Functional analysis of intercellular adhesion molecule-1-expressing human thyroid cells

A P Weetman1, M Freeman, L K Borysiewicz

  • 1Department of Medicine, University of Cambridge Clinical School, Addenbrooke's Hospital, Cambridge, GB.

Insights

Thyroid cells express intercellular adhesion molecule-1 (ICAM-1), enhancing immune cell recognition and cytotoxicity. This ICAM-1 role may contribute to the development and progression of autoimmune thyroiditis.

Area of Science:

  • Immunology
  • Endocrinology
  • Cell Biology

Background:

  • Intercellular adhesion molecule-1 (ICAM-1) is implicated in immune cell interactions.
  • The specific role of ICAM-1 in thyroid cells during autoimmune processes requires further elucidation.

Purpose of the Study:

  • To investigate the expression and function of ICAM-1 in thyroid cells.
  • To determine the impact of ICAM-1 on immune cell clustering and cytotoxicity against thyroid cells.

Main Methods:

  • In vitro assays including cell clustering and cytotoxicity measurements.
  • Stimulation of thyroid cells with cytokines (e.g., interferon-gamma) and lymphocytes.
  • Flow cytometry to assess lymphocyte-thyroid cell cluster formation.
  • Use of monoclonal antibodies against ICAM-1 to block its function.

Main Results:

  • Thyroid cell ICAM-1 expression increased upon cytokine stimulation within 24 hours, unaffected by methimazole.
  • Anti-ICAM-1 antibody reduced lymphocyte-thyroid cell cluster formation by approximately one-third.
  • Phytohemagglutinin-stimulated lymphocyte cytotoxicity against thyroid cells decreased by 23%-28% in the presence of anti-ICAM-1 antibody.
  • Thyroid cells demonstrated rhinovirus infection, confirming functional ICAM-1 ligand presence.

Conclusions:

  • Thyroid cell ICAM-1 expression can enhance immune cell recognition and contribute to cytotoxicity.
  • These ICAM-1 functions may play a significant role in the initiation or perpetuation of autoimmune thyroiditis.

Related Concept Videos

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...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

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.
Cell Sorting During Development
Cell sorting plays an...
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...
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...