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Species restrictions in immune cell interactions have been demonstrated both in Ag-specific responses of T lymphocytes and the phenomenon of natural attachment. To determine the possible contribution of adhesion receptors to these restrictions, we have studied binding between the murine and human homologues of LFA-1 (CD11a/CD18) and ICAM employing purified human LFA-1 and ICAM-1 (CD54) bound to solid substrates. Murine cell lines bind to purified human LFA-1 through ICAM-1 and at least one other counter-receptor. This provides evidence for multiple counter-receptors for LFA-1 in the mouse as well as in the human. In contrast to binding of murine ICAM-1 to human LFA-1, murine LFA-1 does not bind to human ICAM-1. The species specificity maps to the LFA-1 alpha subunit, because mouse x human hybrid cells expressing the human alpha subunit associated with a mouse beta subunit bind to human ICAM-1, whereas those with a human beta subunit associated with a murine alpha subunit do not. Increased adhesiveness for ICAM-1 stimulated by phorbol esters could be demonstrated for hybrid LFA-1 molecules with human alpha and murine beta subunits.

Type

Journal article

Journal

Journal of immunology (Baltimore, Md. : 1950)

Publication Date

08/1990

Volume

145

Pages

1181 - 1187

Addresses

Center for Blood Research, Boston, MA 02115.

Keywords

Hybrid Cells, Animals, Humans, Mice, Tetradecanoylphorbol Acetate, Cell Adhesion Molecules, Lymphocyte Function-Associated Antigen-1, Receptors, Leukocyte-Adhesion, Antigens, Differentiation, Antibodies, Monoclonal, Species Specificity, Binding Sites