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Related Concept Videos

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.
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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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Nanoscale increases in CD2-CD48-mediated intermembrane spacing decrease adhesion and reorganize the immunological

Oren Milstein1, Su-Yi Tseng, Toby Starr

  • 1Programs in Molecular Pathogenesis and Structural Biology, Helen and Martin Kimmel Center for Biology and Medicine of the Skirball Institute and New York University School of Medicine, New York, New York 10016, USA.

The Journal of Biological Chemistry
|October 2, 2008
PubMed
Summary
This summary is machine-generated.

The study reveals how different forms of CD48 impact cell adhesion and T cell sensitivity. Wild-type CD48 (CD48-WT) is more efficient than CD48-CD2 or CD48-CD22, affecting T cell receptor clustering.

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Area of Science:

  • Immunology
  • Biophysics
  • Cell Biology

Background:

  • The interplay between intermembrane spacing, adhesion receptor organization, and adhesion efficiency remains unclear.
  • Understanding these factors is crucial for deciphering cell-cell interactions in biological systems.

Purpose of the Study:

  • To investigate the relationship between CD48 ligand variants, intermembrane spacing, adhesion efficiency, and lateral organization.
  • To determine how different CD48 forms influence the structure of the immunological synapse and T cell sensitivity.

Main Methods:

  • Utilized wild-type CD48 (CD48-WT) and chimeric CD48 variants (CD48-CD2, CD48-CD22) with varying Ig-like domains.
  • Employed electron tomography to measure intermembrane spacing in contact areas.
  • Used confocal imaging to analyze the formation of immunological synapses in T lymphocytes.

Main Results:

  • CD48-WT mediated adhesion 10-fold more efficiently than CD48-CD2 or CD48-CD22.
  • Intermembrane spacing increased with more Ig-like domains (CD48-WT: 12.8 nm, CD48-CD2: 14.7 nm, CD48-CD22: 15.6 nm).
  • CD48-CD2 and CD48-CD22 induced eccentric clustering of the CD2/T cell antigen receptor (TCR) in immunological synapses, reducing T cell sensitivity.

Conclusions:

  • The number of Ig-like domains in CD48 significantly affects adhesion efficiency and intermembrane spacing.
  • CD48 variants can reorganize the immunological synapse, sequestering the TCR and modulating T cell activation.
  • This provides insights into the molecular mechanisms governing immune cell interactions and sensitivity.