메뉴 건너뛰기




Volumn 421, Issue 4, 2012, Pages 665-670

Lysine-specific demethylase 1 (LSD1) and histone deacetylase 1 (HDAC1) synergistically repress proinflammatory cytokines and classical complement pathway components

Author keywords

HDAC; Histone demethylases; Inflammation; LSD1; Transcription

Indexed keywords

ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C3; COMPLEMENT FACTOR D; HISTONE DEACETYLASE 1; HYDROLASE; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 1 RECEPTOR ACCESSORY PROTEIN; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; LYSINE SPECIFIC DEMETHYLASE 1; UNCLASSIFIED DRUG;

EID: 84861221167     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.057     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001, 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 7
    • 0035852637 scopus 로고    scopus 로고
    • CoREST is an integral component of the CoREST-human histone deacetylase complex
    • You A., Tong J.K., Grozinger C.M., Schreiber S.L. CoREST is an integral component of the CoREST-human histone deacetylase complex. Proc. Natl. Acad. Sci. USA 2001, 98:1454-1458.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1454-1458
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 10
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi Y.J., Matson C., Lan F., Iwase S., Baba T., Shi Y. Regulation of LSD1 histone demethylase activity by its associated factors. Mol. Cell 2005, 19:857-864.
    • (2005) Mol. Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 11
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast N., Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem. 2010, 79:155-179.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 17
    • 34547785073 scopus 로고    scopus 로고
    • Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1
    • Saleque S., Kim J., Rooke H.M., Orkin S.H. Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1. Mol. Cell 2007, 27:562-572.
    • (2007) Mol. Cell , vol.27 , pp. 562-572
    • Saleque, S.1    Kim, J.2    Rooke, H.M.3    Orkin, S.H.4
  • 18
    • 77950868547 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology
    • Lim S., Janzer A., Becker A., Zimmer A., Schule R., Buettner R., Kirfel J. Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology. Carcinogenesis 2010, 31:512-520.
    • (2010) Carcinogenesis , vol.31 , pp. 512-520
    • Lim, S.1    Janzer, A.2    Becker, A.3    Zimmer, A.4    Schule, R.5    Buettner, R.6    Kirfel, J.7
  • 20
    • 77956636685 scopus 로고    scopus 로고
    • Epigenetic regulation of cancer growth by histone demethylases
    • Lim S., Metzger E., Schule R., Kirfel J., Buettner R. Epigenetic regulation of cancer growth by histone demethylases. Int. J. Cancer 2010, 127:1991-1998.
    • (2010) Int. J. Cancer , vol.127 , pp. 1991-1998
    • Lim, S.1    Metzger, E.2    Schule, R.3    Kirfel, J.4    Buettner, R.5
  • 23
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • Medzhitov R. Origin and physiological roles of inflammation. Nature 2008, 454:428-435.
    • (2008) Nature , vol.454 , pp. 428-435
    • Medzhitov, R.1
  • 24
    • 0036712454 scopus 로고    scopus 로고
    • Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes
    • Saccani S., Natoli G. Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes. Genes Dev. 2002, 16:2219-2224.
    • (2002) Genes Dev. , vol.16 , pp. 2219-2224
    • Saccani, S.1    Natoli, G.2
  • 25
    • 34250823515 scopus 로고    scopus 로고
    • Gene-specific control of inflammation by TLR-induced chromatin modifications
    • Foster S.L., Hargreaves D.C., Medzhitov R. Gene-specific control of inflammation by TLR-induced chromatin modifications. Nature 2007, 447:972-978.
    • (2007) Nature , vol.447 , pp. 972-978
    • Foster, S.L.1    Hargreaves, D.C.2    Medzhitov, R.3
  • 26
    • 34848907192 scopus 로고    scopus 로고
    • Epigenetic silencing of tumor necrosis factor alpha during endotoxin tolerance
    • El Gazzar M., Yoza B.K., Hu J.Y., Cousart S.L., McCall C.E. Epigenetic silencing of tumor necrosis factor alpha during endotoxin tolerance. J. Biol. Chem. 2007, 282:26857-26864.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26857-26864
    • El Gazzar, M.1    Yoza, B.K.2    Hu, J.Y.3    Cousart, S.L.4    McCall, C.E.5
  • 27
    • 18044365415 scopus 로고    scopus 로고
    • Induction of inflammatory cytokines and interferon responses by double-stranded and single-stranded siRNAs is sequence-dependent and requires endosomal localization
    • Sioud M. Induction of inflammatory cytokines and interferon responses by double-stranded and single-stranded siRNAs is sequence-dependent and requires endosomal localization. J. Mol. Biol. 2005, 348:1079-1090.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1079-1090
    • Sioud, M.1
  • 28
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • Lee M.G., Wynder C., Schmidt D.M., McCafferty D.G., Shiekhattar R. Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem. Biol. 2006, 13:563-567.
    • (2006) Chem. Biol. , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhattar, R.5
  • 29
    • 73849090193 scopus 로고    scopus 로고
    • Complement and its role in innate and adaptive immune responses
    • Dunkelberger J.R., Song W.C. Complement and its role in innate and adaptive immune responses. Cell Res. 2010, 20:34-50.
    • (2010) Cell Res. , vol.20 , pp. 34-50
    • Dunkelberger, J.R.1    Song, W.C.2
  • 30
    • 1542404878 scopus 로고    scopus 로고
    • Comparative effects of cytokines and cytokine combinations on complement component C3 secretion by HepG2 cells
    • Andrews E., Feldhoff P., Feldhoff R., Lassiter H. Comparative effects of cytokines and cytokine combinations on complement component C3 secretion by HepG2 cells. Cytokine 2003, 23:164-169.
    • (2003) Cytokine , vol.23 , pp. 164-169
    • Andrews, E.1    Feldhoff, P.2    Feldhoff, R.3    Lassiter, H.4
  • 32
    • 53249108053 scopus 로고    scopus 로고
    • Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice
    • Reddy M.A., Villeneuve L.M., Wang M., Lanting L., Natarajan R. Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice. Circ. Res. 2008, 103:615-623.
    • (2008) Circ. Res. , vol.103 , pp. 615-623
    • Reddy, M.A.1    Villeneuve, L.M.2    Wang, M.3    Lanting, L.4    Natarajan, R.5
  • 33
    • 52949144507 scopus 로고    scopus 로고
    • Role of inflammation in atherosclerosis associated with rheumatoid arthritis
    • Libby P. Role of inflammation in atherosclerosis associated with rheumatoid arthritis. Am. J. Med. 2008, 121:S21-S31.
    • (2008) Am. J. Med. , vol.121
    • Libby, P.1
  • 35
    • 0023778137 scopus 로고
    • Interleukin 6, the third mediator of acute-phase reaction, modulates hepatic protein synthesis in human and mouse. Comparison with interleukin 1 beta and tumor necrosis factor-alpha
    • Ramadori G., Van Damme J., Rieder H., Meyer zum Buschenfelde K.H. Interleukin 6, the third mediator of acute-phase reaction, modulates hepatic protein synthesis in human and mouse. Comparison with interleukin 1 beta and tumor necrosis factor-alpha. Eur. J. Immunol. 1988, 18:1259-1264.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 1259-1264
    • Ramadori, G.1    Van Damme, J.2    Rieder, H.3    Meyer zum Buschenfelde, K.H.4
  • 36
    • 0032710620 scopus 로고    scopus 로고
    • Cytokines associated with amyloid plaques in Alzheimer's disease brain stimulate human glial and neuronal cell cultures to secrete early complement proteins, but not C1-inhibitor
    • Veerhuis R., Janssen I., De Groot C.J., Van Muiswinkel F.L., Hack C.E., Eikelenboom P. Cytokines associated with amyloid plaques in Alzheimer's disease brain stimulate human glial and neuronal cell cultures to secrete early complement proteins, but not C1-inhibitor. Exp. Neurol. 1999, 160:289-299.
    • (1999) Exp. Neurol. , vol.160 , pp. 289-299
    • Veerhuis, R.1    Janssen, I.2    De Groot, C.J.3    Van Muiswinkel, F.L.4    Hack, C.E.5    Eikelenboom, P.6
  • 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., 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. 2008, 83:190-199.
    • (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
    • 77951228749 scopus 로고    scopus 로고
    • Foxp1/2/4-NuRD interactions regulate gene expression and epithelial injury response in the lung via regulation of interleukin-6
    • Chokas A.L., Trivedi C.M., Lu M.M., Tucker P.W., Li S., Epstein J.A., Morrisey E.E. Foxp1/2/4-NuRD interactions regulate gene expression and epithelial injury response in the lung via regulation of interleukin-6. J. Biol. Chem. 2010, 285:13304-13313.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13304-13313
    • Chokas, A.L.1    Trivedi, C.M.2    Lu, M.M.3    Tucker, P.W.4    Li, S.5    Epstein, J.A.6    Morrisey, E.E.7
  • 39
    • 0036203419 scopus 로고    scopus 로고
    • The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1
    • Zhong H., May M.J., Jimi E., Ghosh S. The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. Mol. Cell 2002, 9:625-636.
    • (2002) Mol. Cell , vol.9 , pp. 625-636
    • Zhong, H.1    May, M.J.2    Jimi, E.3    Ghosh, S.4
  • 40
    • 63049083734 scopus 로고    scopus 로고
    • A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death
    • Saijo K., Winner B., Carson C.T., Collier J.G., Boyer L., Rosenfeld M.G., Gage F.H., Glass C.K. A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death. Cell 2009, 137:47-59.
    • (2009) Cell , vol.137 , pp. 47-59
    • Saijo, K.1    Winner, B.2    Carson, C.T.3    Collier, J.G.4    Boyer, L.5    Rosenfeld, M.G.6    Gage, F.H.7    Glass, C.K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.