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Related Concept Videos

Integrins01:10

Integrins

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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,...
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Intracellular Signaling Affects Focal Adhesions01:17

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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...
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Activation of Integrins01:15

Activation of Integrins

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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...
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Selectins01:25

Selectins

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

Overview of Cell-Matrix Interactions

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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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Cancer Cell Migration through Invadopodia01:35

Cancer Cell Migration through Invadopodia

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Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However,...
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Related Experiment Video

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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Nanoscale integrin ligand patterns determine melanoma cell behavior.

Katharina Amschler1, Luise Erpenbeck, Sebastian Kruss

  • 1Department of Dermatology, Venereology and Allergology, Georg August University , Göttingen, Germany.

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|August 30, 2014
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Summary

Cancer cells

Keywords:
RGDcell spreadingintegrinligand presentationmelanomananostructures

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Area of Science:

  • Cell biology
  • Biomaterials science
  • Nanotechnology

Background:

  • Cell adhesion relies on integrin receptors binding to ligands like the arginine-glycine-aspartic acid (RGD) motif.
  • Integrin-directed drugs are developed for cancer, but their effects on tumor progression can be paradoxical.
  • Understanding nanoscale integrin regulation in tumor cells is crucial.

Purpose of the Study:

  • To investigate how nanoscale RGD ligand presentation influences melanoma cell adhesion and integrin function.
  • To explore the mechanisms behind paradoxical effects of integrin-targeting drugs in cancer.

Main Methods:

  • Utilized RGD-functionalized gold nanoparticles patterned by block copolymer nanolithography to create tunable ligand densities (10^3 to 1145 sites/μm²).
  • Examined human melanoma cell spreading, focal contact formation, and cytoskeletal reorganization on surfaces with varying RGD densities.
  • Assessed the impact of low-dose solute RGD on cell behavior and integrin clustering.

Main Results:

  • Melanoma cells exhibited integrin-dependent spreading and cytoskeletal changes at a physiologically relevant RGD density (349 sites/μm²).
  • Low concentrations of soluble RGD altered optimal surface ligand densities, inducing changes in integrin clusters and cytoskeleton.
  • Melanoma cells adapted to suboptimal nanostructured surfaces, entering a 'permissive' state.

Conclusions:

  • Nanoscale RGD ligand presentation significantly modulates melanoma cell integrin function and behavior.
  • Soluble RGD can influence cell responses to surface-bound ligands, potentially explaining paradoxical drug effects.
  • Findings offer insights into individualized therapies by controlling cell-surface interactions.