Evidence map›Paper›PMID 25117412›Full record

ArticleAmerican journal of physiology. Endocrinology and metabolism2014

Differential effects of c-Src and c-Yes on the endocytic vesicle-mediated trafficking events at the Sertoli cell blood-testis barrier: an in vitro study.

Xiang Xiao, Dolores D Mruk, Elissa W P Wong, Will M Lee, Daishu Han, Chris K C Wong, C Yan Cheng

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Endocrinology and metabolism, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.6field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Src family kinases (SFKs) and cell polarity in the testis.Seminars in cell & developmental biology · 2018
    Review
  12. Review
  13. Review
  14. Regulation of spermatogenesis by a local functional axis in the testis: role of the basement membrane-derived noncollagenous 1 domain peptide.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  15. Regulation of the blood-testis barrier by a local axis in the testis: role of laminin α2 in the basement membrane.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  16. Review
  17. Review
  18. Review
  19. Actin binding proteins in blood-testis barrier function.Current opinion in endocrinology, diabetes, and obesity · 2015
    Review
  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

7 authors at 4 institutions in 3 countries.

Xiang XiaoMary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, New York, New York;
Dolores D MrukMary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, New York, New York;
Elissa W P WongMary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, New York, New York;
Will M LeeSchool of Biological Sciences, University of Hong Kong, Hong Kong, China;
Daishu HanDepartment of Cell Biology, School of Basic Medicine, Institute of Basic Medical Sciences, Peking Union Medical College, Beijing, China; and.
Chris K C WongDepartment of Biology, Hong Kong Baptist University, Hong Kong, China.
C Yan ChengMary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, New York, New York; y-cheng@popcbr.rockefeller.edu.
Population Council · USChinese Academy of Medical Sciences & Peking Union Medical College · CNHong Kong Baptist University · HKUniversity of Hong Kong · HK

Funding

SPECIALIZED CONTRACEPTIVE DEVELOPMENT RESEARCH CENTERU54HD029990 · NICHD · POPULATION COUNCIL · PI WARE, REGINE SITRUK · 1992 to 2016
$27.7M
The biology of blood-testis barrier dynamicsR01HD056034 · NICHD · POPULATION COUNCIL · PI CHENG, C. YAN · 2009 to 2018
$3.4M
NICHD NIH HHS R01 HD056034NICHD NIH HHS R01-HD-056034NICHD NIH HHS U54 HD029990NICHD NIH HHS U54-HD-029990
6 · The paper itself

Abstract

The blood-testis barrier (BTB) is one of the tightest blood-tissue barriers in the mammalian body. However, it undergoes cyclic restructuring during the epithelial cycle of spermatogenesis in which the "old" BTB located above the preleptotene spermatocytes being transported across the immunological barrier is "disassembled," whereas the "new" BTB found behind these germ cells is rapidly "reassembled," i.e., mediated by endocytic vesicle-mediated protein trafficking events. Thus, the immunological barrier is maintained when preleptotene spermatocytes connected in clones via intercellular bridges are transported across the BTB. Yet the underlying mechanism(s) in particular the involving regulatory molecules that coordinate these events remains unknown. We hypothesized that c-Src and c-Yes might work in contrasting roles in endocytic vesicle-mediated trafficking, serving as molecular switches, to effectively disassemble and reassemble the old and the new BTB, respectively, to facilitate preleptotene spermatocyte transport across the BTB. Following siRNA-mediated specific knockdown of c-Src or c-Yes in Sertoli cells, we utilized biochemical assays to assess the changes in protein endocytosis, recycling, degradation and phagocytosis. c-Yes was found to promote endocytosed integral membrane BTB proteins to the pathway of transcytosis and recycling so that internalized proteins could be effectively used to assemble new BTB from the disassembling old BTB, whereas c-Src promotes endocytosed Sertoli cell BTB proteins to endosome-mediated protein degradation for the degeneration of the old BTB. By using fluorescence beads mimicking apoptotic germ cells, Sertoli cells were found to engulf beads via c-Src-mediated phagocytosis. A hypothetical model that serves as the framework for future investigation is thus proposed.

Indexed as

AnimalsBlood-Testis BarrierCell Culture TechniquesCells, CulturedEndocytosisGene Knockdown TechniquesGenes, srcMaleMembrane ProteinsPhagocytosisProto-Oncogene Proteins c-yesProto-Oncogene Proteins pp60(c-src)RatsRats, Sprague-DawleyRNA, Small InterferingSertoli CellsMembrane ProteinsProto-Oncogene Proteins c-yesProto-Oncogene Proteins pp60(c-src)RNA, Small Interferingblood-testis barrierc-Srcc-Yesectoplasmic specializationendosomerecyclingseminiferous epithelial cyclespermatogenesistestistight junctiontranscytosis

Identifiers

PMID25117412
PMCPMC4187029
OpenAlexW2113685427

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.