The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration
Filamentous tau-positive protein inclusions in neurons and glia are prominent features of a number of neurodegenerative disorders termed tauopathies. These inclusions are further characterized by the presence of heat shock proteins (HSPs). The group of small HSPs, namely, HSP27 and αB-crystallin, in...
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| Format: | Article |
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Wiley
2010-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2010/717520 |
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| author | Lisa Schwarz Grit Vollmer Christiane Richter-Landsberg |
| author_facet | Lisa Schwarz Grit Vollmer Christiane Richter-Landsberg |
| author_sort | Lisa Schwarz |
| collection | DOAJ |
| description | Filamentous tau-positive protein inclusions in neurons and glia are prominent features of a number of neurodegenerative disorders termed tauopathies. These inclusions are further characterized by the presence of heat shock proteins (HSPs). The group of small HSPs, namely, HSP27 and αB-crystallin, interact with the cytoskeleton, bind to nonnative proteins, and prevent their aggregation after stress. To further investigate their contribution to neurodegenerative diseases, we have analyzed the association of HSP27 with pathological lesions of tauopathies. Microarray and immunoblot analysis revealed that HSP27 is enhanced at the mRNA and protein levels in affected brains, and that it is associated with astrocytic pathology. The upregulation of HSP27 in tauopathies with gial pathology implies distinct mechanisms for glial and neuronal cells. This was sustained by cell culture studies, demonstrating that the small HSPs are specifically and prominently expressed in unstressed astrocytes and not in neurons and in neurons remained at a rather low level even after stress situations. |
| format | Article |
| id | doaj-art-c4d9c6c8183140f390fc002085e2a9c3 |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2010-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-c4d9c6c8183140f390fc002085e2a9c32025-02-03T01:23:23ZengWileyInternational Journal of Cell Biology1687-88761687-88842010-01-01201010.1155/2010/717520717520The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal DegenerationLisa Schwarz0Grit Vollmer1Christiane Richter-Landsberg2Department of Biology, Molecular Neurobiology, University of Oldenburg, POB 2503, 26111 Oldenburg, GermanyDepartment of Biology, Molecular Neurobiology, University of Oldenburg, POB 2503, 26111 Oldenburg, GermanyDepartment of Biology, Molecular Neurobiology, University of Oldenburg, POB 2503, 26111 Oldenburg, GermanyFilamentous tau-positive protein inclusions in neurons and glia are prominent features of a number of neurodegenerative disorders termed tauopathies. These inclusions are further characterized by the presence of heat shock proteins (HSPs). The group of small HSPs, namely, HSP27 and αB-crystallin, interact with the cytoskeleton, bind to nonnative proteins, and prevent their aggregation after stress. To further investigate their contribution to neurodegenerative diseases, we have analyzed the association of HSP27 with pathological lesions of tauopathies. Microarray and immunoblot analysis revealed that HSP27 is enhanced at the mRNA and protein levels in affected brains, and that it is associated with astrocytic pathology. The upregulation of HSP27 in tauopathies with gial pathology implies distinct mechanisms for glial and neuronal cells. This was sustained by cell culture studies, demonstrating that the small HSPs are specifically and prominently expressed in unstressed astrocytes and not in neurons and in neurons remained at a rather low level even after stress situations.http://dx.doi.org/10.1155/2010/717520 |
| spellingShingle | Lisa Schwarz Grit Vollmer Christiane Richter-Landsberg The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration International Journal of Cell Biology |
| title | The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration |
| title_full | The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration |
| title_fullStr | The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration |
| title_full_unstemmed | The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration |
| title_short | The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration |
| title_sort | small heat shock protein hsp25 27 hspb1 is abundant in cultured astrocytes and associated with astrocytic pathology in progressive supranuclear palsy and corticobasal degeneration |
| url | http://dx.doi.org/10.1155/2010/717520 |
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