Evidence map›Paper›PMID 27085702›Full record

ArticleCellular and molecular life sciences : CMLS2016

HspB5/αB-crystallin increases dendritic complexity and protects the dendritic arbor during heat shock in cultured rat hippocampal neurons.

Britta Bartelt-Kirbach, Margarethe Moron, Maximilian Glomb, Clara-Maria Beck, Marie-Pascale Weller, Nikola Golenhofen

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  6. Article
  7. Homeostatic Roles of the Proteostasis Network in Dendrites.Frontiers in cellular neuroscience · 2020
    Review
  8. Article
  9. Heat-Shock Proteins in Neuroinflammation.Frontiers in pharmacology · 2019
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
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 1 institution in 1 country.

Britta Bartelt-KirbachInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Margarethe MoronInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Maximilian GlombInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Clara-Maria BeckInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Marie-Pascale WellerInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Nikola GolenhofenInstitute of Anatomy and Cell Biology, University of Ulm, Albert-Einstein-Allee 11, 89081, Ulm, Germany. nikola.golenhofen@uni-ulm.de.
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small heat shock protein ΗspΒ5 (αB-crystallin) exhibits generally cytoprotective functions and possesses powerful neuroprotective capacity in the brain. However, little is known about the mode of action of ΗspΒ5 or other members of the HspB family particularly in neurons. To get clues of the neuronal function of HspBs, we overexpressed several HspBs in cultured rat hippocampal neurons and investigated their effect on neuronal morphology and stress resistance. Whereas axon length and synapse density were not affected by any HspB, dendritic complexity was enhanced by HspB5 and, to a lesser extent, by HspB6. Furthermore, we could show that this process was dependent on phosphorylation, since a non-phosphorylatable mutant of HspB5 did not show this effect. Rarefaction of the dendritic arbor is one hallmark of several neurodegenerative diseases. To investigate if HspB5, which is upregulated at pathophysiological conditions, might be able to protect dendrites during such situations, we exposed HspB5 overexpressing neuronal cultures to heat shock. HspB5 prevented heat shock-induced rarefaction of dendrites. In conclusion, we identified regulation of dendritic complexity as a new function of HspB5 in hippocampal neurons.

Indexed as

Heat-Shock ResponseNeuroprotectionAnimalsCells, CulturedCrystallinsDendritesHippocampusLentivirusMicrotubule-Associated ProteinsMutagenesis, Site-DirectedPhosphorylationRatsSynapsesTransduction, GeneticcryaB protein, ratCrystallinsMicrotubule-Associated ProteinsDendritic branchingHippocampusNeuroprotectionSmall heat shock proteinsStress tolerance

Identifiers

PMID27085702
PMCPMC11108385
OpenAlexW2338977713

What OpenQuestion holds

Textmetadata
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.