicci P. G. The acute promyelocytic-specific PML-RARa fusion protein inhibits differentiation and promotes survival of myeloid precursor cells. Cell 1993; 74: 423–431
   PubMed Web of Science ®Google Scholar
• Rousselot P., Hardas B., Patel A., Guidez F., Giken J., Castaigne S., Dejean A., De The H., Degos L., Farzaneh F., Chomienne C. The PML-RARa gene product of the t(15.17) translocation inhibits retinoic acid-induced granulocytic differentiation and mediated transactivation in human myeloid cells. Oncogene 1994; 9: 545–551
   PubMed Web of Science ®Google Scholar
• Lanotte M., Martin-Thouvenin V., Najman S., Balerini P., Valensi F., Berger R. NB4, a maturation inducible cell line with t(15; 17) marker isolated from a human acute promyelocytic leukemia (M3). Blood 1991; 77: 1080–1086
   PubMed Web of Science ®Google Scholar
• Huang M., Ye Y. C., Chen B. R., Chai J. R., Lu J. X., Zhoa L., Gu L. J., Wang Z. Y. Use of all-trans-retinoic acid in the treatment of acute promyelocytic leukemia. Blood 1988; 72: 567–572
   PubMed Web of Science ®Google Scholar
• Castaigne S., Chomienne C., Daniel M. T., Ballerini P., Berger R., Fenaux P., Degos L. All-trans-retinoic acid as a differentiation theraphy for acute promyelocytic leukemia. I. Clinical results. Blood 1990; 76: 1704–1709
   PubMed Web of Science ®Google Scholar
• Warrell R. P., Frankel S. R., Miller W. H., Scheinberg D. A., Itri L. M., Hittelman M. N., Vyas R., Andreeff M., Tafuri A., Jakubowski A., Gabrilove J., Gordon M. S. Differentiation therapy for acute promyelocytic leukemia with tretinoin (all-trans-retinoic acid). N. Engl. J. Med. 1991; 324: 1385–1393
   PubMed Web of Science ®Google Scholar
• Harada H., Fujita T., Miyamoto M., Kimura Y., Maruyama M., Furia A., Miyata T., Taniguchi T. Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN inducible genes. Cell 1989; 58: 729–739
   PubMed Web of Science ®Google Scholar
• Pine R., Decker T., Kessler D. S., Levy D. E., Darnell J. E., Jr. Purification and cloning of interferon-stimulated gene factor 2 (ISGF2): ISGF2 (IRF-1) can bind to the promoters of both beta-interferon and interferon-stimulated genes but is not a primary transcriptional activator of either. Mol. Cell. Biol. 1990; 10: 248–2457
   Google Scholar
• Maruyama M., Fujita T., Taniguchi T. Sequence of a cDNA coding for human IRF-I. Nucleic Acids Res. 1989; 17: 3292
   PubMed Web of Science ®Google Scholar
• Itoh S., Harada H., Fujita T., Mimura T., Taniguchi T. Sequence of a cDNA coding for human IRF-2. Nucleic Acids Res. 1989; 17: 8372
   PubMed Web of Science ®Google Scholar
• Au W-C., Moore P. A., Lowther W., Juang Y-T, Pitha P. M. Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes. Proc. Natl. Acad. Sci. 1995; 92: 11657–11661
   PubMed Web of Science ®Google Scholar
• Yamagata T., Nishida J., Tanaka T., Sakai R., Mitani K., Yoshida M., Taniguchi T., Yazaki Y., Hirai H. A novel interferon regulatory factor family transcription factor, ICSAT/Pip/LSIRF, that negatively regulates the activity of interferon-regulated genes. Mol. Cell. Biol. 1996; 16: 1283–1294
   PubMed Web of Science ®Google Scholar
• Veals S. A., Schindler C., Leonard D., Fu X-Y., Aebersold R., Darnell J. E., Jr., Levy D. E. Subunit of an alpha-interferon-responsive transcription factor is related to interferon regulatory factor and myb families of DNA-binding proteins. Mol. Cell. Biol. 1992; 12: 3315–3324
   PubMed Web of Science ®Google Scholar
• Weiz A., Marx P., Sharf R., Appella E., Driggers P. H., Ozato K., Levi B-Z. Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes. J. Biol. Chem. 1992; 267: 25589–25596
   PubMed Web of Science ®Google Scholar
• Driggers P. H., Elenbaas B. A., An J.-B., Lee I. J., Ozato K. Two upstream elements activate transcription of major histocompability complex class I gene in vitro. Nucleic Acids Res. 1992; 20: 2533–2540
   PubMed Web of Science ®Google Scholar
• Matsuyama T., Grossman A., Mittrucker H. W., Siderovski D. P., Kiefer F., Kawakami T., Richardson C. D., Taniguehi T., Yoshinaga S. K., Mak T. W. Molecular cloning of LSIRF, a lymphoid-specific member of the inteferon regulatory factor family that binds the interferon-stimulated response element (ISRE). Nucleic Acids Res. 1995; 23: 2127–2136
   PubMed Web of Science ®Google Scholar
• Eisenbeis C. F., Singh H., Storb U. Pip, a novel IRF family member, is a lymphoid-specific, PU. 1-dependent transcriptional activator. Genes Dev. 1995; 9: 1377–1387
   PubMed Web of Science ®Google Scholar
• Mittrucker H-W., Matsuyama T., Grossman A., Kundig T. M., Potter J., Shahinian A., Wakeham A., Patterson B., Ohashi P. S., Mak T. W. Requirement for the transcription factor LSIRF/IRF4 for mature B and T lymphocyte function. Science 1997; 275: 540–543
   PubMed Web of Science ®Google Scholar
• Bluyssen H. A. R., Durbin J. E., Levy D. E. ISGF3γ p48, a specificity switch for interferon activated transcription factors. Cytokine and Growth Factor Reviews 1996; 7: 11–17
   PubMedGoogle Scholar
• Tanaka N., Kawakami T., Taniguehi T. Recognition DNA sequences of inteferon regulatory factor 1 (IRF-1) and IRF-2, regulators of cell growth and the interferon system. Mol. Cell. Biol. 1993; 13: 4531–4538
   PubMed Web of Science ®Google Scholar
• Kimura T., Kadokawa Y., Harada H., Matsumoto M., Sato M., Kashiwazaki Y., Tarutani M., Sok-Pin Tan R., Takasugi T., Matsuyama T., Mak T. W., Noguchi S., Taniguehi T. Essential and non-redundant roles of p48 (ISGF3y) and IRF-1 in both type I and type II inteferon responses, as revealed by gene targeting studies. Genes to Cells 1996; 1: 115–124
   PubMed Web of Science ®Google Scholar
• Bovolenta C., Driggers P. H., Marks M. S., Medin J. A., Poltis A. D., Vogel S. N., Levy D. E., Sakaguchi K., Appella E., Coligan I. E., Ozato K. Molecular interactions between interferon consensus sequence binding protein and members of the interferon regulatory factor family. Proc. Natl. Acad. Sci. 1994; 91: 5046–5050
   PubMed Web of Science ®Google Scholar
• Sharf R., Meraro D., Azriel A., Thornton A. M., Ozato K., Petricoin E. F., Schaper F., Hauser H., Levi B. Z. Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA. J. Biol. Chem. 1997; 272: 9785–9792
   PubMed Web of Science ®Google Scholar
• Taniguehi T., Harada H., Lamphier M. Regulation of the interferon system and cell growth by the IRF transcription factors. J Cancer Res. Clin. Oncol. 1995; 121: 516–520
   PubMed Web of Science ®Google Scholar
• Harada H., Kitagawa M., Tanaka N., Yamamoto H., Harada K., Ishihara M., Taniguehi T. Anti-oncogenic and oncogenic potentials of interferon regulatory factors-1 and-2. Science 1993; 259: 971–974
   PubMed Web of Science ®Google Scholar
• Tanaka N., Ishihara M., Kitagawa M., Harada H., Kimura T., Matsuyama T., Lamphier M. S., Aizawa S., Mak T. W., Taniguehi T. Cellular commitment to oncogene-induced transformation or apoptosis is dependent on the transcription factor IRF-1. Cell 1993; 77: 829–839
   Web of Science ®Google Scholar
• Tamura T., Ishihara M., Lamphier M. S., Tanaka N., Oishi I., Aizawa S., Matsuyama T., Mak T. W., Taki S., Taniguehi T. An IRF-1 dependent pathway of DNA-damage induced apoptosis in mitogen activated T-lymphocytes. Nature 1995; 376: 596–599
   PubMed Web of Science ®Google Scholar
• Willman C. L., Sever C. E., Pallavicini M. G., Harada H., Tanaka N., Slovak M. L., Yamamoto H., Harada K., Meeker T. C., List A. F., Taniguehi T. Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia. Science 1993; 259: 968–971
   PubMed Web of Science ®Google Scholar
• Holtschke T., LÖHler J., Kanno Y., Fehr T., Giese N., Rosenbauer F., Lou J., Knobeloch K-P., Gabriele L., Waring J. F., Bachmann M. F., Zinkernagel R. M., Morse H. C., III, Ozato K., Horak I. Immunodeficiency and chronic myelogenous leukemia-like syndrome in mice with a targeted mutation of the ICSBP gene. Cell 1996; 87: 307–317
   PubMed Web of Science ®Google Scholar
• Matikainen S., Ronni T., Hurme M., Pine R., Julkunen I. Retinoic acid activates interferon regulatory factor-1 gene expression in myeloid cells. Blood 1996; 88: 114–123
   PubMed Web of Science ®Google Scholar
• Gianni M., Terao M., Fortino I., Licalzi M., Viggiano V., Barbui T., Rambaldi A., Garattini E. Stat1 is induced and activated by all-trans retinoic acid in acute promyelocytic leukemia cells. Blood 1997; 89: 1001–1012
   PubMed Web of Science ®Google Scholar
• Giandomenico V., Lancillotti F., Fioruggi G., Percario Z. A., Rivabene R., Malorni W., Affabris E., Romeo G. Retinoic acid and IFN inhibition of cell proliferation is associated with apoptosis in squamous carcinoma cell lines: role of IRF-1 and TGase II-dependent pathways. Cell Growth & Differ. 1997; 8: 91–100
   PubMedGoogle Scholar
• Sims S. H., Cha Y., Romine M. F., Gao P.-Q., Gottlieb K., Deisseroth A. A novel interferon-inducible domain: structural and functional analysis of the human interferon regulatory factor 1 gene promoter. Mol. Cell. Biol. 1993; 13: 690–702
   PubMed Web of Science ®Google Scholar
• Pine R., Canova A., Schindler C. Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFNα and IFGγ, and is likely to autoregulate the p91 gene. EMBO J. 1994; 13: 158–167
   PubMed Web of Science ®Google Scholar
• Lehtonen A., Matikainen S., Julkunen I. Interferons upregulate STAT1, STAT2, and IRF family transcription factor gene expression in human peripheral blood mononuclear cells and macrophages. J. Immunol. 1997; 14: 794–803
   Google Scholar
• Ohmori Y., Schreiber R. D., Hamilton T. A. Synergy between interferon-gamma and tumor necrosis factor-alpha in transcriptional activation is mediated by cooperation between signal transducer and activator of transcription 1 and nuclear factor kappaB. J. Biol. Chem. 1997; 272: 14899–14907
   PubMed Web of Science ®Google Scholar
• Matikainen S., Ronni T., Lehtonen A., Sareneva T., Melen K., Nordlin S., Levy D. E., Julkunen I. Retinoic acid induces signal transducers and activator of transcription (STAT) 1, STAT2, and p48 expression in myeloid leukemia cells and enhances their responsiveness to interferons. Cell Growth & Differ. 1997; 8: 687–698
   PubMedGoogle Scholar
• Kolla V., Lindner D. J., Weihua X., Borden E. C., Kalvakolanu D. J. Modulation of interferon (IFN)-inducible gene expression by retinoic acid. J. Biol. Chem. 1996; 271: 10508–10514
   PubMed Web of Science ®Google Scholar
• Xu B., Grander D., Sangfelt O., Einhorn S. Primary leukemia cells resistant to α-interferon in vitro are defective in the activation of the DNA-binding factor interferon-stimulated gene factor 3. Blood 1994; 84: 1942–1949
   PubMed Web of Science ®Google Scholar
• Watanabe N., Sakakibara J., Hovanessian A. G., Taniguehi T., Fujita T. Activation of IFN-β element by IRF-1 requires a posttranslational event in addition to IRF-1 synthesis. Nucleic Acids Res. 1991; 19: 4421–4428
   PubMed Web of Science ®Google Scholar
• Nagata S. Apoptosis by death factor. Cell 1997; 88: 355–365
   PubMed Web of Science ®Google Scholar
• Tanaka N., Ishihara M., Lamphier M. S., Nozawa H., Matsuyama T., Mak T. W., Aizawa S., Tokino T., Oren M., Taniguchi T. Cooperation of the tumor suppressors IRF-1 and p53 in response to DNA damage. Nature 1996; 382: 816–818
   PubMed Web of Science ®Google Scholar
• Kamijo R., Harada H., Matsuyama T., Bosland M., Gerecitano J., Shapiro D., Le J., Koh S. J., Kimura T., Green S. J., Mak T. W., Taniguchi T., Vilcek J. Requirement for transcription factor IRF-1 in NO synthase induction in macrophages. Science 1994; 263: 1612–1615
   PubMed Web of Science ®Google Scholar
• Moilanen E., Vapaatalo H. Nitric oxide in inflammation and immune response. Ann. Med. 1995; 27: 359–367
   PubMed Web of Science ®Google Scholar
• Albina J. E., Abate J. A., Henry W. L. Nitric oxide production is required for murine resident peritoneal macrophages to suppress mitogen-stimulated T-cell proliferation: a role of IFN-gamma in the induction of nitric oxide synthesizing pathway. J. Immunol. 1991; 147: 1441–1448
   Google Scholar
• Mills C. D. Molecular basis of “suppressor” macrophages: arginine metabolism via the nitric oxide synthase pathway. J. Immunol. 1991; 146: 2719–2723
   PubMed Web of Science ®Google Scholar