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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 events provide an effective stimulus.
Regulation of Angiogenesis and Blood Supply01:24

Regulation 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...
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...
Mechanism of Angiogenesis01:10

Mechanism 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...
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,...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...

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Incorporating Pericytes into an Endothelial Cell Bead Sprouting Assay
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Angiogenesis: a balancing act between integrin activation and inhibition?

Federico Bussolino1, Francesca Caccavari, Donatella Valdembri

  • 1Department of Oncological Sciences and Division of Molecular Angiogenesis, IRCC, Institute for Cancer Research and Treatment, University of Torino School of Medicine, Candiolo, Italy. federico.bussolino@ircc.it

European Cytokine Network
|February 20, 2010
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New genes for extracellular matrix (ECM) proteins and integrins are vital for blood vessel development. Understanding how integrin activation is altered in tumor cells is key for cancer therapy.

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Incorporating Pericytes into an Endothelial Cell Bead Sprouting Assay
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Monitoring Functionality and Morphology of Vasculature Recruited by Factors Secreted by Fast-growing Tumor-generating Cells
09:03

Monitoring Functionality and Morphology of Vasculature Recruited by Factors Secreted by Fast-growing Tumor-generating Cells

Published on: November 23, 2014

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Cancer Biology

Background:

  • Vascular network development in embryos requires extracellular matrix (ECM) proteins, integrins, and angiogenic factors.
  • Pathological neovascularization is critical for tumor growth and impacts cancer therapy effectiveness.
  • Integrins, as major ECM receptors, exhibit varying affinities and require regulated activation for biological functions.

Purpose of the Study:

  • To investigate the molecular mechanisms regulating integrin function in normal endothelial cells (ECs).
  • To identify alterations in integrin function within tumor ECs compared to normal ECs.
  • To understand how disrupted integrin fine-tuning contributes to abnormal tumor vasculature.

Main Methods:

  • The abstract does not specify the methods used.
  • Further research is needed to elucidate the specific molecular mechanisms.

Main Results:

  • The abstract does not specify the results.
  • Integrin activation is finely modulated by guidance cues during embryonic vascular development.
  • Tumor vasculature is structurally and functionally abnormal, impairing drug and oxygen delivery.

Conclusions:

  • Fine-tuning of endothelial integrin function is essential for normal vascular development.
  • Disrupted integrin regulation in tumor ECs contributes to abnormal tumor vasculature.
  • Identifying these molecular alterations is crucial for improving cancer treatment efficacy.