The effects of cysteine to alanine mutations of CD18 on the expression and adhesion of the CD11/CD18 integrins

FEBS Letters

Mathew, Elizabeth C.¹  Law, S.K.Alex¹  Scarth, Sarah L.¹  Al-Shamkhani, Aymen¹  Nolan, Sheila M.¹ 

[1] The MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

关键词: Cysteine to alanine mutation;    CD11/CD18 antigen;    Integrin;    Disulphide bond;    mAb;    monoclonal antibody;    ICAM;    intracellular adhesion molecule;    LFA;    leukocyte function-associated antigen;    HCR;    highly conserved region;    CRR;    cysteine-rich region;   

DOI  :  10.1016/S0014-5793(00)02247-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Of the 56 cysteines in the extracellular domain of the CD18 antigen (β2 integrin subunit), corresponding ones are not found in 12 positions in the β4, β7, or β8 integrin subunits. These 12 cysteines were mutated to alanines, either singly or in pairs, in CD18. All these mutants can support the expression of all three CD11/CD18 integrins. Transfectants expressing these variant integrins are generally more adhesive than the wild-type, suggesting that the cysteine residues, perhaps by engaging in disulphide bonds, may contribute to the maintenance of the CD11/CD18 integrins in a resting state.

【 授权许可】

Unknown