Evidence map›Paper›PMID 10473629›Full record

ArticleMolecular biology of the cell1999

Division of labor among the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells.

J Muschler, A Lochter, C D Roskelley, P Yurchenco, M J Bissell

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

56 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
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  11. Three-dimensional cultures of mouse mammary epithelial cells.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  12. Article
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  19. Cell-matrix interactions in mammary gland development and breast cancer.Cold Spring Harbor perspectives in biology · 2010
    Review
  20. The contribution of adhesion signaling to lactogenesis.Journal of cell communication and signaling · 2010
    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

5 authors at 4 institutions in 3 countries.

J MuschlerLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. jlmuschler@lbl.gov
A Lochter
C D Roskelley
P Yurchenco
M J Bissell
Lawrence Berkeley National Laboratory · USCenter for Clinical & Basic Research · DKJohnson University · USUniversity of British Columbia · CA

Funding

Role of Metalloproteinases in Mammary Gland RemodelingR01CA057621 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WERB, ZENA · 1993 to 2017
$9.0M
NCI NIH HHS CA57621NCI NIH HHS R01 CA057621
6 · The paper itself

Abstract

Contact of cultured mammary epithelial cells with the basement membrane protein laminin induces multiple responses, including cell shape changes, growth arrest, and, in the presence of prolactin, transcription of the milk protein beta-casein. We sought to identify the specific laminin receptor(s) mediating the multiple cell responses to laminin. Using assays with clonal mammary epithelial cells, we reveal distinct functions for the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor. Signals from laminin for beta-casein expression were inhibited in the presence of function-blocking antibodies against both the alpha6 and beta1 integrin subunits and by the laminin E3 fragment. The alpha6-blocking antibody perturbed signals mediated by the alpha6beta4 integrin, and the beta1-blocking antibody perturbed signals mediated by another integrin, the alpha subunit(s) of which remains to be determined. Neither alpha6- nor beta1-blocking antibodies perturbed the cell shape changes resulting from cell exposure to laminin. However, the E3 laminin fragment and heparin both inhibited cell shape changes induced by laminin, thereby implicating an E3 laminin receptor in this function. These results elucidate the multiplicity of cell-extracellular matrix interactions required to integrate cell structure and signaling and ultimately permit normal cell function.

Indexed as

AnimalsAntigens, SurfaceBasement MembraneBlotting, WesternCaseinsCell DifferentiationCells, CulturedCell SizeEpithelial CellsGene ExpressionHeparinIntegrin alpha6beta4Integrin beta1IntegrinsLamininMammary Glands, AnimalAntigens, SurfaceCaseinsHeparinIntegrin alpha6beta4Integrin beta1IntegrinsLamininPeptide FragmentsReceptors, Laminin

Identifiers

PMID10473629
PMCPMC25520
OpenAlexW1913063313

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.