ICAM‐2 peptides mediate lymphocyte adhesion by binding to CD11a/CD18 and CD49d/CD29 integrins

FEBS Letters

Seth, R.¹  Patarroyo, M.²  Makgoba, M.W.¹  Salcedo, R.² 

[1] Division of Molecular Endocrinology, Department of Chemical Pathology, Royal Postgraduate Medical School, Hammersmith Hospital, Ducane Road, London, W12 ONN, UK;Department of Immunology, Karolinska Institutet, Stockholm, Sweden

关键词: Cell adhesion: Integrin;    CD11a/CD18;    CD49d/CD29;    Phorbol ester;    Cell attachment assay;    Monoclonal antibody;    ICAM-2;   

DOI  :  10.1016/0014-5793(91)80475-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three fifteen-amino-acid polypeptides designated peptides 1, 2 and 3 were synthesised as likely candidates for mimicking the role of ICAM-2 as a ligand. The ability of each peptide to bind lymphoid cells was tested. Peptide 2 largely mediated cell attachment of unstimulated cells and this binding was only marginally increased by stimulating the cells with phorbol dibutyrate (P(Bu)₂), Peptide 3 mediated minimal spontaneous cell attachment, but this binding was significantly enhanced following P(Bu)₂ stimulation. Peptide I had no effect on cell attachment with or without stimulation. The cell attachment to peptide 2 was both temperature- and cation-dependent. Studies using specific monoclonal antibodies showed that with unstimulated cells, anti-VLA-4α(CD49d) or β chain (CD29) antibodies (KD4-13 and 4B4) and anti-CD18 (1B4) each partially inhibited the cell binding. Monoclonal antibodies against CD54 (ICAM-1; 84H10 or LB2). MHC class I (W6/32) and control mouse 1gG had no effect. When anti-CD29 and anti-CD18 monoclonal antibodies were used concurrently, there was almost complete inhibition of the cell attachment. These observations indicated that cell adhesion via ICAM-2 is mediated: (i) predominantly by peptide 2 in unstimulated and P(Bu)₂-stimulated cells, and also, to some extent, by peptide 3 in P(Bu)₂-stimulated cells and (ii) by binding to both CD11/CD18 and CD49d/CD29 integrins.

【 授权许可】

Unknown