Evidence map›Paper›PMID 19357365›Full record

ArticleBiology of reproduction2009

Clusterin facilitates exchange of glycosyl phosphatidylinositol-linked SPAM1 between reproductive luminal fluids and mouse and human sperm membranes.

Genevieve S Griffiths, Deni S Galileo, Rolands G Aravindan, Patricia A Martin-DeLeon

Open access · bronzeAbstract read
In one paragraph

Article in Biology of reproduction, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

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  13. Presence, localization, and origin of clusterin in normal human spermatozoa.Journal of assisted reproduction and genetics · 2012
    Article
  14. Article
  15. Recent advances in physiological priming of spermatozoa.Journal of human reproductive sciences · 2010
    Article
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  18. Review
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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

4 authors at 1 institution in 1 country.

Genevieve S GriffithsDepartment of Biological Sciences, University of Delaware, Newark, Delaware 19716, USA.
Deni S Galileo
Rolands G Aravindan
Patricia A Martin-DeLeon
University of Delaware · US

Funding

TOWARDS SOLID-STATE NMR STRUCTURES OF GPCRSP20RR015588 · NCRR · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2000 to 2009
$18.2M
SPAM 1 ALLELES, SPERM PHENOTYPE AND FUNCTIONR01HD038273 · NICHD · UNIVERSITY OF DELAWARE · PI DELEON, PATRICIA ANASTASIA · 2001 to 2004
$1.1M
NCRR NIH HHS 5P20RR015588NCRR NIH HHS P20 RR015588NICHD NIH HHS R01 HD038273NICHD NIH HHS R01 HD38273
6 · The paper itself

Abstract

Glycosyl phosphatidylinositol (GPI)-linked proteins, which are involved in post-testicular maturation of sperm and have a role in fertilization, are acquired on the sperm surface from both vesicular and membrane-free soluble fractions of epididymal luminal fluid (LF) and uterine LF. Herein, we investigate the mechanism of uptake of these proteins from the soluble fraction of LFs using sperm adhesion molecule 1 (SPAM1) as a model. Ultracentrifugation and native Western blot analysis of the soluble fraction revealed that SPAM1 is present in low-molecular-weight (monomeric) and high-molecular-weight (oligomeric) complexes. The latter are incapable of transferring SPAM1 and may serve to produce monomers. Monomers are stabilized by hydrophobic interactions with clusterin (CLU), a lipid carrier that is abundantly expressed in LFs. We show that CLU is involved in the transfer of SPAM1 monomers, whose delivery was decreased by anti-CLU antibody under normal and apolipoprotein-enhanced conditions. Coimmunoprecipitation revealed an intimate association of CLU with SPAM1. Both plasma and recombinant CLU had a dose-related effect on transfer efficiency: high concentrations reduced and low concentrations enhanced delivery of SPAM1 to human and mouse sperm membranes, reflecting physiological states in the epididymal tract. We propose a lipid exchange model (akin to the lipid-poor model for cholesterol efflux) for the delivery of GPI-linked proteins to sperm membranes via CLU. Our investigation defines specific conditions for membrane-free GPI-linked protein transfer in vitro and could lead to technology for improving fertility or treating sperm pathology by the addition of relevant GPI-linked proteins critical for successful fertilization in humans and domestic animals.

Indexed as

AdultAnimalsAntibodiesCell Adhesion MoleculesCell MembraneClusterinExtracellular FluidFemaleGlycosylphosphatidylinositolsHumansHyaluronoglucosaminidaseMaleMiceModels, BiologicalProtein TransportReproductionAntibodiesCell Adhesion MoleculesClusterinGlycosylphosphatidylinositolshyaluronidase PH-20Hyaluronoglucosaminidase

Identifiers

PMID19357365
PMCPMC2731979
OpenAlexW2152046517

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.