Evidence map›Paper›PMID 25865850›Full record

ReviewAsian journal of andrology

The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition.

Brett Nixon, Elizabeth G Bromfield, Matthew D Dun, Kate A Redgrove, Eileen A McLaughlin, R John Aitken

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Asian journal of andrology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. TheFrontiers in molecular biosciences · 2022
    Article
  14. Review
  15. Review
  16. Article
  17. Machine learning for sperm selection.Nature reviews. Urology · 2021
    Review
  18. Article
  19. Article
  20. Identification of Sialyl-Lewis(x)-Interacting Protein on Human Spermatozoa.Frontiers in cell and developmental biology · 2021
    Article
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 2 institutions in 1 country.

Brett NixonPriority Research Centre in Reproductive Science; Priority Research Centre in Chemical Biology, School of Environmental and Life Sciences, Discipline of Biological Sciences, University of Newcastle, Callaghan, NSW 2308, Australia.
Elizabeth G Bromfield
Matthew D Dun
Kate A Redgrove
Eileen A McLaughlin
R John Aitken
University of Newcastle Australia · AUHunter Cancer Research Alliance · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection (ICSI), recent large-scale epidemiological studies have encouraged the cautious use of this technology and highlighted the need for further research into the mechanisms responsible for defective sperm-egg recognition. Previous work in this field has established that the sperm domains responsible for oocyte interaction are formed during spermatogenesis prior to being dynamically modified during epididymal maturation and capacitation in female reproductive tract. While the factors responsible for the regulation of these sequential maturational events are undoubtedly complex, emerging research has identified the molecular chaperone, heat shock protein A2 (HSPA2), as a key regulator of these events in human spermatozoa. HSPA2 is a testis-enriched member of the 70 kDa heat shock protein family that promotes the folding, transport, and assembly of protein complexes and has been positively correlated with in vitro fertilization (IVF) success. Furthermore, reduced expression of HSPA2 from the human sperm proteome leads to an impaired capacity for cumulus matrix dispersal, sperm-egg recognition and fertilization following both IVF and ICSI. In this review, we consider the evidence supporting the role of HSPA2 in sperm function and explore the potential mechanisms by which it is depleted in the spermatozoa of infertile patients. Such information offers novel insights into the molecular mechanisms governing sperm function.

Indexed as

AnimalsFemaleHSP70 Heat-Shock ProteinsHumansInfertility, MaleMaleMiceSperm-Ovum InteractionsHSP70 Heat-Shock ProteinsHSPA2 protein, humanHspa2 protein, mouse

Identifiers

PMID25865850
PMCPMC4492046
OpenAlexW2132965208

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.