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Updated: Aug 8, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Vascular cell adhesion molecule-1 mediates lymphocyte adherence to cytokine-activated cultured human endothelial
T M Carlos1, B R Schwartz, N L Kovach
1Department of Medicine, University of Washington, Seattle.
Insights
Vascular cell adhesion molecule-1 (VCAM-1) is a novel protein induced by cytokines on endothelial cells. It mediates lymphocyte adhesion to inflamed endothelium via a pathway independent of CD18.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Cytokine-induced cell adhesion molecules play critical roles in immune responses.
- Understanding these interactions is key to modulating inflammatory processes.
Purpose of the Study:
- To characterize the expression and function of vascular cell adhesion molecule-1 (VCAM-1).
- To investigate the role of VCAM-1 in lymphocyte adherence to cytokine-stimulated endothelium.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) and radioimmunoprecipitation were used to assess VCAM-1 expression.
- Monoclonal antibody (MoAb) 4B9 was employed to block VCAM-1 function.
- Lymphocyte adherence assays were performed on cytokine-activated human umbilical vein endothelium (HUVE).
Main Results:
- VCAM-1 expression was minimal on unstimulated HUVE but rapidly induced by tumor necrosis factor-alpha (TNF-alpha), interleukin-1, and lipopolysaccharide.
- MoAb 4B9 significantly inhibited peripheral blood lymphocyte (PBL) adherence to activated HUVE.
- VCAM-1 mediated a CD18-independent pathway for PBL adherence.
Conclusions:
- VCAM-1 is a cytokine-inducible adhesion molecule on endothelium.
- VCAM-1 facilitates lymphocyte binding to inflamed endothelium through a CD18-independent mechanism.
- This interaction may be crucial for lymphocyte emigration during inflammation.
Abstract:
The expression and function of a new cytokine-induced endothelial cell adhesion protein, vascular cell adhesion molecule-1 (VCAM-1), was characterized in vitro by using a monoclonal antibody, MoAb 4B9, which recognizes a functional epitope on this protein. As determined by enzyme-linked immunosorbent assay and radioimmunoprecipitation of metabolically labeled cells, VCAM-1 was minimally expressed on unstimulated human umbilical vein endothelium (HUVE), but was rapidly induced by recombinant human tumor necrosis factor-alpha (rhTNF-alpha), rh interleukin-1, and lipopolysaccharide. In contrast to intercellular adhesion molecule-1, VCAM-1 was not induced on dermal fibroblasts or arterial smooth muscle cells after stimulation with rhTNF, or on keratinocytes after stimulation with rh interferon-gamma. MoAb 4B9 significantly inhibited the adherence of peripheral blood lymphocytes (PBL) and lymphocytic cell lines, but not neutrophils, to rhTNF-activated HUVE. The inhibitory effect of MoAb 4B9 on PBL adherence to HUVE was additive to that produced by the CD18 MoAb 60.3. These results show that VCAM-1 mediates a CD18-independent pathway of peripheral blood lymphocyte adherence to cytokine-stimulated HUVE. We propose that lymphocyte binding to VCAM-1, induced on endothelium by cytokines, may be an important component of lymphocyte emigration at sites of inflammation or immune reaction.
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