Evidence map›Paper›PMID 9230086›Full record

ArticleThe Journal of cell biology1997

Interactions between germ cells and extracellular matrix glycoproteins during migration and gonad assembly in the mouse embryo.

M I García-Castro, R Anderson, J Heasman, C Wylie

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Stay on the road: from germ cell specification to gonadal colonization in mammals.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  7. Germline stem cells in human.Signal transduction and targeted therapy · 2022
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Finding their way: themes in germ cell migration.Current opinion in cell biology · 2016
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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.

M I García-CastroWellcome/CRC Institute for Developmental Biology and Cancer, Cambridge CB2 1QR, England.
R Anderson
J Heasman
C Wylie
University of Minnesota · US

Funding

PRIMORDIAL GERM CELL MIGRATION IN THE EMBRYOR01HD033440 · NICHD · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WYLIE, CHRISTOPHER C · 1995 to 2003
$1.0M
NICHD NIH HHS HD33440-01NICHD NIH HHS R01 HD033440Wellcome Trust
6 · The paper itself

Abstract

Cells are known to bind to individual extracellular matrix glycoproteins in a complex and poorly understood way. Overall strength of adhesion is thought to be mediated by a combinatorial mechanism, involving adhesion of a cell to a variety of binding sites on the target glycoproteins. During migration in embryos, cells must alter their overall adhesiveness to the substrate to allow locomotion. The mechanism by which this is accomplished is not well understood. During early development, the cells destined to form the gametes, the primordial germ cells (PGCs), migrate from the developing hind gut to the site where the gonad will form. We have used whole-mount immunocytochemistry to study the changing distribution of three extracellular matrix glycoproteins, collagen IV, fibronectin, and laminin, during PGC migration and correlated this with quantitative assays of adhesiveness of PGCs to each of these. We show that PGCs change their strength of adhesion to each glycoprotein differentially during these stages. Furthermore, we show that PGCs interact with a discrete tract of laminin at the end of migration. Closer analysis of the adhesion of PGCs to laminin revealed that PGCs adhere particularly strongly to the E3 domain of laminin, and blocking experiments in vitro suggest that they adhere to this domain using a cell surface proteoglycan.

Indexed as

AnimalsCell AdhesionCell MovementChelating AgentsEdetic AcidExtracellular Matrix ProteinsGerm CellsGonadsHeparinLamininMiceOligopeptidesarginyl-glycyl-aspartic acidChelating AgentsEdetic AcidExtracellular Matrix ProteinsHeparinLamininOligopeptides

Identifiers

PMID9230086
PMCPMC2138185
OpenAlexW2111166148

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.