On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.

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 ho...

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主要な著者: Johnston, S, Dustin, M, Hibbs, M, Springer, T
フォーマット: Journal article
言語:English
出版事項: 1990
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author Johnston, S
Dustin, M
Hibbs, M
Springer, T
author_facet Johnston, S
Dustin, M
Hibbs, M
Springer, T
author_sort Johnston, S
collection OXFORD
description 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.
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spelling oxford-uuid:4777e3a6-16fb-45c2-9844-e2c5065d8ad52022-03-26T15:20:20ZOn the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4777e3a6-16fb-45c2-9844-e2c5065d8ad5EnglishSymplectic Elements at Oxford1990Johnston, SDustin, MHibbs, MSpringer, TSpecies 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.
spellingShingle Johnston, S
Dustin, M
Hibbs, M
Springer, T
On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title_full On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title_fullStr On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title_full_unstemmed On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title_short On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules.
title_sort on the species specificity of the interaction of lfa 1 with intercellular adhesion molecules
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