Evidence map›Paper›PMID 33832207›Full record

ReviewHaematologica2021

The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance.

Yasith Mathangasinghe, Bruno Fauvet, Stephen M Jane, Pierre Goloubinoff, Nadinath B Nillegoda

Open access · goldAbstract readReview
In one paragraph

Review in Haematologica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

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  20. Journal of clinical medicine · 2022
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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

5 authors at 4 institutions in 2 countries.

Yasith MathangasingheAustralian Regenerative Medicine Institute, Monash University, Clayton, Victoria.
Bruno FauvetDepartment of Plant Molecular Biology, Lausanne University, Lausanne.
Stephen M JaneCentral Clinical School, Monash University, Prahran, Victoria, Australia; Department of Hematology, Alfred Hospital, Monash University, Prahran, Victoria.
Pierre GoloubinoffDepartment of Plant Molecular Biology, Lausanne University, Lausanne.
Nadinath B NillegodaAustralian Regenerative Medicine Institute, Monash University, Clayton, Victoria. nadinath.nillegoda@monash.edu.
University of Lausanne · CHAustralian Regenerative Medicine Institute · AUMonash University · AUThe Alfred Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Erythropoiesis is a tightly regulated cell differentiation process in which specialized oxygen- and carbon dioxide-carrying red blood cells are generated in vertebrates. Extensive reorganization and depletion of the erythroblast proteome leading to the deterioration of general cellular protein quality control pathways and rapid hemoglobin biogenesis rates could generate misfolded/aggregated proteins and trigger proteotoxic stresses during erythropoiesis. Such cytotoxic conditions could prevent proper cell differentiation resulting in premature apoptosis of erythroblasts (ineffective erythropoiesis). The heat shock protein 70 (Hsp70) molecular chaperone system supports a plethora of functions that help maintain cellular protein homeostasis (proteostasis) and promote red blood cell differentiation and survival. Recent findings show that abnormalities in the expression, localization and function of the members of this chaperone system are linked to ineffective erythropoiesis in multiple hematological diseases in humans. In this review, we present latest advances in our understanding of the distinct functions of this chaperone system in differentiating erythroblasts and terminally differentiated mature erythrocytes. We present new insights into the protein repair-only function(s) of the Hsp70 system, perhaps to minimize protein degradation in mature erythrocytes to warrant their optimal function and survival in the vasculature under healthy conditions. The work also discusses the modulatory roles of this chaperone system in a wide range of hematological diseases and the therapeutic gain of targeting Hsp70.

Indexed as

HSP70 Heat-Shock ProteinsMolecular ChaperonesAnimalsErythroblastsErythrocytesErythropoiesisHumansHSP70 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID33832207
PMCPMC8168490
OpenAlexW3147086275

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.