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Related Concept Videos

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,...
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...
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.
Drug-Receptor Interaction: Antagonist01:28

Drug-Receptor Interaction: Antagonist

An antagonist is a drug that binds strongly to a receptor without activating it. An antagonist prevents other molecules, such as neurotransmitters or hormones, from binding to the receptor and triggering a cellular response. Such interaction effectively hinders the normal physiological processes mediated by the receptor, resulting in various pharmacological effects depending on the specific receptor targeted.
Antagonists can be classified as competitive or noncompetitive based on their...
Drug-Receptor Interaction: Agonist01:25

Drug-Receptor Interaction: Agonist

Agonists are drugs that interact with specific receptors in the body to produce a biological response. When an agonist binds to a receptor, it activates or enhances the receptor's function, leading to physiological effects. The interaction between agonist drugs and receptors is crucial for their therapeutic action in various medical treatments.
Agonists can bind to receptors in different ways. Some agonists bind directly to the receptor's active site, mimicking the endogenous ligand's action.
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...

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Updated: Jun 23, 2026

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

Published on: February 2, 2024

Agonizing integrin antagonists?

Sara M Weis1, Dwayne G Stupack, David A Cheresh

  • 1Moores UCSD Cancer Center and Department of Pathology, University of California, San Diego, La Jolla, CA 92093, USA.

Cancer Cell
|May 5, 2009
PubMed
Summary
This summary is machine-generated.

Low-dose integrin inhibitors may unexpectedly boost tumor growth by enhancing angiogenesis. Future cancer treatments require redesigned drug delivery to avoid low concentrations and improve effectiveness.

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Area of Science:

  • Oncology
  • Molecular Biology
  • Pharmacology

Background:

  • Integrin inhibitors are investigated for cancer therapy.
  • RGD-mimetic compounds target integrin function.
  • Previous studies explored their anti-cancer potential.

Purpose of the Study:

  • To investigate the paradoxical effects of low-dose RGD-mimetic integrin inhibitors.
  • To determine the impact of these inhibitors on angiogenesis and tumor growth.
  • To inform the redesign of integrin inhibitor delivery for cancer treatment.

Main Methods:

  • Utilized RGD-mimetic integrin inhibitors in a low-dose treatment model.
  • Assessed the effects on angiogenesis (new blood vessel formation).
  • Monitored tumor growth in response to treatment.

Main Results:

  • Low-dose RGD-mimetic integrin inhibitors paradoxically enhanced angiogenesis.
  • Enhanced angiogenesis correlated with accelerated tumor growth.
  • Nanomolar plasma concentrations were identified as a critical factor.

Conclusions:

  • Current low-dose strategies with RGD-mimetic integrin inhibitors may be counterproductive.
  • Drug delivery systems must be redesigned to achieve higher, non-nanomolar concentrations.
  • Optimized delivery could improve the efficacy of integrin inhibitors in treating human cancers.