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

FEBS Letters

Hyland, Robert H.¹  Shaw, Jacqueline M.¹  Law, S.K.Alex¹  Scarth, Sarah L.¹  Al-Shamkhani, Aymen¹  Douglass, Wendy A.¹  Simmons, David L.²  Buckley, Christopher D.² 

[1] MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK;Cell Adhesion Laboratory, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK

关键词: Integrin;    Leukocyte-function-associated antigen-1;    Heterodimer formation;    Adhesion;    Activation;    mAb;    monoclonal antibodies;    ICAM;    intercellular adhesion molecule;    LFA;    leukocyte-function-associated antigen;    HCR;    highly conserved region;    CRR;    cysteine-rich region;    Mg/EGTA;    5 mM MgCl2 and 1 mM EGTA;   

DOI  :  10.1016/S0014-5793(98)01498-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown