Evidence map›Paper›PMID 20378539›Full record

ArticleThe Journal of biological chemistry2010

The integrin co-activator Kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell.

Katarzyna Bialkowska, Yan-Qing Ma, Kamila Bledzka, Khalid Sossey-Alaoui, Lahoucine Izem, Xiaoxia Zhang, Nikolay Malinin, Jun Qin, Tatiana Byzova, Edward F Plow

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
–field-weighted citation impact
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

70 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021
    Review
  15. Article
  16. Kindlins as modulators of breast cancer progression.Journal of breast cancer research · 2021
    Article
  17. Article
  18. Article
  19. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  20. Adhesive dynamics simulations quantitatively predict effects of kindlin-3 deficiency on T-cell homing.Integrative biology : quantitative biosciences from nano to macro · 2019
    Article

10 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

10 authors.

Katarzyna BialkowskaDepartment of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.
Yan-Qing Ma
Kamila Bledzka
Khalid Sossey-Alaoui
Lahoucine Izem
Xiaoxia Zhang
Nikolay Malinin
Jun Qin
Tatiana Byzova
Edward F Plow

Funding

Structure Basis for Talin-mediated Integrin ActivationP01HL073311 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI BYZOVA, TATIANA V · 2004 to 2019
$27.4M
Activation of the beta-3 integrins: Role of the KindlinsR01HL096062 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2009 to 2022
$5.6M
NHLBI NIH HHS P01 HL073311NHLBI NIH HHS P01HL073311NHLBI NIH HHS R01 HL096062NHLBI NIH HHS R01 HL096062-01
6 · The paper itself

Abstract

Integrin activation is crucial for numerous cellular responses, including cell adhesion, migration, and survival. Recent studies in mice have specifically emphasized the vital role of kindlin-3 in integrin activation. Kindlin-3 deficiency in humans also has now been documented and includes symptoms of bleeding, frequent infections, and osteopetrosis, which are consequences of an inability to activate beta1, beta2, and beta3 integrins. To date, kindlin-3 was thought to be restricted to hematopoietic cells. In this article, we demonstrate that kindlin-3 is present in human endothelial cells derived from various anatomical origins. The mRNA and protein for KINDLIN-3 was detected in endothelial cells by reverse transcription-PCR and Western blots. When subjected to sequencing by mass spectrometry, the protein was identified as authentic kindlin-3 and unequivocally distinguished from KINDLIN-1 and KINDLIN-2 or any other known protein. By quantitative real time PCR, the level of kindlin-3 in endothelial cells was 20-50% of that of kindlin-2. Using knockdown approaches, we show that kindlin-3 plays a role in integrin-mediated adhesion of endothelial cells. This function depends upon the integrin and substrate and is distinct from that of kindlin-2. Formation of tube-like structures in Matrigel also was impaired by kindlin-3 knockdown. Mechanistically, the distinct functions of the kindlins can be traced to differences in their subcellular localization in integrin-containing adhesion structures. Thus, the prevailing view that individual kindlins exert their functions in a cell type-specific manner must now be modified to consider distinct functions of the different family members within the same cell type.

Indexed as

Gene Expression RegulationBlood PlateletsBlotting, WesternCell AdhesionCell SurvivalDNA, ComplementaryEndothelial CellsHematopoietic Stem CellsHumansMass SpectrometryMembrane ProteinsNeoplasm ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerDNA, ComplementaryFERMT3 protein, humanMembrane ProteinsNeoplasm ProteinsRNA, Messenger

Identifiers

PMID20378539
PMCPMC2881789

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.