Related Experiment Video

Updated: Dec 2, 2025

Preparing a 68Ga-labeled Arginine Glycine Aspartate RGD-peptide for Angiogenesis
07:48

Preparing a 68Ga-labeled Arginine Glycine Aspartate RGD-peptide for Angiogenesis

Published on: January 7, 2019

7.2K

Biological Relevance of RGD-Integrin Subtype-Specific Ligands in Cancer

Saidu Sani1,2, Mélissa Messe1,3, Quentin Fuchs1

  • 1Laboratoire de Bioimagerie et Pathologies (LBP), UMR CNRS 7021, Institut Thématique Interdisciplinaire InnoVec, Université de Strasbourg, Faculté de Pharmacie, 74 route du, Rhin, CS 60024, 67401, Illkirch Cedex, France.

Chembiochem : a European Journal of Chemical Biology
|November 3, 2020
PubMed

Insights

Targeting cancer involves understanding integrins, which are cell receptors. Developing selective Arg-Gly-Asp (RGD) ligands is crucial for precisely targeting RGD-integrins like αvβ3 and α5β1 in tumors for better therapies.

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • Integrins are transmembrane receptors mediating cell-extracellular matrix interactions.
  • These receptors are implicated in numerous cancer hallmarks.
  • Integrins recognizing the Arg-Gly-Asp (RGD) motif are key therapeutic targets.

Purpose of the Study:

  • To review the biological rationale for developing selective RGD-integrin ligands.
  • To discuss the complex roles of RGD-integrins in tumors.
  • To evaluate the current utility of selective ligands in cancer research.

Main Methods:

  • Literature review focusing on the biological aspects of RGD-integrins in cancer.
  • Analysis of the development of selective RGD-like ligands.
  • Discussion of the roles of αvβ3 and α5β1 integrins in tumor progression.

Main Results:

  • Selective targeting of RGD-integrin subtypes is necessary due to their diverse roles in cancer.
  • Significant efforts have been made in designing specific RGD-mimetic ligands.
  • The biological characteristics of each integrin subtype in specific tumors remain incompletely understood.

Conclusions:

  • Selective ligands are essential tools for dissecting the functions of individual RGD-integrins in cancer.
  • Further research into integrin subtype-specific roles could refine their use as therapeutic targets.
  • Targeting specific integrins offers potential for novel cancer therapies.
Keywords:
CancerRGD-integrinsinhibitorsligand designpeptides

More Related Videos

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors09:45

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

11.0K
Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion09:56

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Published on: February 11, 2022

2.9K

Related Concept Videos

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...
4.6K
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,...
4.9K
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,...
3.8K
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...
3.3K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
4.9K
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
7.5K