Evidence map›Paper›PMID 10831617›Full record

ArticleThe Journal of cell biology2000

The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading.

K Iba, R Albrechtsen, B Gilpin, C Fröhlich, F Loechel, A Zolkiewska, K Ishiguro, T Kojima, W Liu, J K Langford and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
7.7field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 245 citations in OpenAlex.

  1. Article
  2. Review
  3. Coreceptor functions of cell surface heparan sulfate proteoglycans.American journal of physiology. Cell physiology · 2022
    Review
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  10. Article
  11. Proteoglycans as Mediators of Cancer Tissue Mechanics.Frontiers in cell and developmental biology · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 4 countries.

K IbaThe Institute of Molecular Pathology, University of Copenhagen, 2100 Copenhagen, Denmark.
R Albrechtsen
B Gilpin
C Fröhlich
F Loechel
A Zolkiewska
K Ishiguro
T Kojima
W Liu
J K Langford
R D Sanderson
C Brakebusch
R Fässler
U M Wewer
University of Copenhagen · DKUniversity of Arkansas for Medical Sciences · USLund University · SENagoya University · JPKansas State University · US

Funding

SYNDECAN FUNCTION ON MYELOMA CELLSR01CA068494 · NCI · UNIVERSITY OF ARKANSAS MED SCIS LTL ROCK · PI SANDERSON, RALPH D · 1996 to 2004
$1.5M
NCI NIH HHS CA68494NCI NIH HHS R01 CA068494
6 · The paper itself

Abstract

The ADAMs (a disintegrin and metalloprotease) family of proteins is involved in a variety of cellular interactions, including cell adhesion and ecto- domain shedding. Here we show that ADAM 12 binds to cell surface syndecans. Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP). Mesenchymal cells specifically and in a dose-dependent manner attach to ADAM 12 via members of the syndecan family. After binding to syndecans, mesenchymal cells spread and form focal adhesions and actin stress fibers. Integrin beta1 was responsible for cell spreading because function-blocking monoclonal antibodies completely inhibited cell spreading, and chondroblasts lacking beta1 integrin attached but did not spread. These data suggest that mesenchymal cells use syndecans as the initial receptor for the ADAM 12 cysteine-rich domain-mediated cell adhesion, and then the beta1 integrin to induce cell spreading. Interestingly, carcinoma cells attached but did not spread on ADAM 12. However, spreading could be efficiently induced by the addition of either 1 mM Mn(2+) or the beta1 integrin-activating monoclonal antibody 12G10, suggesting that in these carcinoma cells, the ADAM 12-syndecan complex fails to modulate the function of beta1 integrin.

Indexed as

ActinsADAM12 ProteinADAM ProteinsAnimalsAntibodies, MonoclonalBreast NeoplasmsCell AdhesionCell SizeChick EmbryoChondrocytesColonic NeoplasmsCysteineCytoskeletonHumansIntegrin beta1MagnesiumActinsADAM12 ProteinADAM12 protein, humanADAM ProteinsAntibodies, MonoclonalCysteineIntegrin beta1MagnesiumMembrane GlycoproteinsMembrane ProteinsMetalloendopeptidasesProteoglycansSyndecans

Identifiers

PMID10831617
PMCPMC2174829
OpenAlexW2111964851

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.