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Volumn 17, Issue 5-6, 2011, Pages 391-396

Inhibition of hdac activity by itf2357 ameliorates joint inflammation and prevents cartilage and bone destruction in experimental arthritis

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; COLLAGEN TYPE 2; DEXAMETHASONE; GAMMA INTERFERON; GIVINOSTAT; INTERLEUKIN 12; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 6; LEFLUNOMIDE; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; OSTEOCLAST DIFFERENTIATION FACTOR; ROMIDEPSIN; TRICHOSTATIN A; TUMOR NECROSIS FACTOR ALPHA;

EID: 79957958931     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/molmed.2011.00058     Document Type: Article
Times cited : (85)

References (41)
  • 1
    • 37849019672 scopus 로고    scopus 로고
    • Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors
    • Khan N, et al. (2008) Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors. Biochem. J. 409:581-9.
    • (2008) Biochem. J , vol.409 , pp. 581-589
    • Khan, N.1
  • 2
    • 39049142019 scopus 로고    scopus 로고
    • Oral valproic acid for epilepsy-long-term experience in therapy and side effects
    • Gerstner T, Bell N, Konig S. (2008) Oral valproic acid for epilepsy-long-term experience in therapy and side effects. Expert. Opin. Pharmacother. 9:285-92.
    • (2008) Expert. Opin. Pharmacother , vol.9 , pp. 285-292
    • Gerstner, T.1    Bell, N.2    Konig, S.3
  • 3
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: Potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren M, Leng Y, Jeong M, Leeds PR, Chuang DM. (2004) Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J. Neurochem. 89:1358-67.
    • (2004) J. Neurochem , vol.89 , pp. 1358-1367
    • Ren, M.1    Leng, Y.2    Jeong, M.3    Leeds, P.R.4    Chuang, D.M.5
  • 4
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylases and cancer: Causes and therapies
    • Marks PA, et al. (2001) Histone deacetylases and cancer: causes and therapies. Nature Rev. Cancer. 1:194-202.
    • (2001) Nature Rev. Cancer , vol.1 , pp. 194-202
    • Marks, P.A.1
  • 5
    • 79955552937 scopus 로고    scopus 로고
    • Safety and efficacy of an oral histone deacetylase inhibitor in systemic-onset juvenile idiopathic arthritis
    • Vojinovic J, et al. (2011) Safety and efficacy of an oral histone deacetylase inhibitor in systemic-onset juvenile idiopathic arthritis. Arthritis Rheum. 63:1452-8.
    • (2011) Arthritis Rheum , vol.63 , pp. 1452-1458
    • Vojinovic, J.1
  • 6
    • 33644836549 scopus 로고    scopus 로고
    • Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoy-lanilide hydroxamic acid in patients with advanced hematologic malignancies
    • O'Connor OA, et al. (2006) Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoy-lanilide hydroxamic acid in patients with advanced hematologic malignancies. J. Clin. Oncol. 24:166-73.
    • (2006) J. Clin. Oncol , vol.24 , pp. 166-173
    • O'Connor, O.A.1
  • 7
    • 0035046529 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Development of suberoylanilide hydroxamic acid (saha) for the treatment of cancers
    • Richon VM, Zhou X, Rifkind RA, Marks PA. (2001) Histone deacetylase inhibitors: development of suberoylanilide hydroxamic acid (saha) for the treatment of cancers. Blood Cells Mol. Dis. 27:260-4.
    • (2001) Blood Cells Mol. Dis , vol.27 , pp. 260-264
    • Richon, V.M.1    Zhou, X.2    Rifkind, R.A.3    Marks, P.A.4
  • 8
    • 4143101371 scopus 로고    scopus 로고
    • Class I histone deacetylase-selective novel synthetic inhibitors potently inhibit human tumor proliferation
    • Park JH, et al. (2004) Class I histone deacetylase-selective novel synthetic inhibitors potently inhibit human tumor proliferation. Clin. Cancer Res. 10:5271-81.
    • (2004) Clin. Cancer Res , vol.10 , pp. 5271-5281
    • Park, J.H.1
  • 9
    • 0037022598 scopus 로고    scopus 로고
    • The antitumor histone deacetylase inhibitor suberoylanilide hydroxamic acid exhibits antiinflammatory properties via suppression of cytokines
    • Leoni F, et al. (2002) The antitumor histone deacetylase inhibitor suberoylanilide hydroxamic acid exhibits antiinflammatory properties via suppression of cytokines. Proc. Natl. Acad. Sci. U.S.A. 99:2995-3000.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2995-3000
    • Leoni, F.1
  • 10
    • 77951670390 scopus 로고    scopus 로고
    • The histone deacetylase in hibitor ITF2357 decreases surface CXCR4 and CCR5 expression on CD4+ T-cells and monocytes and is superior to valproic acid for latent HIV-1 expression in vitro
    • Matalon S, et al. (2010) The histone deacetylase in hibitor ITF2357 decreases surface CXCR4 and CCR5 expression on CD4+ T-cells and monocytes and is superior to valproic acid for latent HIV-1 expression in vitro. J. Acquir. Immune Defic. Syndr. 54:1-9.
    • (2010) J. Acquir. Immune Defic. Syndr , vol.54 , pp. 1-9
    • Matalon, S.1
  • 11
    • 1642415712 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect
    • Reddy P, et al. (2004) Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect. Proc. Natl. Acad. Sci. U.S.A. 101:3921-6.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 3921-3926
    • Reddy, P.1
  • 12
    • 4644307426 scopus 로고    scopus 로고
    • Modulation of renal disease in MRL/lpr mice by suberoylanilide hy-droxamic acid
    • Reilly CM, et al. (2004) Modulation of renal disease in MRL/lpr mice by suberoylanilide hy-droxamic acid. J. Immunol. 173:4171-8.
    • (2004) J. Immunol , vol.173 , pp. 4171-4178
    • Reilly, C.M.1
  • 13
    • 33645775726 scopus 로고    scopus 로고
    • Histone hyperacetylation is associated with amelioration of experimental colitis in mice
    • Glauben R, et al. (2006) Histone hyperacetylation is associated with amelioration of experimental colitis in mice. J. Immunol. 176:5015-22.
    • (2006) J. Immunol , vol.176 , pp. 5015-5022
    • Glauben, R.1
  • 14
    • 33646495294 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor ITF2357 reduces production of pro-inflammatory cytokines in vitro and systemic inflammation in vivo
    • Leoni F, et al. (2005) The histone deacetylase inhibitor ITF2357 reduces production of pro-inflammatory cytokines in vitro and systemic inflammation in vivo. Mol. Med. 11:1-15.
    • (2005) Mol. Med , vol.11 , pp. 1-15
    • Leoni, F.1
  • 15
    • 33646710170 scopus 로고    scopus 로고
    • Reduction of graft-versus-host disease by histone deacetylase inhibitor suberony-lanilide hydroxamic acid is associated with modulation of inflammatory cytokine milieu and involves inhibition of STAT1
    • Leng C, et al. (2006) Reduction of graft-versus-host disease by histone deacetylase inhibitor suberony-lanilide hydroxamic acid is associated with modulation of inflammatory cytokine milieu and involves inhibition of STAT1. Exp. Hematol. 34:776-87.
    • (2006) Exp. Hematol , vol.34 , pp. 776-787
    • Leng, C.1
  • 16
    • 72749101742 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor ITF2357 is neuroprotective, improves functional recovery, and induces glial apoptosis following experimental traumatic brain injury
    • Shein NA, et al. (2009) Histone deacetylase inhibitor ITF2357 is neuroprotective, improves functional recovery, and induces glial apoptosis following experimental traumatic brain injury. FASEB J. 23:4266-75.
    • (2009) FASEB J , vol.23 , pp. 4266-4275
    • Shein, N.A.1
  • 17
    • 42549114401 scopus 로고    scopus 로고
    • Histone deacetylases: Novel targets for prevention of colitis-associated cancer in mice
    • Glauben R, et al. (2008) Histone deacetylases: novel targets for prevention of colitis-associated cancer in mice. Gut. 57:613-22.
    • (2008) Gut , vol.57 , pp. 613-622
    • Glauben, R.1
  • 18
    • 77954286123 scopus 로고    scopus 로고
    • Increased Activity and Expression of Histone Deacetylase 1 In Relation to Tumor Necrosis Factor-alpha In Synovial Tissue of Rheumatoid Arthritis
    • Kawabata T, et al. (2010) Increased activity and expression of histone deacetylase 1 in relation to tumor necrosis factor-alpha in synovial tissue of rheumatoid arthritis. Arthritis Res. Ther. 12:R133.
    • (2010) Arthritis Res. Ther , vol.12
    • Kawabata, T.1
  • 19
    • 77951925741 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress inflammatory activation of rheumatoid arthritis patient synovial macrophages and tissue
    • Grabiec AM, et al. (2010) Histone deacetylase inhibitors suppress inflammatory activation of rheumatoid arthritis patient synovial macrophages and tissue. J. Immunol. 184:2718-28.
    • (2010) J. Immunol , vol.184 , pp. 2718-2728
    • Grabiec, A.M.1
  • 20
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato RR, et al. (2003) Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol. Cancer Ther. 2:1273-84.
    • (2003) Mol. Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.R.1
  • 21
    • 77954752923 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors MS-275 and SAHA induced growth arrest and suppressed lipopolysaccharide-stimulated NF-kappaBp65 nuclear accumulation in human rheumatoid arthritis synovial fibro -blastic E11 cells
    • Choo QY, et al. (2010) Histone deacetylase inhibitors MS-275 and SAHA induced growth arrest and suppressed lipopolysaccharide-stimulated NF-kappaBp65 nuclear accumulation in human rheumatoid arthritis synovial fibro -blastic E11 cells. Rheumatology. 49:1447-60.
    • (2010) Rheumatology , vol.49 , pp. 1447-1460
    • Choo, Q.Y.1
  • 22
    • 44549083450 scopus 로고    scopus 로고
    • Trichostatin A, a histone deacetylase inhibitor, suppresses synovial inflammation and subsequent cartilage destruction in a collagen antibody-induced arthritis mouse model
    • Nasu Y, et al. (2008) Trichostatin A, a histone deacetylase inhibitor, suppresses synovial inflammation and subsequent cartilage destruction in a collagen antibody-induced arthritis mouse model. Osteoarthritis Cartilage. 16:723-32.
    • (2008) Osteoarthritis Cartilage , vol.16 , pp. 723-732
    • Nasu, Y.1
  • 23
    • 5644239630 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suppression of autoantibody-mediated arthritis in mice via regulation of p16INK4a and p21(WAF1/Cip1) expression
    • Nishida K, et al. (2004) Histone deacetylase inhibitor suppression of autoantibody-mediated arthritis in mice via regulation of p16INK4a and p21(WAF1/Cip1) expression. Arthritis Rheum. 50:3365-76.
    • (2004) Arthritis Rheum , vol.50 , pp. 3365-3376
    • Nishida, K.1
  • 24
    • 79957951510 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors for treating a spectrum of diseases not related to cancer
    • Dinarello CA, Fossati G, Mascagni P. (2011) Histone deacetylase inhibitors for treating a spectrum of diseases not related to cancer. Mol. Med. 17:333-352.
    • (2011) Mol. Med , vol.17 , pp. 333-352
    • Dinarello, C.A.1    Fossati, G.2    Mascagni, P.3
  • 25
    • 70349385423 scopus 로고    scopus 로고
    • Deacetylase inhibition increases regulatory T cell function and decreases incidence and severity of collagen-induced arthritis
    • Saouaf SJ, et al. (2009). Deacetylase inhibition increases regulatory T cell function and decreases incidence and severity of collagen-induced arthritis. Exp. Mol. Pathol. 87:99-104.
    • (2009) Exp. Mol. Pathol , vol.87 , pp. 99-104
    • Saouaf, S.J.1
  • 26
    • 0019137699 scopus 로고
    • Identification of catabolin, a protein fro synovium which induces degradation of cartilage in organ culture
    • Saklatvala J, Dingle JT. (1980) Identification of catabolin, a protein fro synovium which induces degradation of cartilage in organ culture. Biochem. Biophys. Res. Commun. 96:1225-31.
    • (1980) Biochem. Biophys. Res. Commun , vol.96 , pp. 1225-1231
    • Saklatvala, J.1    Dingle, J.T.2
  • 27
    • 73649088291 scopus 로고    scopus 로고
    • Local interleukin-1-driven joint pathology is dependent on toll-like receptor 4 activation
    • Abdollahi-Roodsaz S, et al. (2009) Local interleukin-1-driven joint pathology is dependent on toll-like receptor 4 activation. Am. J. Pathol. 175:2004-13.
    • (2009) Am. J. Pathol , vol.175 , pp. 2004-2013
    • Abdollahi-Roodsaz, S.1
  • 28
    • 0032169765 scopus 로고    scopus 로고
    • Different roles of tumour necrosis factor alpha and interleukin 1 in murine streptococcal cell wall arthritis
    • Kuiper S, et al. (1998) Different roles of tumour necrosis factor alpha and interleukin 1 in murine streptococcal cell wall arthritis. Cytokine. 10:690-702.
    • (1998) Cytokine , vol.10 , pp. 690-702
    • Kuiper, S.1
  • 29
    • 0032752705 scopus 로고    scopus 로고
    • IL-1 alpha beta blockade prevents cartilage and bone destruction in murine type II collagen-induced arthritis, whereas TNF-alpha blockade only ameliorates joint inflammation
    • Joosten LA, et al. (1999) IL-1 alpha beta blockade prevents cartilage and bone destruction in murine type II collagen-induced arthritis, whereas TNF-alpha blockade only ameliorates joint inflammation. J. Immunol. 163:5049-55.
    • (1999) J. Immunol , vol.163 , pp. 5049-5055
    • Joosten, L.A.1
  • 30
    • 38149108323 scopus 로고    scopus 로고
    • T cell dependence of chronic destructive murine arthritis induced by repeated local activation of Toll-like receptor-driven pathways: Crucial role of both interleukin-1beta and interleukin-17
    • Joosten LA, et al. (2008) T cell dependence of chronic destructive murine arthritis induced by repeated local activation of Toll-like receptor-driven pathways: crucial role of both interleukin-1beta and interleukin-17. Arthritis Rheum. 58:98-108.
    • (2008) Arthritis Rheum , vol.58 , pp. 98-108
    • Joosten, L.A.1
  • 31
    • 10744223444 scopus 로고    scopus 로고
    • Toll-like receptor 2 pathway drives streptococcal cell wall-induced joint inflammation: Critical role of myeloid differentiation factor 88
    • Joosten LA, et al. (2003) Toll-like receptor 2 pathway drives streptococcal cell wall-induced joint inflammation: critical role of myeloid differentiation factor 88. J. Immunol. 171:6145-53.
    • (2003) J. Immunol , vol.171 , pp. 6145-6153
    • Joosten, L.A.1
  • 32
    • 48249109581 scopus 로고    scopus 로고
    • Differential function of the NACHT-LRR (NLR) members Nod1 and Nod2 in arthritis
    • Joosten LA, et al. (2008) Differential function of the NACHT-LRR (NLR) members Nod1 and Nod2 in arthritis. Proc. Natl. Acad. Sci. U.S.A. 105:9017-22.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 9017-9022
    • Joosten, L.A.1
  • 33
    • 34047210698 scopus 로고    scopus 로고
    • Anti-rheumatic activities of histone deacetylase (HDAC) inhibitors in vivo in collagen-induced arthritis in rodents
    • Lin HS, et al. (2007) Anti-rheumatic activities of histone deacetylase (HDAC) inhibitors in vivo in collagen-induced arthritis in rodents. Br. J. Pharmacol. 150:862-72.
    • (2007) Br. J. Pharmacol , vol.150 , pp. 862-872
    • Lin, H.S.1
  • 34
    • 34547436716 scopus 로고    scopus 로고
    • TNF-induced structural joint damage is mediated by IL-1
    • Zwerina J, et al. (2007) TNF-induced structural joint damage is mediated by IL-1. Proc. Natl. Acad. Sci. U.S.A. 104:11742-7.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 11742-11747
    • Zwerina, J.1
  • 35
    • 73449088382 scopus 로고    scopus 로고
    • Interleukin-1 is essential for systemic inflammatory bone loss
    • Polzer K, et al. (2010) Interleukin-1 is essential for systemic inflammatory bone loss. Ann. Rheum. Dis. 69:284-90.
    • (2010) Ann. Rheum. Dis , vol.69 , pp. 284-290
    • Polzer, K.1
  • 36
    • 0022644438 scopus 로고
    • Actions of recombi-nant interleukin 1, interleukin 2, and interferon-gamma on bone resorption in vitro
    • Gowen M, Mundy GR. (1986) Actions of recombi-nant interleukin 1, interleukin 2, and interferon-gamma on bone resorption in vitro. J. Immunol. 136:2478-82.
    • (1986) J. Immunol , vol.136 , pp. 2478-2482
    • Gowen, M.1    Mundy, G.R.2
  • 37
    • 70350182197 scopus 로고    scopus 로고
    • Trichostatin A inhibits os-teoclastogenesis and bone resorption by suppressing the induction of c-Fos by RANKL
    • Kim HN, et al. (2009) Trichostatin A inhibits os-teoclastogenesis and bone resorption by suppressing the induction of c-Fos by RANKL. Eur. J. Pharmacol. 623:22-9.
    • (2009) Eur. J. Pharmacol , vol.623 , pp. 22-29
    • Kim, H.N.1
  • 38
    • 27144487343 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase suppresses osteoclastogenesis and bone destruction by inducing IFN-beta production
    • Nakamura T, et al. (2005) Inhibition of histone deacetylase suppresses osteoclastogenesis and bone destruction by inducing IFN-beta production. J. Immunol. 175:5809-16.
    • (2005) J. Immunol , vol.175 , pp. 5809-5816
    • Nakamura, T.1
  • 39
    • 21644471962 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors modulate metalloproteinase gene expression in chondrocytes and block cartilage resorp-tion
    • Young DA, et al. (2005) Histone deacetylase inhibitors modulate metalloproteinase gene expression in chondrocytes and block cartilage resorp-tion. Arthritis Res. Ther. 7:R503-12.
    • (2005) Arthritis Res. Ther , vol.7
    • Young, D.A.1
  • 40
    • 58149123407 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases antagonized FGF2 and IL-1beta effects on MMP expression in human articular chondrocytes
    • Wang X, Song Y, Jacobi JL, Tuan RS. (2009) Inhibition of histone deacetylases antagonized FGF2 and IL-1beta effects on MMP expression in human articular chondrocytes. Growth Factors. 27:40-9.
    • (2009) Growth Factors , vol.27 , pp. 40-49
    • Wang, X.1    Song, Y.2    Jacobi, J.L.3    Tuan, R.S.4
  • 41
    • 76649099170 scopus 로고    scopus 로고
    • Correlation between MMP-13 and HDAC7 expression in human knee osteoarthritis
    • Higashiyama R, et al. (2010) Correlation between MMP-13 and HDAC7 expression in human knee osteoarthritis. Mod. Rheumatol. 20:11-7.
    • (2010) Mod. Rheumatol , vol.20 , pp. 11-17
    • Higashiyama, R.1


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