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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.
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,...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Selectins01:25

Selectins

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, which...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

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).
CAM Families
The Integrin family of proteins is primarily  involved in a...

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A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
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Regulation of integrin affinity on cell surfaces.

Thomas Schürpf1, Timothy A Springer

  • 1Department of Pathology, Harvard Medical School, Immune Disease Institute and Children's Hospital, Boston, MA, USA.

The EMBO Journal
|September 28, 2011
PubMed
Summary

Lymphocyte activation increases lymphocyte function-associated antigen-1 (LFA-1) adhesiveness. High affinity requires an open LFA-1 headpiece, with immobilized ICAM-1 triggering further affinity maturation.

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Area of Science:

  • Immunology
  • Cellular Biology
  • Biochemistry

Background:

  • Lymphocyte activation enhances lymphocyte function-associated antigen-1 (LFA-1) binding to intercellular adhesion molecules (ICAMs).
  • The mechanism by which activation signals alter LFA-1 affinity for ligands remains debated.
  • Understanding LFA-1 activation is crucial for immune response and autoimmune disease research.

Purpose of the Study:

  • To comprehensively measure LFA-1 affinities on T lymphocytes for ICAM-1 under various activation conditions.
  • To elucidate the structural requirements for LFA-1 adhesiveness and high affinity.
  • To investigate the role of immobilized versus soluble ICAM-1 in LFA-1 activation.

Main Methods:

  • Quantitative measurements of LFA-1 affinity on T lymphocytes using diverse activation stimuli.
  • Stabilization of specific LFA-1 conformations using Fab fragments.
  • Comparative analysis of LFA-1 interactions with soluble and immobilized ICAM-1.

Main Results:

  • Chemokine or T-cell receptor ligation induced modest LFA-1 affinity increases for soluble ICAM-1 but robust adhesion to ICAM-1 substrates.
  • An open LFA-1 headpiece conformation is essential for LFA-1 adhesiveness and high affinity.
  • Interaction with immobilized ICAM-1, but not soluble ICAM-1, triggers energy-dependent affinity maturation of LFA-1.

Conclusions:

  • LFA-1 activation involves more than just signal transmission to the ligand-binding domain.
  • Adhesiveness and high affinity are critically dependent on the LFA-1 headpiece conformation.
  • Integrin activation may be influenced by physical factors like traction or motion, particularly in interactions with immobilized ligands.