Related Experiment Video
Updated: Jun 27, 2026
09:03
Modified In Vivo Matrix Gel Plug Assay for Angiogenesis Studies
Published on: June 30, 2023
Integrin and growth factor receptor alliance in angiogenesis
Payaningal R Somanath1, Alieta Ciocea, Tatiana V Byzova
1Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, NB50, Lerner Research Institute, The Cleveland Clinic, 9500 Euclid Ave, Cleveland, OH 44195, USA.
Cell Biochemistry and Biophysics
|December 3, 2008
Summary
Cellular communication involving integrins and growth factor receptors is crucial for regulating blood vessel formation (angiogenesis) and tissue repair. Understanding these interactions advances vascular biology research.
Area of Science:
- Vascular Biology
- Cell Signaling
- Extracellular Matrix Interactions
Background:
- Angiogenesis and tissue remodeling depend on coordinated cellular signaling pathways.
- Cellular responses to environmental cues involve integrin activation and communication with growth factor receptors.
- Specific interactions between growth factors, receptors, integrins, and extracellular matrix ligands are vital for vascular processes.
Purpose of the Study:
- To review recent advancements in understanding the cross-talk between integrins and growth factor receptors.
- To highlight the implications of these associations in regulating vascular processes.
- To update current knowledge on signaling events governing angiogenesis.
Main Methods:
- Review of in vitro and in vivo studies on cell signaling in vascular biology.
- Analysis of literature on integrin-growth factor receptor associations.
- Synthesis of recent findings on cross-talk mechanisms.
Main Results:
- Evidence supports the critical role of coordinated extracellular signals activating tyrosine kinase receptors and integrins in angiogenesis.
- Growth factors and cytokines directly interact with integrins, modulating integrin-related processes based on concentration.
- Novel signaling events reveal intricate cross-talk between growth factor receptors and integrins.
Conclusions:
- Integrin-growth factor receptor associations are central to regulating angiogenesis and vascular biology.
- Further research into these signaling pathways offers insights into physiological and pathological vascular conditions.
- Understanding these molecular interactions is key to advancing therapeutic strategies in vascular diseases.
Related Concept Videos
01:24Regulation of Angiogenesis and Blood Supply
Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits. Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
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...
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,...
01:10Mechanism of Angiogenesis
Blood vessel formation starts early during embryonic development, around day 7. In the extraembryonic yolk sac, mesodermal precursor cells called hemangioblast proliferate and differentiate into angioblast. Angioblasts express vascular endothelial growth factor receptor 2 or VEGFR2, which binds VEGF-A, a proangiogenic factor, guiding blood vessel formation. VEGF signaling promotes angioblasts to form a blood island in the developing embryo. Angioblasts further differentiate, giving rise to...
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.
02:38Mitogens 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...