Evidence map›Paper›PMID 28236106›Full record

ArticleJournal of assisted reproduction and genetics2017

Progesterone requires heat shock protein 90 (HSP90) in human sperm to regulate motility and acrosome reaction.

Vrushali Sagare-Patil, Rashmi Bhilawadikar, Mosami Galvankar, Kusum Zaveri, Indira Hinduja, Deepak Modi

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Journal of assisted reproduction and genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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, 49 citations in OpenAlex.

  1. Article
  2. Review
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  12. Trendiness in human ARTs as technology transits from the macro to nano.Journal of assisted reproduction and genetics · 2017
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Vrushali Sagare-PatilMolecular and Cellular Biology Laboratory, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012, India.
Rashmi BhilawadikarHinduja IVF Centre, PD Hinduja Hospital and Medical Research Center, Veer Savarkar Marg, Mahim, Mumbai, 400016, India.
Mosami GalvankarMolecular and Cellular Biology Laboratory, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012, India.
Kusum ZaveriHinduja IVF Centre, PD Hinduja Hospital and Medical Research Center, Veer Savarkar Marg, Mahim, Mumbai, 400016, India.
Indira HindujaHinduja IVF Centre, PD Hinduja Hospital and Medical Research Center, Veer Savarkar Marg, Mahim, Mumbai, 400016, India.
Deepak ModiMolecular and Cellular Biology Laboratory, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012, India. deepaknmodi@yahoo.com.ORCID http://orcid.org/0000-0002-4230-4219
National Institute for Research in Reproductive Health · INP. D. Hinduja Hospital and Medical Research Centre · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeThe aims of this paper were to study whether heat shock protein 90 (HSP90) is a regulator of sperm functions and to determine its association with oligoasthenozoospermia.

methodsThe levels of HSP90 in sperm lysates were measured by ELISA. Localization of HSP90 and its isoforms was evaluated by immunofluorescence. Sperm motility and kinetics were assessed by computer-assisted sperm analysis. Acrosome reaction was determined by lectin staining.

resultsThe levels of HSP90 were lower in oligoasthenozoospermic men and correlated positively with the number of motile spermatozoa. In capacitated human spermatozoa, HSP90α was mostly found in residual nuclear envelope, and the HSP90β isoform was higher in the flagella. Inhibition of HSP90 by geldanamycin or 17-AAG did not affect basal motility, but suppressed progesterone-mediated forward progressive motility, hyperactivation and acrosome reaction. Progesterone treatment dephosphorylated both HSP90α and HSP90β at Ser/Thr-Pro residues, but not Tyr residues.

conclusionHSP90 levels are downregulated in oligoasthenozoospermia, and its functional inhibition attenuates progesterone-mediated sperm motility and acrosome reaction.

Indexed as

Acrosome ReactionBenzoquinonesGene Expression Regulation, DevelopmentalHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicMaleOligospermiaProgesteroneSemen AnalysisSpermatozoaSperm CapacitationSperm MotilityBenzoquinonesgeldanamycinHSP90 Heat-Shock ProteinsLactams, MacrocyclicProgesteronetanespimycinAcrosome reactionHeat shock proteinHSP90Human spermMotilityOligoasthenozoospermiaPhosphorylationProgesterone

Identifiers

PMID28236106
PMCPMC5401699
OpenAlexW2591560056

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.