메뉴 건너뛰기




Volumn 314, Issue 14, 2008, Pages 2661-2673

Induction of truncated form of tenascin-X (XB-S) through dissociation of HDAC1 from SP-1/HDAC1 complex in response to hypoxic conditions

Author keywords

HDAC1; Hypoxia; Sp1; Tenascin X; Truncated form; XA; XB S

Indexed keywords

GUANINE; HISTONE DEACETYLASE 1; PREGNANCY SPECIFIC BETA1 GLYCOPROTEIN; TENASCIN; TENASCIN X;

EID: 48849107453     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.05.019     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0348013068 scopus 로고    scopus 로고
    • Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse
    • Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., and Hood L. Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res 13 (2003) 2621-2636
    • (2003) Genome Res , vol.13 , pp. 2621-2636
    • Xie, T.1    Rowen, L.2    Aguado, B.3    Ahearn, M.E.4    Madan, A.5    Qin, S.6    Campbell, R.D.7    Hood, L.8
  • 2
    • 0028246851 scopus 로고
    • Structure and genetics of the partially duplicated gene RP located immediately upstream of the complement C4A and the C4B genes in the HLA class III region
    • Shen L., Wu L.C., Sanlioglu S., Chen R., Mendoza A.R., Dangel A.W., Carroll M.C., Zipf W.B., and Yu C.Y. Structure and genetics of the partially duplicated gene RP located immediately upstream of the complement C4A and the C4B genes in the HLA class III region. J. Biol. Chem 269 (1994) 8466-8476
    • (1994) J. Biol. Chem , vol.269 , pp. 8466-8476
    • Shen, L.1    Wu, L.C.2    Sanlioglu, S.3    Chen, R.4    Mendoza, A.R.5    Dangel, A.W.6    Carroll, M.C.7    Zipf, W.B.8    Yu, C.Y.9
  • 3
    • 0034686608 scopus 로고    scopus 로고
    • Deficiencies of human complement component C4A and C4B and heterozygosity in length variants of RP-C4-CYP21-TNX (RCCX) modules in Caucasians. The load of RCCX genetic diversity on major histocompatibility complex-associated disease
    • Blanchong C.A., Zhou B., Rupert K.L., Chung E.K., Jones K.N., Sotos J.F., Zipf W.B., Rennebohm R.M., and Yu C.Y. Deficiencies of human complement component C4A and C4B and heterozygosity in length variants of RP-C4-CYP21-TNX (RCCX) modules in Caucasians. The load of RCCX genetic diversity on major histocompatibility complex-associated disease. J. Exp. Med 191 (2000) 2183-2196
    • (2000) J. Exp. Med , vol.191 , pp. 2183-2196
    • Blanchong, C.A.1    Zhou, B.2    Rupert, K.L.3    Chung, E.K.4    Jones, K.N.5    Sotos, J.F.6    Zipf, W.B.7    Rennebohm, R.M.8    Yu, C.Y.9
  • 4
    • 0026606265 scopus 로고
    • Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin
    • Matsumoto K., Arai M., Ishihara N., Ando A., Inoko H., and Ikemura T. Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin. Genomics 12 (1992) 485-491
    • (1992) Genomics , vol.12 , pp. 485-491
    • Matsumoto, K.1    Arai, M.2    Ishihara, N.3    Ando, A.4    Inoko, H.5    Ikemura, T.6
  • 5
    • 0027231385 scopus 로고
    • Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow J., Tee M.K., Gitelman S.E., Mellon S.H., and Miller W.L. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J. Cell Biol 122 (1993) 265-278
    • (1993) J. Cell Biol , vol.122 , pp. 265-278
    • Bristow, J.1    Tee, M.K.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 6
    • 0032517136 scopus 로고    scopus 로고
    • Structural analysis of mouse tenascin-X: evolutionary aspects of reduplication of FNIII repeats in the tenascin gene family
    • Ikuta T., Sogawa N., Ariga H., Ikemura T., and Matsumoto K. Structural analysis of mouse tenascin-X: evolutionary aspects of reduplication of FNIII repeats in the tenascin gene family. Gene 217 (1998) 1-13
    • (1998) Gene , vol.217 , pp. 1-13
    • Ikuta, T.1    Sogawa, N.2    Ariga, H.3    Ikemura, T.4    Matsumoto, K.5
  • 8
    • 0029822205 scopus 로고    scopus 로고
    • Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue
    • Hagios C., Koch M., Spring J., Chiquet M., and Chiquet-Ehrismann R. Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue. J. Cell Biol 134 (1996) 1499-1512
    • (1996) J. Cell Biol , vol.134 , pp. 1499-1512
    • Hagios, C.1    Koch, M.2    Spring, J.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 9
    • 0031970896 scopus 로고    scopus 로고
    • Zebrafish tenascin-W, a new member of the tenascin family
    • Weber P., Montag D., Schachner M., and Bernhardt R.R. Zebrafish tenascin-W, a new member of the tenascin family. J. Neurobiol 35 (1998) 1-16
    • (1998) J. Neurobiol , vol.35 , pp. 1-16
    • Weber, P.1    Montag, D.2    Schachner, M.3    Bernhardt, R.R.4
  • 10
    • 0038383036 scopus 로고    scopus 로고
    • Tenascin-N: characterization of a novel member of the tenascin family that mediates neurite repulsion from hippocampal explants
    • Neidhardt J., Fehr S., Kutsche M., Löhler J., and Schachner M. Tenascin-N: characterization of a novel member of the tenascin family that mediates neurite repulsion from hippocampal explants. Mol. Cell. Neurosci 23 (2003) 193-209
    • (2003) Mol. Cell. Neurosci , vol.23 , pp. 193-209
    • Neidhardt, J.1    Fehr, S.2    Kutsche, M.3    Löhler, J.4    Schachner, M.5
  • 11
    • 1242284590 scopus 로고    scopus 로고
    • Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development
    • Scherberich A., Tucker R.P., Samandari E., Brown-Luedi M., Martin D., and Chiquet-Ehrismann R. Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development. J. Cell Sci 117 (2004) 571-581
    • (2004) J. Cell Sci , vol.117 , pp. 571-581
    • Scherberich, A.1    Tucker, R.P.2    Samandari, E.3    Brown-Luedi, M.4    Martin, D.5    Chiquet-Ehrismann, R.6
  • 12
    • 0026638378 scopus 로고
    • Mechanism and consequences of the duplication of the human C4/P450c21/gene X locus
    • Gitelman S.E., Bristow J., and Miller W.L. Mechanism and consequences of the duplication of the human C4/P450c21/gene X locus. Mol. Cell. Biol 12 (1992) 2124-2134
    • (1992) Mol. Cell. Biol , vol.12 , pp. 2124-2134
    • Gitelman, S.E.1    Bristow, J.2    Miller, W.L.3
  • 13
    • 0029166289 scopus 로고
    • Sequences promoting the transcription of the human XA gene overlapping P450c21A correctly predict the presence of a novel, adrenal-specific, truncated form of tenascin-X
    • Tee M.K., Thomson A.A., Bristow J., and Miller W.L. Sequences promoting the transcription of the human XA gene overlapping P450c21A correctly predict the presence of a novel, adrenal-specific, truncated form of tenascin-X. Genomics 28 (1995) 171-178
    • (1995) Genomics , vol.28 , pp. 171-178
    • Tee, M.K.1    Thomson, A.A.2    Bristow, J.3    Miller, W.L.4
  • 14
    • 0034643894 scopus 로고    scopus 로고
    • Primary structure, genomic organization and expression of the major secretory protein of murine epididymis, ME1
    • Nakamura Y., Takayama N., Minamitani T., Ikuta T., Ariga H., and Matsumoto K. Primary structure, genomic organization and expression of the major secretory protein of murine epididymis, ME1. Gene 251 (2000) 55-62
    • (2000) Gene , vol.251 , pp. 55-62
    • Nakamura, Y.1    Takayama, N.2    Minamitani, T.3    Ikuta, T.4    Ariga, H.5    Matsumoto, K.6
  • 15
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem 162 (1987) 156-159
    • (1987) Anal. Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 16
    • 0036748317 scopus 로고    scopus 로고
    • Invasion of melanoma in double knockout mice lacking tenascin-X and tenascin-C
    • Matsumoto K., Takahashi K., Yoshiki A., Kusakabe M., and Ariga H. Invasion of melanoma in double knockout mice lacking tenascin-X and tenascin-C. Jpn. J. Cancer Res 93 (2002) 968-975
    • (2002) Jpn. J. Cancer Res , vol.93 , pp. 968-975
    • Matsumoto, K.1    Takahashi, K.2    Yoshiki, A.3    Kusakabe, M.4    Ariga, H.5
  • 17
    • 0023651237 scopus 로고
    • OVEC, a versatile system to study transcription in mammalian cells and cell-free extracts
    • Westin G., Gerster T., Müller M.M., Schaffner G., and Schaffner W. OVEC, a versatile system to study transcription in mammalian cells and cell-free extracts. Nucleic Acids Res 15 (1987) 6787-6798
    • (1987) Nucleic Acids Res , vol.15 , pp. 6787-6798
    • Westin, G.1    Gerster, T.2    Müller, M.M.3    Schaffner, G.4    Schaffner, W.5
  • 18
    • 0034684993 scopus 로고    scopus 로고
    • Transcription factor Sp1 activates the expression of the mouse tenascin-X gene
    • Minamitani T., Ariga H., and Matsumoto K. Transcription factor Sp1 activates the expression of the mouse tenascin-X gene. Biochem. Biophys. Res. Commun 267 (2000) 626-631
    • (2000) Biochem. Biophys. Res. Commun , vol.267 , pp. 626-631
    • Minamitani, T.1    Ariga, H.2    Matsumoto, K.3
  • 19
    • 0029788268 scopus 로고    scopus 로고
    • Cloning and characterization of the genomic DNA of the human MSSP genes
    • Haigermoser C., Fujimoto M., Iguchi-Ariga S.M., and Ariga H. Cloning and characterization of the genomic DNA of the human MSSP genes. Nucleic Acids Res 24 (1996) 3846-3857
    • (1996) Nucleic Acids Res , vol.24 , pp. 3846-3857
    • Haigermoser, C.1    Fujimoto, M.2    Iguchi-Ariga, S.M.3    Ariga, H.4
  • 20
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., and Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 11 (1983) 1475-1489
    • (1983) Nucleic Acids Res , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 21
    • 0027136260 scopus 로고
    • Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction
    • Wang G.L., and Semenza G.L. Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction. Blood 82 (1993) 3610-3615
    • (1993) Blood , vol.82 , pp. 3610-3615
    • Wang, G.L.1    Semenza, G.L.2
  • 22
    • 0034929708 scopus 로고    scopus 로고
    • Sp1 and Krüppel-like factor family of transcription factors in cell growth regulation and cancer
    • Black A.R., Black J.D., and Azizkhan-Clifford J.R. Sp1 and Krüppel-like factor family of transcription factors in cell growth regulation and cancer. J. Cell Physiol 188 (2001) 143-160
    • (2001) J. Cell Physiol , vol.188 , pp. 143-160
    • Black, A.R.1    Black, J.D.2    Azizkhan-Clifford, J.R.3
  • 24
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M., Kijima M., Akita M., and Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem 265 (1990) 17174-17179
    • (1990) J. Biol. Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 25
    • 33644511058 scopus 로고    scopus 로고
    • Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription
    • Hung J.J., Wang Y.T., and Chang W.C. Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol. Cell. Biol 26 (2006) 1770-1785
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1770-1785
    • Hung, J.J.1    Wang, Y.T.2    Chang, W.C.3
  • 26
    • 0034663989 scopus 로고    scopus 로고
    • HIF-1 and human disease: one highly involved factor
    • Semenza G.L. HIF-1 and human disease: one highly involved factor. Genes Dev 14 (2000) 1983-1991
    • (2000) Genes Dev , vol.14 , pp. 1983-1991
    • Semenza, G.L.1
  • 27
    • 0034107952 scopus 로고    scopus 로고
    • Mammalian oxygen sensing, signalling and gene regulation
    • Wenger R.H. Mammalian oxygen sensing, signalling and gene regulation. J. Exp. Biol 203 (2000) 1253-1263
    • (2000) J. Exp. Biol , vol.203 , pp. 1253-1263
    • Wenger, R.H.1
  • 29
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon P.C., Hirota K., and Semenza G.L. FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 15 (2001) 2675-2686
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 31
    • 15244344206 scopus 로고    scopus 로고
    • HIF-1a induces genetic instability by transcriptionally downregulating MutSa expression
    • Koshiji M., To K.K., Hammer S., Kumamoto K., Harris A.L., Modrich P., and Huang L.E. HIF-1a induces genetic instability by transcriptionally downregulating MutSa expression. Mol. Cell 17 (2005) 793-803
    • (2005) Mol. Cell , vol.17 , pp. 793-803
    • Koshiji, M.1    To, K.K.2    Hammer, S.3    Kumamoto, K.4    Harris, A.L.5    Modrich, P.6    Huang, L.E.7
  • 32
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription
    • Pazin M.J., and Kadonaga J.T. What's up and down with histone deacetylation and transcription. Cell 89 (1997) 325-328
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 33
    • 0029926303 scopus 로고    scopus 로고
    • Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F
    • Karlseder J., Rotheneder H., and Wintersberger E. Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F. Mol. Cell. Biol 16 (1996) 1659-1667
    • (1996) Mol. Cell. Biol , vol.16 , pp. 1659-1667
    • Karlseder, J.1    Rotheneder, H.2    Wintersberger, E.3
  • 34
    • 0036469146 scopus 로고    scopus 로고
    • Oxygen sensing gets a second wind
    • Bruick R.K., and McKnight S.L. Oxygen sensing gets a second wind. Science 295 (2002) 807-808
    • (2002) Science , vol.295 , pp. 807-808
    • Bruick, R.K.1    McKnight, S.L.2
  • 35
    • 33645322383 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1
    • Yoo Y.G., Kong G., and Lee M.O. Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1. EMBO J 25 (2006) 1231-1241
    • (2006) EMBO J , vol.25 , pp. 1231-1241
    • Yoo, Y.G.1    Kong, G.2    Lee, M.O.3
  • 36
    • 0023103578 scopus 로고
    • Two mammalian genes transcribed from opposite strands of the same DNA locus
    • Adelman J.P., Bond C.T., Douglass J., and Herbert E. Two mammalian genes transcribed from opposite strands of the same DNA locus. Science 235 (1987) 1514-1517
    • (1987) Science , vol.235 , pp. 1514-1517
    • Adelman, J.P.1    Bond, C.T.2    Douglass, J.3    Herbert, E.4
  • 37
    • 38149059720 scopus 로고    scopus 로고
    • The interaction with Sp1 and reduction in the activity of histone deacetylase 1 are critical for the constitutive gene expression of IL-1 alpha in human melanoma cells
    • Enya K., Hayashi H., Takii T., Ohoka N., Kanata S., Okamoto T., and Onozaki K. The interaction with Sp1 and reduction in the activity of histone deacetylase 1 are critical for the constitutive gene expression of IL-1 alpha in human melanoma cells. J. Leukoc. Biol 83 (2008) 190-199
    • (2008) J. Leukoc. Biol , vol.83 , pp. 190-199
    • Enya, K.1    Hayashi, H.2    Takii, T.3    Ohoka, N.4    Kanata, S.5    Okamoto, T.6    Onozaki, K.7
  • 38
    • 33744535033 scopus 로고    scopus 로고
    • Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP: phosphocholine cytidylyltransferase-alpha transcription
    • Banchio C., Lingrell S., and Vance D.E. Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP: phosphocholine cytidylyltransferase-alpha transcription. J. Biol. Chem 281 (2006) 10010-10015
    • (2006) J. Biol. Chem , vol.281 , pp. 10010-10015
    • Banchio, C.1    Lingrell, S.2    Vance, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.