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Adhesion-mediating molecules of human monocytes
M Patarroyo1, J Prieto, P G Beatty
1Department of Immunology, Karolinska Institute, Stockholm, Sweden.
Cellular Immunology
|May 1, 1988
Summary
Monoclonal antibody 60.3 targeting GP90 (CD18) significantly inhibits monocyte aggregation and adhesion to T cells. This highlights GP90
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Phorbol esters enhance monocyte adhesion to T cells and substrates.
- Monocyte aggregation and adhesion are critical processes in immune responses.
Purpose of the Study:
- To investigate the role of specific leukocyte surface glycoproteins in monocyte adhesion and aggregation.
- To identify the molecular targets mediating monocyte interactions.
Main Methods:
- Utilized monoclonal antibodies to inhibit monocyte aggregation and adhesion.
- Tested antibodies targeting GP90 (CD18), LFA-1 (CD11a), CD11b, CD11c, and other cell surface antigens.
- Employed phorbol esters to stimulate monocyte adhesion.
Main Results:
- Monoclonal antibody 60.3, recognizing GP90 (CD18), inhibited monocyte aggregation by over 90%.
- Antibody 60.3 also inhibited monocyte adhesion to T cells and plastic surfaces.
- Antibodies against CD11a, CD11b, and CD11c showed limited or no inhibition.
- LB-2 antibody demonstrated partial inhibition of monocyte adhesion.
Conclusions:
- GP90 (CD18), alone or complexed with other glycoproteins, is a key mediator of monocyte adhesion.
- The LB-2 antigen also plays a role in monocyte adhesion.
- Monoclonal antibody 60.3 is a potent inhibitor of monocyte adhesion processes.