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Cited by 32Heat shock proteins researchGenetic Neurodegenerative DiseasesEndoplasmic Reticulum Stress and Disease

Impact of Heat Shock Proteins in Neurodegeneration: Possible Therapeutical Targets

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Beretta, Giangiacomo, Shala, Aida Loshaj·2022·Annals of Neurosciences
DOI 10.1177/09727531211070528PMC PMC9305912
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Abstract

Background: Human neurodegenerative diseases occur as a result of various factors. Regardless of the variety in the etiology of development, many of these diseases are characterized by the accumulation of pathological, misfolded proteins; hence, such diseases are considered as proteinopathies. While plenty of research study has been conducted in order to identify the pathophysiology of these proteinopathies, there is still a lack of understanding in terms of potential therapeutic targets. Summary: Molecular chaperones present the main workforce for cellular protection and stress response. Therefore, considering these functions, molecular chaperones present a promising target for research within the field of conformational diseases that arise from proteinopathies. Since the association between neurodegenerative disorders and their long-term consequences is well documented, the need for the development of new therapeutic strategies becomes even more critical Key message: In this review, we summarized the molecular function of heat shock proteins and recent progress on their role, involvement, and other mechanisms related to neurodegeneration caused by different etiological factors. Based on the relevant scientific data, we will highlight the functional classification of heat shock proteins, regulation, and their therapeutic potential for neurodegenerative disorders.

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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 [29]

    The “HSP27 in Neurodegenerative Diseases” section says that HSP27, a small heat-shock protein, can increase in neurons and glia in neurodegenerative diseases and discusses its involvement in AD. It does not say that ER chaperones increase in those cells or establish that either increase occurs specifically at a late stage of AD. No page number is available in our copy. (LLM, conf=0.86)

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Sorted by citations

Authors
Beretta, G., & Shala, A. L.
Affiliations
  • University of Milan (IT)
  • University of Prishtina (XK)
Corresponding author
Shala, Aida Loshaj
ORCID
Venue
Annals of Neurosciences
Publisher
SAGE Publications
Published
2022-01
Volume
29
Issue
1
Pages
71-82
ISSN
  • 0972-7531 (ISSN-L)
  • 0976-3260
DOI
10.1177/09727531211070528
PMC
PMC9305912
OpenAlex
W4210278051
Cited by
32
References
4
Citations by year
2026: 5 · 2025: 10 · 2024: 9 · 2023: 7 · 2022: 1
FWCI
0.70
Type
journal article
Language
en
Open access
Licence
Locations
  • Annals of Neurosciences (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Keywords
heat shock proteins, neurodegeneration, proteinopathies, molecular chaperones, protein misfolding, therapeutic target, stress response, protein conformational diseases

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