Evidence map›Paper›PMID 8794871›Full record

ArticleThe Journal of cell biology1996

Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation.

J M Lewis, D A Cheresh, M A Schwartz

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 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.0field-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

51 citing papers in PubMed, 190 citations in OpenAlex.

  1. Article
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  8. Use of protein-engineered fabrics to identify design rules for integrin ligand clustering in biomaterials.Integrative biology : quantitative biosciences from nano to macro · 2016
    Article
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  15. Therapeutic potential for protein kinase C inhibitor in vascular restenosis.Journal of cardiovascular pharmacology and therapeutics · 2011
    Review
  16. Article
  17. Article
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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

3 authors at 1 institution in 1 country.

J M LewisDepartment of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
D A Cheresh
M A Schwartz
Scripps Research Institute · US

Funding

REGULATION OF TUMOR CELL ATTACHMENT BY SURFACE ANTIGENSR01CA045726 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1988 to 2017
$7.4M
REGULATION OF SECOND MESSENGERS BY BETA3 INTEGRINS IN THE VASCULAR SYSTEMP01HL048728 · NHLBI · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1992 to 2003
$7.4M
NCI NIH HHS CA45726NHLBI NIH HHS HL48728NIGMS NIH HHS GM16000
6 · The paper itself

Abstract

Integrins alpha v beta 3 and alpha v beta 5 both mediate cell adhesion to vitronectin yet trigger different postligand binding events. Integrin alpha v beta 3 is able to induce cell spreading, migration, angiogenesis, and tumor metastasis without additional stimulators, whereas alpha v beta 5 requires exogenous activation of protein kinase C (PKC) to mediate these processes. To investigate this difference, the ability of beta 3 or beta 5 to induce colocalization of intracellular proteins was assessed by immunofluorescence in hamster CS-1 melanoma cells. We found that alpha v beta 5 induced colocalization of talin, alpha-actinin, tensin, and actin very weakly relative to alpha v beta 3. alpha v beta 5 was able to efficiently induce colocalization of focal adhesion kinase (FAK); however, it was unable to increase phosphorylation of FAK on tyrosine. Activation of PKC by adding phorbol ester to alpha v beta 5-expressing cells induced spreading, increased colocalization of alpha-actinin, tensin, vinculin, p130cas and actin, and triggered tyrosine phosphorylation of FAK. Unexpectedly, talin colocalization remained low even after activation of PKC. Treatment of cells with the PKC inhibitor calphostin C inhibited spreading and the colocalization of talin, alpha-actinin, tensin, and actin for both alpha v beta 3 and alpha v beta 5. We conclude that PKC regulates localization of cytoskeletal proteins and phosphorylation of FAK induced by alpha v beta 5. Our results also show that FAK can be localized independent of its phosphorylation and that cells can spread and induce localization of other focal adhesion proteins in the absence of detectable talin.

Indexed as

AnimalsCell AdhesionCell Adhesion MoleculesCricetinaeCytoskeletal ProteinsCytoskeletonEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrinsMicroscopy, ConfocalPhosphorylationProtein Kinase CProtein-Tyrosine KinasesReceptors, VitronectinCell Adhesion MoleculesCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine Kinasesintegrin alphaVbeta5IntegrinsProtein Kinase CProtein-Tyrosine KinasesPTK2 protein, humanReceptors, VitronectinVitronectin

Identifiers

PMID8794871
PMCPMC2120976
OpenAlexW2135112491

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.