Histone deacetylases are critical targets of bortezomib-induced cytotoxicity in multiple myeloma
Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results, recent investigations have indicated that bortezomib does not inactivate nuclear factor-κB activity in MM cells, suggesting the presence of...
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Published in | Blood Vol. 116; no. 3; pp. 406 - 417 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Washington, DC
Elsevier Inc
22.07.2010
Americain Society of Hematology |
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Abstract | Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results, recent investigations have indicated that bortezomib does not inactivate nuclear factor-κB activity in MM cells, suggesting the presence of other critical pathways leading to cytotoxicity. In this study, we show that histone deacetylases (HDACs) are critical targets of bortezomib, which specifically down-regulated the expression of class I HDACs (HDAC1, HDAC2, and HDAC3) in MM cell lines and primary MM cells at the transcriptional level, accompanied by reciprocal histone hyperacetylation. Transcriptional repression of HDACs was mediated by caspase-8–dependent degradation of Sp1 protein, the most potent transactivator of class I HDAC genes. Short-interfering RNA-mediated knockdown of HDAC1 enhanced bortezomib-induced apoptosis and histone hyperacetylation, whereas HDAC1 overexpression inhibited them. HDAC1 overexpression conferred resistance to bortezomib in MM cells, and administration of the HDAC inhibitor romidepsin restored sensitivity to bortezomib in HDAC1-overexpressing cells both in vitro and in vivo. These results suggest that bortezomib targets HDACs via distinct mechanisms from conventional HDAC inhibitors. Our findings provide a novel molecular basis and rationale for the use of bortezomib in MM treatment. |
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AbstractList | Abstract
Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results, recent investigations have indicated that bortezomib does not inactivate nuclear factor-κB activity in MM cells, suggesting the presence of other critical pathways leading to cytotoxicity. In this study, we show that histone deacetylases (HDACs) are critical targets of bortezomib, which specifically down-regulated the expression of class I HDACs (HDAC1, HDAC2, and HDAC3) in MM cell lines and primary MM cells at the transcriptional level, accompanied by reciprocal histone hyperacetylation. Transcriptional repression of HDACs was mediated by caspase-8–dependent degradation of Sp1 protein, the most potent transactivator of class I HDAC genes. Short-interfering RNA-mediated knockdown of HDAC1 enhanced bortezomib-induced apoptosis and histone hyperacetylation, whereas HDAC1 overexpression inhibited them. HDAC1 overexpression conferred resistance to bortezomib in MM cells, and administration of the HDAC inhibitor romidepsin restored sensitivity to bortezomib in HDAC1-overexpressing cells both in vitro and in vivo. These results suggest that bortezomib targets HDACs via distinct mechanisms from conventional HDAC inhibitors. Our findings provide a novel molecular basis and rationale for the use of bortezomib in MM treatment. Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results, recent investigations have indicated that bortezomib does not inactivate nuclear factor-κB activity in MM cells, suggesting the presence of other critical pathways leading to cytotoxicity. In this study, we show that histone deacetylases (HDACs) are critical targets of bortezomib, which specifically down-regulated the expression of class I HDACs (HDAC1, HDAC2, and HDAC3) in MM cell lines and primary MM cells at the transcriptional level, accompanied by reciprocal histone hyperacetylation. Transcriptional repression of HDACs was mediated by caspase-8–dependent degradation of Sp1 protein, the most potent transactivator of class I HDAC genes. Short-interfering RNA-mediated knockdown of HDAC1 enhanced bortezomib-induced apoptosis and histone hyperacetylation, whereas HDAC1 overexpression inhibited them. HDAC1 overexpression conferred resistance to bortezomib in MM cells, and administration of the HDAC inhibitor romidepsin restored sensitivity to bortezomib in HDAC1-overexpressing cells both in vitro and in vivo. These results suggest that bortezomib targets HDACs via distinct mechanisms from conventional HDAC inhibitors. Our findings provide a novel molecular basis and rationale for the use of bortezomib in MM treatment. Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results, recent investigations have indicated that bortezomib does not inactivate nuclear factor-kappaB activity in MM cells, suggesting the presence of other critical pathways leading to cytotoxicity. In this study, we show that histone deacetylases (HDACs) are critical targets of bortezomib, which specifically down-regulated the expression of class I HDACs (HDAC1, HDAC2, and HDAC3) in MM cell lines and primary MM cells at the transcriptional level, accompanied by reciprocal histone hyperacetylation. Transcriptional repression of HDACs was mediated by caspase-8-dependent degradation of Sp1 protein, the most potent transactivator of class I HDAC genes. Short-interfering RNA-mediated knockdown of HDAC1 enhanced bortezomib-induced apoptosis and histone hyperacetylation, whereas HDAC1 overexpression inhibited them. HDAC1 overexpression conferred resistance to bortezomib in MM cells, and administration of the HDAC inhibitor romidepsin restored sensitivity to bortezomib in HDAC1-overexpressing cells both in vitro and in vivo. These results suggest that bortezomib targets HDACs via distinct mechanisms from conventional HDAC inhibitors. Our findings provide a novel molecular basis and rationale for the use of bortezomib in MM treatment. |
Author | Noborio-Hatano, Kaoru Ozawa, Keiya Furukawa, Yusuke Wada, Taeko Nobuyoshi, Masaharu Kano, Yasuhiko Mitsunaga, Kanae Izumi, Tohru Kikuchi, Jiro Shimizu, Rumi Akutsu, Miyuki |
Author_xml | – sequence: 1 givenname: Jiro surname: Kikuchi fullname: Kikuchi, Jiro organization: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Shimotsuke, Tochigi – sequence: 2 givenname: Taeko surname: Wada fullname: Wada, Taeko organization: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Shimotsuke, Tochigi – sequence: 3 givenname: Rumi surname: Shimizu fullname: Shimizu, Rumi organization: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Shimotsuke, Tochigi – sequence: 4 givenname: Tohru surname: Izumi fullname: Izumi, Tohru organization: Division of Hematology, Tochigi Cancer Center, Utsunomiya, Tochigi; and – sequence: 5 givenname: Miyuki surname: Akutsu fullname: Akutsu, Miyuki organization: Division of Hematology, Tochigi Cancer Center, Utsunomiya, Tochigi; and – sequence: 6 givenname: Kanae surname: Mitsunaga fullname: Mitsunaga, Kanae organization: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Shimotsuke, Tochigi – sequence: 7 givenname: Kaoru surname: Noborio-Hatano fullname: Noborio-Hatano, Kaoru organization: Division of Hematology, Department of Internal Medicine, Jichi Medical University, Shimotsuke, Tochigi, Japan – sequence: 8 givenname: Masaharu surname: Nobuyoshi fullname: Nobuyoshi, Masaharu organization: Division of Hematology, Department of Internal Medicine, Jichi Medical University, Shimotsuke, Tochigi, Japan – sequence: 9 givenname: Keiya surname: Ozawa fullname: Ozawa, Keiya organization: Division of Hematology, Department of Internal Medicine, Jichi Medical University, Shimotsuke, Tochigi, Japan – sequence: 10 givenname: Yasuhiko surname: Kano fullname: Kano, Yasuhiko organization: Division of Hematology, Tochigi Cancer Center, Utsunomiya, Tochigi; and – sequence: 11 givenname: Yusuke surname: Furukawa fullname: Furukawa, Yusuke email: furuyu@jichi.ac.jp organization: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Shimotsuke, Tochigi |
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Keywords | Antineoplastic agent Immunopathology Histone deacetylase Bortezomib Targeting Hematology Cytotoxicity Malignant hemopathy Myeloma Immunoglobulinopathy Analog Proteasome inhibitor Lymphoproliferative syndrome Dipeptides Cancer |
Language | English |
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Snippet | Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial results,... Abstract Bortezomib is now widely used for the treatment of multiple myeloma (MM); however, its action mechanisms are not fully understood. Despite the initial... |
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SubjectTerms | Animals Apoptosis - drug effects Biological and medical sciences Boronic Acids - administration & dosage Boronic Acids - therapeutic use Bortezomib Caspase 8 - metabolism Cell Line, Tumor Depsipeptides - administration & dosage Down-Regulation - drug effects Drug Synergism Gene Knockdown Techniques Hematologic and hematopoietic diseases Histone Deacetylase 1 - genetics Histone Deacetylase Inhibitors - administration & dosage Histone Deacetylase Inhibitors - therapeutic use Histone Deacetylases - classification Histone Deacetylases - genetics Histone Deacetylases - metabolism Humans Immunodeficiencies. Immunoglobulinopathies Immunoglobulinopathies Immunopathology Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis Medical sciences Mice Mice, Inbred NOD Mice, SCID Multiple Myeloma - drug therapy Multiple Myeloma - enzymology Multiple Myeloma - genetics Multiple Myeloma - pathology Pyrazines - administration & dosage Pyrazines - therapeutic use RNA, Small Interfering - genetics Sp1 Transcription Factor - metabolism Xenograft Model Antitumor Assays |
Title | Histone deacetylases are critical targets of bortezomib-induced cytotoxicity in multiple myeloma |
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