Evidence map›Paper›PMID 2513332›Full record

ArticleThe Journal of cell biology1989

Dynamic cytoskeleton-integrin associations induced by cell binding to immobilized fibronectin.

S C Mueller, T Kelly, M Z Dai, H N Dai, W T Chen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. 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
2.6field-weighted citation impact, top 10% 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, 97 citations in OpenAlex.

  1. Review
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  4. Integrins can directly mediate metastatic tumor cell adhesion within the liver sinusoids.Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary Tract · 2004
    Article
  5. Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
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  14. Review
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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 1 institution in 1 country.

S C MuellerDepartment of Anatomy and Cell Biology, Georgetown University School of Medicine, Washington, DC 20007.
T Kelly
M Z Dai
H N Dai
W T Chen
Georgetown University · US

Funding

MOLECULAR ULTRASTRUCTURE UNDERLYING CELL ADHESIONR01CA039077 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI CHEN, WEN-TIEN · 1985 to 2007
$1.6M
REGULATION OF TISSUE REPAIRR01HL033711 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI CHEN, WEN-TIEN · 1985 to 2002
$1.0M
NCI NIH HHS R01 CA-39077NHLBI NIH HHS R01 HL-33711
6 · The paper itself

Abstract

We have examined the early events of cellular attachment and spreading (10-30 min) by allowing chick embryonic fibroblasts transformed by Rous sarcoma virus to interact with fibronectin immobilized on matrix beads. The binding activity of cells to fibronectin beads was sensitive to both the mAb JG22E and the GRGDS peptide, which inhibit the interaction between integrin and fibronectin. The precise distribution of cytoskeleton components and integrin was determined by immunocytochemistry of frozen thin sections. In suspended cells, the distribution of talin was diffuse in the cytoplasm and integrin was localized at the cell surface. Within 10 min after binding of cells and fibronectin beads at 22 degrees C or 37 degrees C, integrin and talin aggregated at the membrane adjacent to the site of bead attachment. In addition, an internal pool of integrin-positive vesicles accumulated. The mAb ES238 directed against the extracellular domain of the avian beta 1 integrin subunit, when coupled to beads, also induced the aggregation of talin at the membrane, whereas ES186 directed against the intracellular domain of the beta 1 integrin subunit did not. Cells attached and spread on Con A beads, but neither integrin nor talin aggregated at the membrane. After 30 min, when many of the cells were at a more advanced stage of spreading around beads or phagocytosing beads, alpha-actinin and actin, but not vinculin, form distinctive aggregates at sites along membranes associated with either fibronectin or Con A beads. Normal cells also rapidly formed aggregates of integrin and talin after binding to immobilized fibronectin in a manner that was similar to the transformed cells, suggesting that the aggregation process is not dependent upon activity of the pp60v-src tyrosine kinase. Thus, the binding of cells to immobilized fibronectin caused integrin-talin coaggregation at the sites of membrane-ECM contact, which can initiate the cytoskeletal events necessary for cell adhesion and spreading.

Indexed as

AnimalsAntibodies, MonoclonalCell AdhesionCell Line, TransformedCell MovementChick EmbryoConcanavalin ACytoskeletal ProteinsCytoskeletonFibronectinsIntegrinsMicrospheresProtein BindingSignal TransductionTalinAntibodies, MonoclonalConcanavalin ACytoskeletal ProteinsFibronectinsIntegrinsTalin

Identifiers

PMID2513332
PMCPMC2115959
OpenAlexW1978977830

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.