Related Experiment Video
Updated: Jun 9, 2026
09:33
Preparation Of Neovascular Tissues from Human Glioma Tissues for Quantitative Proteomics Analysis of Tumor Angiogenesis
Published on: March 20, 2026
Targeting integrins in malignant glioma
Ghazaleh Tabatabai1, Michael Weller, Burt Nabors
1Department of Neurology, University Hospital Zurich, Frauenklinikstrasse 26, 8091 Zurich, Switzerland. ghazaleh.tabatabai@usz.ch
Targeted Oncology
|September 8, 2010
Summary
Integrin inhibitors like cilengitide show promise for treating glioma. Clinical trials indicate durable remissions in glioblastoma (GBM) and potential synergy with standard therapies.
Area of Science:
- Oncology
- Molecular Biology
- Cell Adhesion Research
Background:
- Integrins are cell adhesion receptors implicated in cancer.
- AlphaVbeta3 and alphaVbeta5 integrins are overexpressed in glioma and tumor vasculature.
- Cilengitide is a leading integrin inhibitor in oncology.
Purpose of the Study:
- To review the role of integrins in gliomagenesis.
- To summarize the therapeutic potential of integrin inhibition for glioma.
- To outline ongoing clinical trials for integrin inhibitors in GBM.
Main Methods:
- Review of preclinical data on integrin function in glioma.
- Analysis of clinical trial results for cilengitide in recurrent and newly diagnosed GBM.
- Summary of ongoing phase III studies (e.g., CENTRIC).
Main Results:
- Cilengitide demonstrates antitumor activity in glioma.
- Durable remissions observed in Phase I/II trials for recurrent glioblastoma.
- Encouraging results from pilot trials in newly diagnosed GBM with standard therapy.
Conclusions:
- Integrin inhibition is a promising anticancer strategy for glioma.
- Cilengitide shows potential for treating glioblastoma, particularly in combination therapy.
- Ongoing trials will further define the efficacy of integrin inhibitors in GBM.
Related Concept Videos
01:15Activation 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.
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.
01:10Integrins
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,...
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,...
01:17Intracellular 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...
Some...