Evidence map›Paper›PMID 20815087›Full record

ArticleProteomics2010

Characterization of the proteomes associating with three distinct membrane raft sub-types in murine sperm.

Atsushi Asano, Jacquelyn L Nelson, Sheng Zhang, Alexander J Travis

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.8field-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

25 citing papers in PubMed, 72 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. Testis-Specific Isoform of NaInternational journal of molecular sciences · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Organization of Membrane Rafts in Chicken Sperm.The journal of poultry science · 2016
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Atsushi AsanoThe Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Jacquelyn L Nelson
Sheng Zhang
Alexander J Travis
Cornell University · US

Funding

Nanoscale energy production for implantable medical devicesDP1OD006431 · OD · CORNELL UNIVERSITY · PI TRAVIS, ALEXANDER J · 2009 to 2011
$2.3M
ORGANIZATION AND FUNCTIONS OF LIPID RAFTS IN SPERMATOZOAR01HD045664 · NICHD · CORNELL UNIVERSITY ITHACA · PI TRAVIS, ALEXANDER J · 2004 to 2008
$1.3M
NICHD NIH HHS R01 HD045664NICHD NIH HHS R01-HD-045664NIH HHS 5DP1-OD-006431NIH HHS DP1 OD006431
6 · The paper itself

Abstract

Mammalian sperm are transcriptionally and translationally inactive. To meet changing needs in the epididymis and female tract, they rely heavily on post-translational modifications and protein acquisition/degradation. Membrane rafts are sterol and sphingolipid-enriched micro-domains that organize and regulate various pathways. Rafts have significance in sperm by transducing the stimulus of sterol efflux into changes in intracellular signaling that confer fertilization competence. We recently characterized three biochemically distinct sub-types of sperm rafts, and now present profiles for proteins targeting to and associating with these sub-types, along with a fraction largely comprised of "non-raft" domains. Proteomics analysis using a gel-based LC-MS/MS approach identified 190 strictly validated proteins in the raft sub-types. Interestingly, many of these are known to be expressed in the epididymis, where sperm membrane composition matures. To investigate potential roles for rafts in epididymal protein acquisition, we compared the expression and localization of two different sterol-interacting proteins, apolipoprotein-A1 (apoA1) and prominin-1 (prom1) in sperm from different zones. We found that apoA1 was gradually added to the plasma membrane overlying the acrosome, whereas prom1 was not, suggesting different mechanisms for raft protein acquisition. Our results define raft-associating proteins, demonstrate functional similarities and differences among raft sub-types, and provide insights into raft-mediated epididymal protein acquisition.

Indexed as

AnimalsEpididymisMaleMass SpectrometryMembrane MicrodomainsMiceProteomeSpermatozoaProteome

Identifiers

PMID20815087
PMCPMC2950924
OpenAlexW2077356953

What OpenQuestion holds

Textmetadata
LicenceTDM
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.