Evidence map›Paper›PMID 19450503›Full record

ArticleBiophysical journal2009

Filamin A is essential for active cell stiffening but not passive stiffening under external force.

K E Kasza, F Nakamura, S Hu, P Kollmannsberger, N Bonakdar, B Fabry, T P Stossel, N Wang, D A Weitz

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Nuclear lamin isoforms differentially contribute to LINC complex-dependent nucleocytoskeletal coupling and whole-cell mechanics.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. The mechanobiome: a goldmine for cancer therapeutics.American journal of physiology. Cell physiology · 2021
    Review
  15. Review
  16. Article
  17. Review
  18. Stiffness Sensing by Cells.Physiological reviews · 2020
    Review
  19. Article
  20. Article

5 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

9 authors at 4 institutions in 2 countries.

K E KaszaSchool of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts, USA.
F Nakamura
S Hu
P Kollmannsberger
N Bonakdar
B Fabry
T P Stossel
N Wang
D A Weitz
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEBrigham and Women's Hospital · USHarvard University · USUniversity of Illinois Urbana-Champaign · US

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
PHAGOCYTOSIS: PULMONARY ALVEOLAR MACROPHAGESR37HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1989 to 1998
–
NHLBI NIH HHS HL-19429NHLBI NIH HHS R01 HL019429NIGMS NIH HHS GM07274
6 · The paper itself

Abstract

The material properties of a cell determine how mechanical forces are transmitted through and sensed by that cell. Some types of cells stiffen passively under large external forces, but they can also alter their own stiffness in response to the local mechanical environment or biochemical cues. Here we show that the actin-binding protein filamin A is essential for the active stiffening of cells plated on collagen-coated substrates. This appears to be due to a diminished capability to build up large internal contractile stresses in the absence of filamin A. To show this, we compare the material properties and contractility of two human melanoma cell lines that differ in filamin A expression. The filamin A-deficient M2 cells are softer than the filamin A-replete A7 cells, and exert much smaller contractile stresses on the substratum, even though the M2 cells have similar levels of phosphorylated myosin II light chain and only somewhat diminished adhesion strength. In contrast to A7 cells, the stiffness and contractility of M2 cells are insensitive to either myosin-inhibiting drugs or the stiffness of the substratum. Surprisingly, however, filamin A is not required for passive stiffening under large external forces.

Indexed as

ElasticityActinsCell AdhesionCell Line, TumorContractile ProteinsCytoskeletonFilaminsHeterocyclic Compounds, 4 or More RingsHumansMicrofilament ProteinsMyosin Light ChainsMyosin Type IIPhosphorylationStress, MechanicalActinsblebbistatinContractile ProteinsFilaminsHeterocyclic Compounds, 4 or More RingsMicrofilament ProteinsMyosin Light ChainsMyosin Type II

Identifiers

PMID19450503
PMCPMC2712146
OpenAlexW2113778176

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.