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Related Concept Videos

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.
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Immunoglobulin-like Cell Adhesion Molecules01:31

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
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Anchoring Junctions01:03

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Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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Cadherins in Tissue Organization01:19

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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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Desmosomes01:05

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The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are  essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein...
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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Dimerization of Cell-Adhesion Molecules Can Increase Their Binding Strength.

Wenmao Huang1, Meng Qin1, Ying Li2

  • 1Collaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University , Nanjing 210093, China.

Langmuir : the ACS Journal of Surfaces and Colloids
|January 24, 2017
PubMed
Summary

Cell-adhesion molecules (CAMs) binding strength increases through dimerization via ligand rebinding and exchange. This molecular mechanism enhances cell-adhesion bonds, with applications in drug delivery and biomaterials.

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Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
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Area of Science:

  • Biophysics
  • Molecular Biology
  • Materials Science

Background:

  • Cell-adhesion molecules (CAMs) typically form homodimers.
  • Steric hindrance limits simultaneous ligand binding to homodimers.
  • The molecular mechanism for CAM dimerization benefits remains unclear.

Purpose of the Study:

  • To develop a theoretical model for understanding cell-adhesion bond rupture with multiple ligands.
  • To investigate the role of dimerization in enhancing binding strength at the single-molecule level.

Main Methods:

  • Theoretical modeling of cell-adhesion bond rupture dynamics.
  • Atomic force microscopy-based single-molecule force spectroscopy.
  • Measurement of dimeric cyclic Arg-Gly-Asp (cRGD) unbinding from integrin (αvβ3).

Main Results:

  • A ligand rebinding and exchange mechanism significantly enhances dissociation forces compared to monomeric interactions.
  • Experimental validation confirmed the theoretical prediction of increased binding strength.
  • Dimeric cRGD showed enhanced unbinding resistance from integrin αvβ3.

Conclusions:

  • Dimerization of CAMs increases cell-adhesion bond strength through a ligand rebinding and exchange mechanism at the single-molecule level.
  • This finding provides insight into the design principles of natural cell-adhesion systems.
  • Results offer opportunities for engineering stronger bioconjunctions for biomedical applications.