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CD30 Induces Heat Shock Protein 90 and Signal Integration in Classic Hodgkin Lymphoma Cells.
Watanabe, Mariko; Nakano, Kazumi; Kadin, Marshall E; Higashihara, Masaaki; Watanabe, Toshiki; Horie, Ryouichi.
Afiliación
  • Watanabe M; Department of Hematology, School of Medicine, Kitasato University, Minami-ku, Sagamihara, Kanagawa, Japan.
  • Nakano K; Laboratory of Tumor Cell Biology, Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Tokyo, Japan.
  • Kadin ME; Department of Dermatology and Skin Surgery, Boston University School of Medicine, Roger Williams Medical Center, Providence, Rhode Island.
  • Higashihara M; Department of Hematology, School of Medicine, Kitasato University, Minami-ku, Sagamihara, Kanagawa, Japan.
  • Watanabe T; Laboratory of Tumor Cell Biology, Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Tokyo, Japan.
  • Horie R; Department of Hematology, School of Medicine, Kitasato University, Minami-ku, Sagamihara, Kanagawa, Japan; Division of Hematology, Department of Laboratory Sciences, School of Allied Health Sciences, Kitasato University, Minami-ku, Sagamihara, Kanagawa, Japan. Electronic address: rhorie@med.kitasato
Am J Pathol ; 187(1): 163-175, 2017 Jan.
Article en En | MEDLINE | ID: mdl-27870927
Previous studies report deregulation of multiple signaling pathways in classic Hodgkin lymphoma (cHL) cells. However, the mechanisms of how these pathways are integrated are not fully understood. Herein, we show involvement of cHL hallmark antigen CD30 in this process. CD30 facilitates phosphorylation of heat shock factor 1, activates heat shock promoter element, and induces heat shock protein (HSP) 90. CD30 repression and subsequent inhibition of HSP90 suppresses NF-κB, extracellular signal-regulated kinase, AKT, and STAT pathways in cHL cell lines. Thus, CD30-mediated induction of HSP90 appears to serve as a central hub for integration of intracellular signaling in cHL cells. We also show that CD30 induces HSP90 through phosphorylation of heat shock factor 1 via c-Jun N-terminal kinase in cHL cells. Although anaplastic large-cell lymphoma (ALCL) also is associated with CD30 overexpression, our experiments reveal that HSP90 induction in ALCL-bearing nucleophosmin-anaplastic lymphoma kinase (ALK) does not depend on CD30 but instead on ALK via c-Jun N-terminal kinase. Together, these results highlight a novel role for CD30 in mediating integration of signaling pathways of cHL cells while being replaced in this function by ALK in ALCL cells.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedad de Hodgkin / Transducción de Señal / Antígeno Ki-1 / Proteínas HSP90 de Choque Térmico Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Am J Pathol Año: 2017 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedad de Hodgkin / Transducción de Señal / Antígeno Ki-1 / Proteínas HSP90 de Choque Térmico Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Am J Pathol Año: 2017 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos