Navegar

Colección

Datos Estadísticas

Artículo

Este artículo es de Acceso Abierto y puede ser descargado en su versión final desde nuestro repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Although hypoxia-inducible factor-α (HIFα) subunit-specific hydroxylation and proteolytic breakdown explain the binary switch between the presence (hypoxia) and absence (normoxia) of HIFs, little is known of the mechanisms that fine-tune HIF activity under constant, rather than changing, oxygen tensions. Here, we report that the Drosophila HIFα homolog, the basic helix-loop-helix/PAS protein Sima (Similar), in hypoxic cultures of SL2 cells is expressed in full-length (fl) and splice variant (sv) isoforms. The following evidence supports the role of flSima as functional HIFα and the role of SL2 HIF as a transcriptional activator or suppressor. The pO2 dependence of Sima abundance matched that of HIF activity. HIF-dependent changes in candidate target gene expression were detected through variously effective stimuli: hypoxia (strong) > iron chelation, e.g. desferrioxamine (moderate) ≪ transition metals, e.g. cobalt ≃ normoxia (ineffective). Sima overexpression augmented hypoxic induction or suppression of different targets. In addition to the full-length exon 1-12 transcript yielding the 1510-amino acid HIFα homolog, the sima gene also expressed, specifically under hypoxia, an exon 1-7/12 splice variant, which translated into a 426-amino acid Sima truncation termed svSima. svSima contains basic helix-loop-helix and PAS sequences identical to those of flSima, but, because of deletion of exons 8-11, lacks the oxygen-dependent degradation domain and nuclear localization signals. Overexpressed svSima failed to transactivate reporter genes. However, it attenuated HIF (Sima-Tango)-stimulated reporter expression in a dose-dependent manner. Thus, svSima has the potential to regulate Drosophila HIF function under steady and hypoxic pO2 by creating a cytosolic sink for the Sima partner protein Tango.

Registro:

Documento: Artículo
Título:Regulation of Drosophila hypoxia-inducible factor (HIF) activity in SL2 cells: Identification of a hypoxia-induced variant isoform of the HIFα homolog gene similar
Autor:Gorr, T.A.; Tomita, T.; Wappner, P.; Bunn, H.F.
Filiación:Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, United States
Instituto Leloir, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Patricias Argentinas 435, Buenos Aires 1405, Argentina
Dept. of Medicine, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Ave., Boston, MA 02115, United States
Palabras clave:Amino acids; Chelation; Genes; Hydroxylation; Iron; Iron chelation; Sima genes; Cell culture; amino acid; cobalt; complementary DNA; deferoxamine; erythropoietin; helix loop helix protein; hypoxia inducible factor 1alpha; iron; luciferase; messenger RNA; metal; oxygen; PAS protein; protein Tango; RNA; Sima protein; unclassified drug; animal cell; article; controlled study; Drosophila; gene overexpression; genetic transfection; hydroxylation; hypoxia; hypoxia response element; molecular cloning; nonhuman; Northern blotting; open reading frame; oxygen tension; priority journal; protein degradation; protein localization; reporter gene; reverse transcription polymerase chain reaction; RNA isolation; signal transduction; transcription regulation; untranslated region; Western blotting; Amino Acid Sequence; Animals; Aryl Hydrocarbon Receptor Nuclear Translocator; Carrier Proteins; Cell Hypoxia; Cell Line; DNA-Binding Proteins; Drosophila; Drosophila Proteins; Gene Expression Regulation; Humans; Hypoxia-Inducible Factor 1, alpha Subunit; Molecular Sequence Data; Sequence Homology; Signal Transduction; Transcription Factors; Animalia
Año:2004
Volumen:279
Número:34
Página de inicio:36048
Página de fin:36058
DOI: http://dx.doi.org/10.1074/jbc.M405077200
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:amino acid, 65072-01-7; cobalt, 7440-48-4; deferoxamine, 70-51-9; erythropoietin, 11096-26-7; iron, 14093-02-8, 53858-86-9, 7439-89-6; oxygen, 7782-44-7; RNA, 63231-63-0; Aryl Hydrocarbon Receptor Nuclear Translocator, 138391-32-9; Carrier Proteins; DNA-Binding Proteins; Drosophila Proteins; HIF1A protein, human; Hypoxia-Inducible Factor 1, alpha Subunit; Sima protein, Drosophila; tango protein, Drosophila; Transcription Factors
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00219258_v279_n34_p36048_Gorr.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v279_n34_p36048_Gorr

Referencias:

  • Bunn, H.F., Poyton, R.O., (1996) Physiol. Rev., 76, pp. 839-885
  • Hochachka, P.W., Buck, L.T., Doll, C.J., Land, S.C., (1996) Proc. Natl. Acad. Sci. U. S. A., 93, pp. 9493-9498
  • Hochachka, P.W., (1986) Science, 231, pp. 234-241
  • Wegener, G., (1988) Oxygen Sensing in Tissues, pp. 13-35. , (Acker, H., ed), Springer-Verlag, Berlin
  • Wegener, G., (1993) Surviving Hypoxia: Mechanisms of Control and Adaptation, pp. 417-434. , (Hochachka, P. W., Lutz, P. L., Sick, T., Rosenthal, M., and van den Thillart, G., eds), CRC Press LLC, Boca Raton, FL
  • Haddad, G.G., (2000) J. Appl. Physiol., 88, pp. 1481-1487
  • Csik, L., (1939) Z. Vgl. Physiol., 27, pp. 304-310
  • Chadwick, L.E., Gilmour, D., (1940) Physiol. Zool., 13, pp. 398-410
  • Keister, M., Buck, J., (1974) The Physiology of Insecta, 6, pp. 469-509. , (Rockstein, M., ed) 2nd Ed., Academic Press, Inc., New York
  • Loudon, C., (1988) J. Insect Physiol., 34, pp. 97-103
  • Wingrove, J.A., O'Farrell, P.H., (1999) Cell, 98, pp. 105-114
  • Krishnan, S.N., Sun, Y.-A., Mohsenin, A., Wyman, R.J., Haddad, G.G., (1997) J. Insect Physiol., 43, pp. 203-210
  • Grieshaber, M.K., Hardewig, I., Kreutzer, U., Pörtner, H.-O., (1994) Rev. Physiol. Biochem. Pharmacol., 125, pp. 43-147
  • Foe, V.E., Alberts, B.M., (1985) J. Cell Biol., 100, pp. 1623-1636
  • Douglas, R.M., Xu, T., Haddad, G.G., (2001) Amer. J. Physiol., 280, pp. R1555-R1563
  • DiGregorio, P.J., Ubersax, J.A., O'Farrell, P.H., (2001) J. Biol. Chem., 276, pp. 1930-1937
  • Wigglesworth, V.B., (1954) Q. J. Microsc. Sci., 95, pp. 115-137
  • Locke, M., (1958) Q. J. Microsc. Sci., 99, pp. 373-391
  • Jarecki, J., Johnson, E., Krasnow, M.A., (1999) Cell, 99, pp. 211-220
  • Metzger, R.J., Krasnow, M.A., (1999) Science, 284, pp. 1635-1639
  • Klagsbrun, M., Knighton, D., Folkman, J., (1976) Cancer Res., 36, pp. 110-114
  • Shweiki, D., Itin, A., Soffer, D., Keshet, E., (1992) Nature, 359, pp. 843-845
  • Levy, A., Levy, N., Wegner, S., Goldberg, M., (1995) J. Biol. Chem., 270, pp. 13333-13340
  • Maxwell, P.H., Pugh, C.W., Ratcliffe, P.J., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 2423-2427
  • Guang, L.W., Semenza, G.L., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 4304-4308
  • Guillemin, K., Krasnow, M.A., (1997) Cell, 89, pp. 9-12
  • Crews, S., (1998) Genes Dev., 12, pp. 607-620
  • Ledent, V., Vervoort, M., (2001) Genome Res., 11, pp. 754-770
  • Peyrefitte, S., Kahn, D., Haenlin, M., (2001) Mech. Dev., 104, pp. 99-104
  • Wang, G.L., Semenza, G.L., (1995) J. Biol. Chem., 270, pp. 1230-1237
  • Wang, G.L., Jiang, B.H., Rue, E.A., Semenza, G.L., (1995) Proc. Natl. Acad. Sci. U. S. A., 92, pp. 5510-5514
  • Powell-Coffman, J.A., Bradfield, C.A., Wood, W.B., (1998) Proc. Natl. Acad. Sci. U. S. A., 95, pp. 2844-2849
  • Jiang, H., Guo, R., Powell-Coffman, J.A., (2001) Proc. Natl. Acad. Sci. U. S. A., 14, pp. 7916-7921
  • Nambu, J.R., Chen, W., Hu, S., Crews, S.T., (1996) Gene (Amst.), 172, pp. 249-254
  • Ohshiro, T., Saigo, K., (1997) Development (Camb.), 124, pp. 3975-3986
  • Sonnenfeld, M., Ward, M., Nystrom, G., Mosher, J., Stahl, S., Crews, S., (1997) Development (Camb.), 124, pp. 4571-4582
  • Ma, E., Haddad, G.G., (1999) Mol. Brain Res., 73, pp. 11-16
  • Ebert, B.L., Bunn, H.F., (1999) Blood, 94, pp. 1864-1877
  • Wenger, R.H., (2000) J. Exp. Biol., 203, pp. 1253-1263
  • Wenger, R.H., Gassmann, M., (1997) Biol. Chem., 378, pp. 1-8
  • Huang, L.E., Bunn, H.F., (2003) J. Biol. Chem., 278, pp. 19575-19578
  • Epstein, A.C.R., Gleadle, J.M., McNeill, L.A., Hewitson, K.S., O'Rourke, J., Mole, D.R., Mukherji, M., Ratcliffe, P.J., (2001) Cell, 107, pp. 43-54
  • Semenza, G.L., (2001) Cell, 107, pp. 1-3
  • Bruick, R.K., McKnight, S.L., (2001) Science, 294, pp. 1337-1340
  • Huang, L.E., Gu, J., Schau, M., Bunn, H.F., (1998) Proc. Natl. Acad. Sci. U. S. A., 95, pp. 7987-7992
  • Salceda, S., Caro, J., (1997) J. Biol. Chem., 272, pp. 22642-22647
  • Maxwell, P.H., Wiesener, M.S., Chang, G.W., Clifford, S.C., Vaux, E.C., Cockman, M.E., Wykoff, C.C., Ratcliffe, P.J., (1999) Nature, 399, pp. 271-275
  • Cockman, M.E., Masson, N., Mole, D.R., Jaakola, P., Change, G.W., Clifford, S.C., Maher, E.R., Maxwell, P.H., (2000) J. Biol. Chem., 275, pp. 25733-25741
  • Tanimoto, K., Makino, Y., Pereira, T., Poellinger, L., (2000) EMBO J, 19, pp. 4298-4309
  • Nagao, M., Ebert, B.L., Ratcliffe, P.J., Pugh, C.W., (1996) FEBS Lett, 387, pp. 161-166
  • Srinivas, V., Zhang, L.-P., Zhu, X.-H., Caro, J., (1999) Biochem. Biophys. Res. Commun., 260, pp. 557-561
  • Bacon, N.C.M., Wappner, P., O'Rourke, J.F., Bartlett, S.M., Shilo, B.-Z., Pugh, C.W., Ratcliffe, P.J., (1998) Biochem. Biophys. Res. Commun., 249, pp. 811N. C. M.-816N. C. M.
  • Lavista-Llanos, S., Centanin, L., Irisarri, M., Russo, D.M., Gleadle, J.M., Bocca, S.N., Muzzopappa, M., Wappner, P., (2002) Mol. Cell. Biol., 22, pp. 6842-6853
  • Ward, M.P., Mosher, J.T., Crews, S.T., (1998) Development (Camb.), 125, pp. 1599-1608
  • Nambu, J.R., Lewis, J.O., Wharton Jr., K.A., Crews, S.T., (1991) Cell, 67, pp. 1157-1167
  • Isaac, D.D., Andrew, D.J., (1996) Genes Dev., 10, pp. 103-117
  • Wilk, R., Weizman, I., Shilo, B.-Z., (1996) Genes Dev., 10, pp. 93-102
  • Emmons, R.B., Duncan, D., Estes, P.A., Kiefel, P., Mosher, J.T., Sonnenfeld, M., Ward, M.P., Crews, S.T., (1999) Development (Camb.), 126, pp. 3937-3945
  • Jiang, L., Crews, S.T., (2003) Mol. Cell. Biol., 23, pp. 5625-5637
  • Wharton Jr., K.A., Franks, R.G., Kasai, Y., Crews, S.T., (1994) Development (Camb.), 120, pp. 3563-3569
  • Denison, M.S., Fisher, J.M., Whitlock Jr., J.P., (1988) J. Biol. Chem., 263, pp. 17221-17224
  • Hankinson, O., (1995) Annu. Rev. Pharmacol. Toxicol., 35, pp. 307-340
  • Schneider, I., (1972) J. Embryol. Exp. Morphol., 27, pp. 353-365
  • Goldberg, M.A., Dunning, S.P., Bunn, H.F., (1988) Science, 242, pp. 1412-1415
  • Long, E.O., Dawid, I.B., (1980) J. Mol. Biol., 138, pp. 873-878
  • Bell, J., Neilson, L., Pellegrini, M., (1988) Mol. Cell. Biol., 8, pp. 91-95
  • Semenza, G.L., Wang, G.L., (1992) Mol. Cell. Biol., 12, pp. 5447-5454
  • Chung, Y.-T., Keller, E.B., (1990) Mol. Cell. Biol., 10, pp. 6172-6180
  • Southern, J.A., Young, D.F., Heaney, F., Baumgärtner, W.K., Randall, R.E., (1991) J. Gen. Virol., 72, pp. 1551-1557
  • Graham, F.L., Van Der Eb, A.J., (1973) Virology, 52, pp. 456-467
  • Wigler, M., Pellicer, A., Silverstein, S., Axel, R., Urlaub, G., Chasin, L., (1979) Proc. Natl. Acad. Sci. U. S. A., 76, pp. 1373-1376
  • Gorr, T.A., Cahn, J.D., Hradecky, P., Bunn, H.F., (2003) Oxygen Sensing: Responses and Adaptation to Hypoxia, pp. 175-199. , (Lahiri, S., Semenza, G. L., and Prabhakar, N. R., eds), Marcel Dekker, Inc., New York
  • Burmester, T., Hankeln, T., (1999) Mol. Biol. Evol., 16, pp. 1809-1811
  • Hankeln, T., Jaenicke, V., Kiger, L., Dewilde, S., Ungerechts, G., Schmidt, M., Urban, J., Burmester, T., (2002) J. Biol. Chem., 277, pp. 29012-29017
  • Narravula, S., Colgan, S.P., (2001) J. Immunol., 166, pp. 7543-7548
  • (2002) J. Immunol., 168, p. 3113
  • Mazure, N.M., Chauvet, C., Bois-Joyeux, B., Bernard, M.-A., Nacer-Chérif, H., Danan, J.-L., (2002) Cancer Res., 62, pp. 1158-1165
  • Abu-Shumays, R.L., Fristrom, J.W., (1997) Dev. Genet., 20, pp. 11-22
  • Bruening, W., Prowse, A.H., Schultz, D.C., Holgado-Madruga, M., Wong, A., Godwin, A.K., (1999) Cancer Res., 59, pp. 4973-4983
  • Tweedie, S., Ng, H.-H., Barlow, A.L., Turner, B.M., Hendrich, B., Bird, A., (1999) Nat. Genet., 23, pp. 389-390
  • Lyko, F., Ramsahoye, B.H., Jaenisch, R., (2000) Nature, 408, pp. 538-540
  • Gowher, H., Leismann, O., Jeltsch, A., (2000) EMBO J., 19, pp. 6918-6923
  • Lyko, F., (2001) Trends Genet., 17, pp. 169-172
  • Kunert, N., Marhold, J., Stanke, J., Stach, D., Lyko, F., (2003) Development (Camb.), 130, pp. 5083-5090
  • Taylor, B.L., Zhulin, I.B., (1999) Microbiol. Mol. Biol. Rev., 63, pp. 479-506
  • Makino, Y., Cao, R., Svensson, K., Bertilsson, G., Asman, M., Tanaka, H., Cao, Y., Poellinger, L., (2001) Nature, 414, pp. 550-554
  • Makino, Y., Kanopka, A., Wilson, W.J., Tanaka, H., Poellinger, L., (2002) J. Biol. Chem., 277, pp. 32405-32408
  • Gorr, T.A., Cahn, J.D., Yamagata, H., Bunn, H.F., (2004) J. Biol. Chem., 279, pp. 36038-36047

Citas:

---------- APA ----------
Gorr, T.A., Tomita, T., Wappner, P. & Bunn, H.F. (2004) . Regulation of Drosophila hypoxia-inducible factor (HIF) activity in SL2 cells: Identification of a hypoxia-induced variant isoform of the HIFα homolog gene similar. Journal of Biological Chemistry, 279(34), 36048-36058.
http://dx.doi.org/10.1074/jbc.M405077200
---------- CHICAGO ----------
Gorr, T.A., Tomita, T., Wappner, P., Bunn, H.F. "Regulation of Drosophila hypoxia-inducible factor (HIF) activity in SL2 cells: Identification of a hypoxia-induced variant isoform of the HIFα homolog gene similar" . Journal of Biological Chemistry 279, no. 34 (2004) : 36048-36058.
http://dx.doi.org/10.1074/jbc.M405077200
---------- MLA ----------
Gorr, T.A., Tomita, T., Wappner, P., Bunn, H.F. "Regulation of Drosophila hypoxia-inducible factor (HIF) activity in SL2 cells: Identification of a hypoxia-induced variant isoform of the HIFα homolog gene similar" . Journal of Biological Chemistry, vol. 279, no. 34, 2004, pp. 36048-36058.
http://dx.doi.org/10.1074/jbc.M405077200
---------- VANCOUVER ----------
Gorr, T.A., Tomita, T., Wappner, P., Bunn, H.F. Regulation of Drosophila hypoxia-inducible factor (HIF) activity in SL2 cells: Identification of a hypoxia-induced variant isoform of the HIFα homolog gene similar. J. Biol. Chem. 2004;279(34):36048-36058.
http://dx.doi.org/10.1074/jbc.M405077200