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Cited by 9Heat shock proteins researchAlzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis Research

Expression of one important chaperone protein, heat shock protein 27, in neurodegenerative diseases

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Zhang, Xuekai, Shi, Jing, Tian, Jinzhou, Robinson, Andrew C, Davidson, Yvonne S, Mann, David M·2014·Alzheimer's Research & Therapy
DOI 10.1186/s13195-014-0078-xPMC PMC4304251
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Abstract

Introduction: Many neurodegenerative diseases are characterised by accumulations of misfolded proteins that can colocalise with chaperone proteins (for example, heat shock protein 27 (HSP27)), which might act as modulators of protein aggregation. Methods: The role of HSP27 in the pathogenesis of neurodegenerative disorders such as frontotemporal lobar degeneration (FTLD), Alzheimer’s disease (AD) and motor neuron disease (MND) was investigated. We used immunohistochemical and Western blot analysis to determine the distribution and amount of this protein in the frontal and temporal cortices of diseased and control subjects. Results: HSP27 immunostaining presented as accumulations of granules within neuronal and glial cell perikarya. Patients with AD and FTLD were affected more often, and showed greater immunostaining for HSP27, than patients with MND and controls. In FTLD, there was no association between HSP27 and histological type. The neuropathological changes of FTLD, AD and MND were not immunoreactive to HSP27. Western blot analysis revealed higher HSP27 expression in FTLD than in controls, but without qualitative differences in banding patterns. Conclusions: The pattern of HSP27 immunostaining observed may reflect the extent of ongoing neurodegeneration in affected brain areas and is not specific to FTLD, AD or MND. It may represent an accumulation of misfolded, damaged or unwanted proteins, awaiting or undergoing degradation.

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  • ER chaperones and small heat-shock proteins likely increase in neurons and glia in AD at the late stage.

    “ER chaperones and small heat-shock proteins likely increase in neurons and glia in AD at the late stage [29, 30].”

    From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [30]

    The Results and Discussion report greater HSP27 staining in neurons and glial cells in AD than in controls. HSP27 is a small heat-shock protein, but these passages do not establish an increase in ER chaperones or identify the increase as specific to late-stage AD. Page numbers are unavailable in our copy. (LLM, conf=0.88)

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Research works printed but not linked: 28

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Sorted by citations

Authors
Zhang, X., Shi, J., Tian, J., Robinson, A. C., Davidson, Y. S., & Mann, D. M.
Affiliations
  • Beijing University of Chinese Medicine (CN)
  • University of Manchester (GB)
  • Salford Royal NHS Foundation Trust (GB)
Corresponding author
  • Tian, Jinzhou
  • Mann, David M
ORCID
Venue
Alzheimer's Research & Therapy
Publisher
Springer Science and Business Media LLC
Published
2014-12-17
Volume
6
Issue
9
Pages
78-78
ISSN
1758-9193 (ISSN-L)
DOI
10.1186/s13195-014-0078-x
PMC
PMC4304251
OpenAlex
W2068763229
Cited by
9
References
0
Citations by year
2026: 1 · 2022: 2 · 2021: 1 · 2019: 4 · 2017: 1
FWCI
0.14
Type
journal article
Language
en
Open access
Licence
Locations
  • Alzheimer s Research & Therapy (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (publishedVersion)
Funders
  • Alzheimer's Society
  • University of Manchester
  • Beijing University of Chinese Medicine (2011-CXTD-21, Z111107056811043, B08006, 2011ZX09302-006-01)
  • Higher Education Discipline Innovation Project (B08006, 2011ZX09302-006-01, 2011-CXTD-21, Z111107056811043)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
Keywords
HSP27, neurodegenerative diseases, frontotemporal lobar degeneration, Alzheimer's disease, motor neuron disease, protein misfolding, protein aggregation, molecular chaperones, frontal and temporal cortex, neuropathology

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