Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
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...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
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."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multi-omic analysis reveals nitric oxide dependent remodeling in classically activated macrophages and identifies negative regulation mediated by AKR1A1.

Redox biology·2026
Same author

Novel Allocation Strategies Can Boost Kidney Exchange Programs: A Monte Carlo Simulation.

Transplant international : official journal of the European Society for Organ Transplantation·2026
Same author

Evidence that xylazine disrupts skin homeostasis by acting on epithelial cells through the kappa opioid receptor.

Disease models & mechanisms·2026
Same author

The paracrine factor myeloid derived growth factor regulates the inflammatory fate and motility of human induced pluripotent stem cell-derived neutrophils.

Journal of immunology (Baltimore, Md. : 1950)·2026
Same author

Leukocyte-epithelial physical contacts mediate interstitial migration in vivo.

Research square·2026
Same author

Multi-omic analysis reveals nitric oxide dependent remodeling in classically activated macrophages and identifies negative regulation mediated by AKR1A1.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: May 12, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Gelsolin expression increases β1 -integrin affinity and L1210 cell adhesion.

Jeroen D Langereis1, Leo Koenderman, Anna Huttenlocher

  • 1Department of Respiratory Medicine, University Medical Center Utrecht, Utrecht, the Netherlands.

Cytoskeleton (Hoboken, N.J.)
|April 19, 2013
PubMed
Summary
This summary is machine-generated.

Gelsolin regulates beta-1 integrin affinity and cell adhesion in leukemia cells. Increased actin polymerization via gelsolin enhances integrin function and cell binding to collagen.

Keywords:
attachmentcell membranecytoskeletongelsolinmigration

More Related Videos

Preparation of Tunable Extracellular Matrix Microenvironments to Evaluate Schwann Cell Phenotype Specification
07:50

Preparation of Tunable Extracellular Matrix Microenvironments to Evaluate Schwann Cell Phenotype Specification

Published on: June 2, 2020

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

Published on: March 8, 2017

Related Experiment Videos

Last Updated: May 12, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Preparation of Tunable Extracellular Matrix Microenvironments to Evaluate Schwann Cell Phenotype Specification
07:50

Preparation of Tunable Extracellular Matrix Microenvironments to Evaluate Schwann Cell Phenotype Specification

Published on: June 2, 2020

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

Published on: March 8, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Integrins are crucial cell surface receptors involved in cell adhesion and migration.
  • Inside-out signaling regulates integrin function by altering their conformation (affinity) and clustering (avidity).
  • The precise mechanisms governing inside-out signaling remain incompletely understood.

Purpose of the Study:

  • To investigate the role of gelsolin in regulating beta-1 integrin affinity in the L1210 leukemia cell line.
  • To elucidate the mechanisms by which gelsolin influences integrin-mediated cell adhesion.

Main Methods:

  • Proteomics screening to identify proteins involved in integrin inside-out signaling.
  • Cell culture of L1210 and U937 leukemia cell lines.
  • Analysis of gelsolin expression and localization near beta-1 integrins.
  • Manipulation of actin polymerization using jasplakinolide.
  • Gelsolin knockdown experiments.
  • Assessment of beta-1 integrin affinity and cell adhesion to collagen.

Main Results:

  • Gelsolin is primarily localized at the cell membrane, in proximity to beta-1 integrins.
  • Inhibition of actin polymerization with jasplakinolide reduced beta-1 integrin affinity.
  • Gelsolin knockdown in L1210 cells decreased beta-1 integrin affinity and cell adhesion to collagen.
  • These findings indicate a positive correlation between actin polymerization and beta-1 integrin affinity.

Conclusions:

  • Gelsolin plays a significant role in the inside-out regulation of beta-1 integrin affinity.
  • Actin polymerization, modulated by gelsolin, is essential for maintaining beta-1 integrin affinity and cell adhesion.
  • Gelsolin-actin interactions are critical for integrin-mediated cell adhesion in leukemia cells.