The role of the cysteine-rich region of the β2 integrin subunit in the leukocyte function-associated antigen-1 (LFA-1, αLβ2, CD11a/CD18) heterodimer formation and ligand binding |
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| Authors: | Wendy A Douglass Robert H Hyland Christopher D Buckley Aymen Al-Shamkhani Jacqueline M Shaw Sarah L Scarth David L Simmons SKAlex Law |
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| Institution: | aMRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK;bCell Adhesion Laboratory, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK |
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| Abstract: | The cysteine-rich region (CRR) of the β2 integrin subunit was replaced by that of β1 to give the chimera β2NV1. β2NV1 can combine with αL to form a variant leukocyte-function-associated antigen (LFA)-1 on COS cell surface, suggesting that the specificity of the β2 interaction with αL does not lie in the CRR. Unlike those expressing wild-type LFA-1, COS cells expressing αLβ2NV1 are constitutively active in intercellular adhesion molecule (ICAM)-1 adhesion. These results suggest that activation of LFA-1 involves the release of an intramolecular constraint, which is maintained, in part, by the authentic β2 CRR. |
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| Keywords: | Integrin Leukocyte-function-associated antigen-1 Heterodimer formation Adhesion Activation |
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