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Related Concept Videos

Cancer Cell Migration through Invadopodia01:35

Cancer Cell Migration through Invadopodia

Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...
Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Related Experiment Video

Updated: Jun 17, 2026

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
14:23

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts

Published on: August 27, 2012

Laminin-332-beta1 integrin interactions negatively regulate invadopodia.

Shanshan Liu1, Hironobu Yamashita, Brandy Weidow

  • 1Department of Cancer Biology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6840, USA.

Journal of Cellular Physiology
|December 30, 2009
PubMed
Summary

Laminin-332 (Ln-332) interactions, particularly with integrin alpha3beta1, limit invadopodia formation and extracellular matrix degradation by cancer cells. This suggests a mechanism where focal adhesions regulate Src kinase availability, controlling cell invasion.

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Related Experiment Videos

Last Updated: Jun 17, 2026

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
14:23

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts

Published on: August 27, 2012

2D and 3D Matrices to Study Linear Invadosome Formation and Activity
12:25

2D and 3D Matrices to Study Linear Invadosome Formation and Activity

Published on: June 2, 2017

Polyacrylamide Gels for Invadopodia and Traction Force Assays on Cancer Cells
08:48

Polyacrylamide Gels for Invadopodia and Traction Force Assays on Cancer Cells

Published on: January 4, 2015

Area of Science:

  • Cell Biology
  • Cancer Research
  • Biochemistry

Background:

  • Epithelial cell adhesion to basement membranes involves focal contacts and hemidesmosomes, both binding to laminin-332 (Ln-332).
  • Cancer cells utilize invadopodia for basement membrane degradation, potentially competing with adhesion structures for molecular components like Src kinase.

Purpose of the Study:

  • To investigate the role of Ln-332 in regulating invadopodia in 804G rat bladder carcinoma cells.
  • To determine how Ln-332 interactions influence focal contacts, hemidesmosomes, and invadopodia formation.

Main Methods:

  • Used shRNA to reduce Ln-332 gamma2 chain expression in 804G cells.
  • Assessed invadopodia numbers and extracellular matrix degradation.
  • Examined cell spreading and adhesion on different substrates (Ln-332, collagen-I).
  • Inhibited integrin subunits (alpha3, beta1, alpha6, beta4) and kinases (FAK, Src).

Main Results:

  • Knocking down the Ln-332 gamma2 chain increased invadopodia and extracellular matrix degradation.
  • Replating cells on Ln-332 or collagen-I restored normal cell spreading and inhibited invadopodia.
  • Inhibition of alpha3 or beta1 integrins mimicked the effects of gamma2 knockdown, implicating alpha3beta1 in invadopodia regulation.
  • gamma2 knockdown altered focal contact structures and FAK/Src kinase activation.
  • FAK inhibition increased invadopodia, which was reversed by Src inhibition.

Conclusions:

  • Actin-based adhesions, specifically alpha3beta1-mediated focal contacts, limit active Src kinase availability, thereby regulating invadopodia initiation.
  • Ln-332-beta1 interactions serve as a key upstream regulator that restricts cancer cell invasion by controlling invadopodia formation.