Heat Shock Protein 27 Plays a Pivotal Role in Myofibroblast Differentiation and in the Development of Bleomycin-Induced Pulmonary Fibrosis
Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse l...
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| Vydáno v: | PloS one Ročník 11; číslo 2; s. e0148998 |
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| Hlavní autoři: | , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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United States
Public Library of Science
09.02.2016
Public Library of Science (PLoS) |
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| ISSN: | 1932-6203, 1932-6203 |
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| Abstract | Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-β1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with α-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and α-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases. |
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| AbstractList | Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-β1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with α-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and α-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases. Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor [beta]1 (TGF-[beta]1), we observed upregulation of HSP27 along with that of [alpha]-smooth muscle actin ([alpha]-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-[beta]1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with [alpha]-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and [alpha]-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases. Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-β1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with α-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and α-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases.Heat shock protein 27 (HSP27) is a member of the small molecular weight HSP family. Upon treatment with transforming growth factor β1 (TGF-β1), we observed upregulation of HSP27 along with that of α-smooth muscle actin (α-SMA), a marker of myofibroblast differentiation, in cultured human and mouse lung fibroblasts. Furthermore, by using siRNA knockdown, we demonstrated that HSP27 was involved in cell survival and upregulation of fibronectin, osteopontin (OPN) and type 1 collagen, all functional markers of myofibroblast differentiation, in TGF-β1-treated MRC-5 cells. In lung tissues of bleomycin-treated mice, HSP27 was strongly upregulated and substantially co-localized with α-SMA, OPN and type I collagen but not with proSP-C (a marker of type II alveolar epithelial cells), E-cadherin (a marker of epithelial cells) or F4/80 (a marker of macrophages). A similar co-localization of HSP27 and α-SMA was observed in lung tissues of patients with idiopathic pulmonary fibrosis. Furthermore, airway delivery of HSP27 siRNA effectively suppressed bleomycin-induced pulmonary fibrosis in mice. Collectively, our findings indicate that HSP27 is critically involved in myofibroblast differentiation of lung fibroblasts and may be a promising therapeutic target for lung fibrotic diseases. |
| Audience | Academic |
| Author | Yoshie, Osamu Itoh, Tatsuki Sato, Takao Park, Ah-Mee Selman, Moises Kanai, Kyosuke Tsukui, Tatsuya Inagaki, Yutaka Matsushima, Kouji |
| AuthorAffiliation | Medical University of South Carolina, UNITED STATES 5 Instituto Nacional de Enfermedades Respiratorias, México DF, Mexico 2 Department of Pathology, Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan 3 Department of Molecular Preventive Medicine, Graduate School of Medicine, University of Tokyo, Tokyo, Japan 4 Department of Regenerative Medicine, Tokai University School of Medicine, Sagamihara, Kanagawa, Japan 1 Department of Microbiology and Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan |
| AuthorAffiliation_xml | – name: 4 Department of Regenerative Medicine, Tokai University School of Medicine, Sagamihara, Kanagawa, Japan – name: 5 Instituto Nacional de Enfermedades Respiratorias, México DF, Mexico – name: 3 Department of Molecular Preventive Medicine, Graduate School of Medicine, University of Tokyo, Tokyo, Japan – name: 1 Department of Microbiology and Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan – name: Medical University of South Carolina, UNITED STATES – name: 2 Department of Pathology, Kindai University Faculty of Medicine, Osaka-Sayama, Osaka, Japan |
| Author_xml | – sequence: 1 givenname: Ah-Mee surname: Park fullname: Park, Ah-Mee – sequence: 2 givenname: Kyosuke surname: Kanai fullname: Kanai, Kyosuke – sequence: 3 givenname: Tatsuki surname: Itoh fullname: Itoh, Tatsuki – sequence: 4 givenname: Takao surname: Sato fullname: Sato, Takao – sequence: 5 givenname: Tatsuya surname: Tsukui fullname: Tsukui, Tatsuya – sequence: 6 givenname: Yutaka surname: Inagaki fullname: Inagaki, Yutaka – sequence: 7 givenname: Moises surname: Selman fullname: Selman, Moises – sequence: 8 givenname: Kouji surname: Matsushima fullname: Matsushima, Kouji – sequence: 9 givenname: Osamu surname: Yoshie fullname: Yoshie, Osamu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26859835$$D View this record in MEDLINE/PubMed |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Competing Interests: The authors have declared that no competing interests exist. Conceived and designed the experiments: AMP OY. Performed the experiments: AMP KK TI TT. Analyzed the data: AMP KK TI OY. Contributed reagents/materials/analysis tools: TS YI MS KM. Wrote the paper: AMP MS OY. |
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| SubjectTerms | Actin Actins - physiology Aged Alveoli Animal tissues Animals Antibiotics Biocompatibility Biology and Life Sciences Biomedical materials Bleomycin Bleomycin - pharmacology Cell Differentiation - drug effects Cell Differentiation - physiology Cell Line Cell survival Collagen (type I) Collagen Type I - physiology Differentiation E-cadherin Epithelial cells Female Fibroblasts Fibroblasts - drug effects Fibroblasts - physiology Fibronectin Fibronectins - physiology Fibrosis Gene Knockdown Techniques Genetic aspects Growth factors Heat shock proteins HSP27 Heat-Shock Proteins - physiology Hsp27 protein Humans Idiopathic Pulmonary Fibrosis - physiopathology Immunoglobulins Kidneys Localization Lung diseases Macrophages Male Medical prognosis Medicine and Health Sciences Mice Molecular weight Myofibroblasts - physiology Osteopontin Osteopontin - physiology Physiological aspects Polymerase Chain Reaction Polymerization Preventive medicine Pulmonary fibrosis Pulmonary Fibrosis - chemically induced Pulmonary Fibrosis - physiopathology Research and Analysis Methods Respiratory tract Risk factors Rodents siRNA Smooth muscle Transforming growth factor Transforming Growth Factor beta1 - physiology Transforming growth factor-b1 University faculty |
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| Title | Heat Shock Protein 27 Plays a Pivotal Role in Myofibroblast Differentiation and in the Development of Bleomycin-Induced Pulmonary Fibrosis |
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