Regulatory properties of LFA-1 α and β chains in human T-lymphocyte activation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-06

AUTHORS

Carel van Noesel, Frank Miedema, Miranda Brouwer, Menno A. de Rie, Lucien A. Aarden, René A. W. van Lier

ABSTRACT

Lymphocyte function-associated antigen-1 (LFA-1) is a heterodimer composed of an α and β chain that is expressed on the surface of most leukocytes and is an essential molecule for adhesion reactions between cells participating in the immune response1,2. A putative ligand for LFA-1 is the intercellular adhesion molecule ICAM-1 (refs 3-5). Leukocyte adhesion abnormality is found in patients with LFA-1 deficiency6–7. It is not clear whether binding of ligand to the LFA-1 molecule merely spatially orientates cells towards each other or can also induce signals that regulate cell activation and differentiation. We have recently developed a T-cell proliferation assay which uses immobilized anti-CD3 monoclonal antibodies as stimulant and is independent of LFA-1-mediated cellular adhesion. As there is no interference by anti-LFA-1 monoclonal antibodies with the adhesion-dependent activation steps, this T-cell activation system allows us to investigate whether transmembrane signals are induced by binding of ligand to LFA-1 on T cells. Our data indicate that binding of ligand to LFA-1 results in the transduction of regulatory signals across the plasma membrane, rather like other molecules (CD2, CD4, CDS) (refs 8–11) with signal-modifying properties involved in the adhesion of T cells to target/stimulator cells. Indeed, adhesion molecules might generally be important in signal transduction, even in cells not belonging to the immune system. More... »

PAGES

850-852

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/333850a0

DOI

http://dx.doi.org/10.1038/333850a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1043669604

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2968520


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