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ICAM‐2 peptides mediate lymphocyte adhesion by binding to CD11a/CD18 and CD49d/CD29 integrins
Author(s) -
Seth R.,
Salcedo R.,
Patarroyo M.,
Makgoba M.W.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80475-i
Subject(s) - cd11a , cd18 , integrin , adhesion , icam 1 , cell adhesion molecule , cell adhesion , chemistry , microbiology and biotechnology , immunology , biology , biochemistry , cell , organic chemistry
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.