Evidence map›Paper›PMID 8636223›Full record

ArticleThe Journal of cell biology1996

Human neural cell adhesion molecule L1 and rat homologue NILE are ligands for integrin alpha v beta 3.

A M Montgomery, J C Becker, C H Siu, V P Lemmon, D A Cheresh, J D Pancook, X Zhao, R A Reisfeld

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
6.2field-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

67 citing papers in PubMed, 227 citations in OpenAlex.

  1. Article
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  7. αGlia · 2021
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

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

8 authors at 1 institution in 1 country.

A M MontgomeryDepartment of Immunology, Scripps Research Institute, La Jolla, California 92037, USA.
J C Becker
C H Siu
V P Lemmon
D A Cheresh
J D Pancook
X Zhao
R A Reisfeld
Scripps Research Institute · US

Funding

THE GROWTH OF RETINAL GANGLION CELL AXONSR01EY005285 · NEI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI LEMMON, VANCE P · 1985 to 2004
$1.4M
MOLECULAR PROFILE OF MELANOMA AND NEUROBLASTOMA ANTIGENSR35CA042508 · NCI · SCRIPPS RESEARCH INSTITUTE · PI LODE, HOLGER N · 1986 to 2000
$70k
NCI NIH HHS CA42508NEI NIH HHS R01 EY005285
6 · The paper itself

Abstract

Integrin alpha v beta 3 is distinct in its capacity to recognize the sequence Arg-Gly-Asp (RGD) in many extra-cellular matrix (ECM) components. Here, we demonstrate that in addition to the recognition of ECM components, alpha v beta 3 can interact with the neural cell adhesion molecule L1-CAM; a member of the immunoglobulin superfamily (IgSF). M21 melanoma cells displayed significant Ca(++)-dependent adhesion and spreading on immunopurified rat L1 (NILE). This adhesion was found to be dependent on the expression of the alpha v-integrin subunit and could be significantly inhibited by an antibody to the alpha v beta 3 heterodimer. M21 cells also displayed some alpha v beta 3-dependent adhesion and spreading on immunopurified human L1. Ligation between this ligand and alpha v beta 3 was also observed to promote significant haptotactic cell migration. To map the site of alpha v beta 3 ligation we used recombinant L1 fragments comprising the entire extracellular domain of human L1. Significant alpha v beta 3-dependent adhesion and spreading was evident on a L1 fragment containing Ig-like domains 4, 5, and 6. Importantly, mutation of an RGD sequence present in the sixth Ig-like domain of L1 abrogated M21 cell adhesion. We conclude that alpha v beta 3-dependent recognition of human L1 is dependent on ligation of this RGD site. Despite high levels of L1 expression the M21 melanoma cells did not display significant adhesion via a homophilic L1-L1 interaction. These data suggest that M21 melanoma cells recognize and adhere to L1 through a mechanism that is primarily heterophilic and integrin dependent. Finally, we present evidence that melanoma cells can shed and deposit L1 in occluding ECM. In this regard, alpha v beta 3 may recognize L1 in a cell-cell or cell-substrate interaction.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntigens, SurfaceBase SequenceBinding SitesCell AdhesionCell LineCell MovementDNA PrimersHumansKineticsLeukocyte L1 Antigen ComplexLigandsMelanomaMolecular Sequence DataAntibodiesAntigens, Surfacearginyl-glycyl-aspartic acidDNA PrimersLeukocyte L1 Antigen ComplexLigandsNeural Cell Adhesion MoleculesOligopeptidesReceptors, VitronectinRecombinant Fusion Proteins

Identifiers

PMID8636223
PMCPMC2120722
OpenAlexW2047762713

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.