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...
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.
Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
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...
Formation of the Platelet Plug01:22

Formation of the Platelet Plug

The platelet phase, the second stage of hemostasis, commences around 15-20 seconds after an injury. It follows and overlaps with the vascular phase, during which blood vessels constrict to minimize blood loss.
As the injured blood vessel contracts, endothelial cells undergo contraction, revealing collagen fibers in the basement membrane and underlying connective tissue. Furthermore, the plasma membrane of endothelial cells becomes adhesive, preparing the site for platelet adhesion. Platelets...

You might also read

Related Articles

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

Sort by
Same author

The role of activated platelets in cerebral malaria pathogenesis.

Blood·2026
Same author

Fully Synthetic Non-Carbohydrate Heparin Mimetics-Perspectives for Therapeutic Anticoagulation and Beyond?

Archiv der Pharmazie·2026
Same author

Comparing Heparin and Heparin Mimetics in Targeting Immunomodulatory Proteins from Platelets to Activate T Cell-Dependent Immune Response in Oncology.

ACS pharmacology & translational science·2026
Same author

Layilin: a novel regulator of platelet reactivity in IBD.

Blood·2025
Same author

Increased efficacy of PARP inhibitors against cisplatin-sensitive and -resistant ovarian cancer cells mediated via ATR and ATM inhibition.

Cell death discovery·2025
Same author

Target Engagement Studies and Kinetic Live-Cell Degradation Assays Enable the Systematic Characterization of Histone Deacetylase 6 Degraders.

ACS pharmacology & translational science·2025

Related Experiment Video

Updated: Jun 19, 2026

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity
10:41

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Published on: February 17, 2017

Binding between heparin and the integrin VLA-4.

Martin Schlesinger1, Dirk Simonis, Patrick Schmitz

  • 1Department of Pharmacy, Rheinische Friedrich Wilhelms University Bonn, An der Immenburg 4, 53121 Bonn, Germany.

Thrombosis and Haemostasis
|November 6, 2009
PubMed
Summary
This summary is machine-generated.

Heparin and low-molecular-weight heparin (LMWH) inhibit melanoma cell adhesion by binding to integrin VLA-4. This specific molecular recognition explains heparin's antimetastatic effects beyond anticoagulation.

More Related Videos

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
04:15

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs

Published on: February 2, 2024

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
05:43

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers

Published on: November 8, 2024

Related Experiment Videos

Last Updated: Jun 19, 2026

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity
10:41

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Published on: February 17, 2017

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
04:15

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs

Published on: February 2, 2024

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
05:43

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers

Published on: November 8, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Heparin exhibits antimetastatic properties through mechanisms beyond anticoagulation.
  • Heparin's interference with adhesion receptors, particularly selectins and integrins, is a key therapeutic avenue.
  • Previous research indicated heparin's interaction with integrin VLA-4 and VCAM-1 in melanoma metastasis.

Purpose of the Study:

  • To confirm heparin's inhibitory activity on VLA-4 mediated cell adhesion.
  • To investigate the molecular recognition of heparin by integrin VLA-4.
  • To elucidate the role of heparin size in its antimetastatic effects.

Main Methods:

  • Inhibition assays using human melanoma MV3 cells and immobilized VCAM-1.
  • Differential fractionation of heparin to assess the impact of size.
  • Surface acoustic wave-biosensor to analyze kinetic binding constants of tinzaparin to VLA-4.

Main Results:

  • Unfractionated heparin (UFH) and tinzaparin (LMWH) significantly inhibited VLA-4/VCAM-1 binding.
  • Inhibitory activity decreased with smaller heparin fractions, with fondaparinux showing no effect.
  • Tinzaparin demonstrated specific binding to VLA-4 with low micromolar affinity and similar dissociation rates to VCAM-1.

Conclusions:

  • Heparin directly binds to integrin VLA-4, confirming specific molecular recognition.
  • Heparin's size is crucial for its inhibitory activity on VLA-4 mediated cell adhesion.
  • These findings provide a molecular basis for heparin's antimetastatic effects in melanoma.