Evidence map›Paper›PMID 33147803›Full record

ReviewInternational journal of molecular sciences2020

Are Heat Shock Proteins an Important Link between Type 2 Diabetes and Alzheimer Disease?

Joanne Elizabeth Rowles, Kevin Noel Keane, Thiago Gomes Heck, Vinicius Cruzat, Giuseppe Verdile, Philip Newsholme

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Diabetes, Protein Misfolding, and Heat Stress: Molecular Insights and Translational Perspectives.TH open : companion journal to thrombosis and haemostasis · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Joanne Elizabeth RowlesSchool of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Biosciences, Curtin University, Perth 6102, Australia.
Kevin Noel KeaneSchool of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Biosciences, Curtin University, Perth 6102, Australia.
Thiago Gomes HeckPhysiology Research Group, Graduate Program in Integral Attention to Health (PPGAIS-UNIJUÍ/UNICRUZ) and Graduate Program in Mathematical and Computational Modeling, Regional University of Northwestern Rio Grande do Sul State (UNIJUÍ), Ijuí, RS 98700-000, Brazil.ORCID 0000-0002-1242-5423
Vinicius CruzatFaculty of Health, Torrens University Australia, Melbourne 3000, Australia.ORCID 0000-0001-9879-4985
Giuseppe VerdileSchool of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Biosciences, Curtin University, Perth 6102, Australia.
Philip NewsholmeSchool of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute, Biosciences, Curtin University, Perth 6102, Australia.ORCID 0000-0002-0500-6984
Curtin University · AUEdith Cowan University · AUTorrens University Australia · AUUniversity of Cruz Alta · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type 2 diabetes (T2D) and Alzheimer's disease (AD) are growing in prevalence worldwide. The development of T2D increases the risk of AD disease, while AD patients can show glucose imbalance due to an increased insulin resistance. T2D and AD share similar pathological features and underlying mechanisms, including the deposition of amyloidogenic peptides in pancreatic islets (i.e., islet amyloid polypeptide; IAPP) and brain (β-Amyloid; Aβ). Both IAPP and Aβ can undergo misfolding and aggregation and accumulate in the extracellular space of their respective tissues of origin. As a main response to protein misfolding, there is evidence of the role of heat shock proteins (HSPs) in moderating T2D and AD. HSPs play a pivotal role in cell homeostasis by providing cytoprotection during acute and chronic metabolic stresses. In T2D and AD, intracellular HSP (iHSP) levels are reduced, potentially due to the ability of the cell to export HSPs to the extracellular space (eHSP). The increase in eHSPs can contribute to oxidative damage and is associated with various pro-inflammatory pathways in T2D and AD. Here, we review the role of HSP in moderating T2D and AD, as well as propose that these chaperone proteins are an important link in the relationship between T2D and AD.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsBlood GlucoseDiabetes Mellitus, Type 2Extracellular SpaceHeat-Shock ProteinsHSP72 Heat-Shock ProteinsHumansInflammationModels, BiologicalMolecular ChaperonesProtein BindingProtein Foldingtau ProteinsAmyloid beta-Protein PrecursorAPP protein, humanBlood GlucoseHeat-Shock ProteinsHSP72 Heat-Shock ProteinsMAPT protein, humanMolecular Chaperonestau ProteinsAβdementiaeHSPheat shock protein 70IAPPiHSPtau

Identifiers

PMID33147803
PMCPMC7662599
OpenAlexW3097973234

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.