Evidence map›Paper›PMID 21932106›Full record

ArticleJournal of the Association for Research in Otolaryngology : JARO2012

Induction of heat shock proteins by hyperthermia and noise overstimulation in hsf1 -/- mice.

Tzy-Wen Gong, Damon A Fairfield, Lynne Fullarton, David F Dolan, Richard A Altschuler, David C Kohrman, Margaret I Lomax

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the Association for Research in Otolaryngology : JARO, 2012. 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
0.8field-weighted citation impact, top 29% 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, 38 citations in OpenAlex.

  1. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
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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

7 authors at 1 institution in 1 country.

Tzy-Wen GongDepartment of Otolaryngology/Head Neck Surgery, Kresge Hearing Research Institute, University of Michigan, Ann Arbor, MI 48109-5648, USA.
Damon A Fairfield
Lynne Fullarton
David F Dolan
Richard A Altschuler
David C Kohrman
Margaret I Lomax
University of Michigan–Ann Arbor · US

Funding

Scientific Synergy CoreP30DC005188 · NIDCD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DOLAN, DAVID FRANCIS · 2002 to 2016
$10.3M
Sensory Mechanisms and Disorders - Administrative SupplementT32DC000011 · NIDCD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Michael Thomas Roberts · 1989 to 2026
$9.5M
STRESS PATHWAYS IN THE AGING COCHLEAP01AG025164 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHACHT, JOCHEN · 2005 to 2009
$6.6M
NIA NIH HHS P01 AG025164NIDCD NIH HHS P30 DC005188NIDCD NIH HHS T32 DC000011NIDCD NIH HHS T32 DC00011PHS HHS P30 DCO5188
6 · The paper itself

Abstract

Diverse cellular and environmental stresses can activate the heat shock response, an evolutionarily conserved mechanism to protect proteins from denaturation. Stressors activate heat shock transcription factor 1 (HSF1), which binds to heat shock elements in the genes for heat shock proteins, leading to rapid induction of these important molecular chaperones. Both heat and noise stress are known to activate the heat shock response in the cochlea and protect it from subsequent noise trauma. However, the contribution of HSF1 to induction of heat shock proteins following noise trauma has not been investigated at the molecular level. We evaluated the role of HSF1 in the cochlea following noise stress by examining induction of heat shock proteins in Hsf1 ( +/- ) control and Hsf1 ( -/- ) mice. Heat stress rapidly induced expression of Hsp25, Hsp47, Hsp70.1, Hsp70.3, Hsp84, Hsp86, and Hsp110 in the cochleae of wild-type and Hsf1 ( +/- ) mice, but not in Hsf1 ( -/- ) mice, confirming the essential role of HSF1 in mediating the heat shock response. Exposure to broadband noise (2-20 kHz) at 106 dB SPL for 2 h produced partial hearing loss. Maximal induction of heat shock proteins occurred 4 h after the noise. In comparison to heat stress, noise stress resulted in lower induced levels of Hsp25, Hsp70.1, Hsp70.3, Hsp86, and Hsp110 in Hsf1 ( +/- ) mice. Induction of these heat shock proteins was attenuated, but not completely eliminated, in Hsf1 ( -/- ) mice. These same noise exposure conditions induced genes for several immediate early transcription factors and maximum induction occurred earlier than for heat shock proteins. Thus, additional signaling pathways and transcriptional regulators that are activated by noise probably contribute to induction of heat shock proteins in the cochlea.

Indexed as

AnimalsCochleaDNA-Binding ProteinsFemaleFeverGene ExpressionGenes, Immediate-EarlyHearing Loss, Noise-InducedHeat-Shock ProteinsHeat Shock Transcription FactorsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMaleMiceMice, 129 StrainMice, Inbred BALB CDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHsbp1 protein, mouseHsf1 protein, mouseHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHspca protein, mouseMolecular ChaperonesNeoplasm ProteinsTranscription Factors

Identifiers

PMID21932106
PMCPMC3254713
OpenAlexW2057182702

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.