TY - JOUR
T1 - The leukocyte integrin Mac-1 (CD11b/CD18) contributes to binding of human granulocytes to collagen
AU - Walzog, Barbara
AU - Schuppan, Detlef
AU - Heimpel, Caroline
AU - Hafezi-Moghadam, Ali
AU - Gaehtgens, Peter
AU - Ley, Klaus
PY - 1995/5
Y1 - 1995/5
N2 - Adhesion of polymorphonuclear granulocytes (PMN) to extracellular matrix proteins has been shown to be important for their migration in vitro and is thought to participate in PMN recruitment to sites of inflammation. Isolated human PMN stimulated with PMA were found to adhere best to microtiter wells coated with the novel ECM glycoprotein indulin (27 ± 3% of PMNs added), followed by fibrinogen (25 ± 2%), collagen type VI (18 ± 2%), fibronectin (16 ± 2%), and laminin (15 ± 3%). PMN adhesion to other collagens ranged between 3 and 11%. Monoclonal antibodies recognizing CD18 and CD11b subunits of Mac-1 inhibited adhesion of PMN to collagens by an order of magnitude more effectively than to all noncollagenous substrates. F(ab')2 fragments of the anti-CD18 antibody were also able to block adhesion to collagens. Anti-LFA-1 (CD11a) and anti-CD44 antibodies did not significantly reduce adhesion. PMN adhesion was also inhibited by soluble collagens type II and VI (ID50 approximately 75 μg/ml). Binding of soluble radiolabeled collagens type II and VI to PMNs was specific and saturable with apparent dissociation constants of 2.2 and 1.9 nM, respectively, and specific binding of collagens type II and VI was almost completely inhibited by anti-CD18, but not by control antibodies. These data indicate that Mac-1 function is required for binding of human PMN to collagens.
AB - Adhesion of polymorphonuclear granulocytes (PMN) to extracellular matrix proteins has been shown to be important for their migration in vitro and is thought to participate in PMN recruitment to sites of inflammation. Isolated human PMN stimulated with PMA were found to adhere best to microtiter wells coated with the novel ECM glycoprotein indulin (27 ± 3% of PMNs added), followed by fibrinogen (25 ± 2%), collagen type VI (18 ± 2%), fibronectin (16 ± 2%), and laminin (15 ± 3%). PMN adhesion to other collagens ranged between 3 and 11%. Monoclonal antibodies recognizing CD18 and CD11b subunits of Mac-1 inhibited adhesion of PMN to collagens by an order of magnitude more effectively than to all noncollagenous substrates. F(ab')2 fragments of the anti-CD18 antibody were also able to block adhesion to collagens. Anti-LFA-1 (CD11a) and anti-CD44 antibodies did not significantly reduce adhesion. PMN adhesion was also inhibited by soluble collagens type II and VI (ID50 approximately 75 μg/ml). Binding of soluble radiolabeled collagens type II and VI to PMNs was specific and saturable with apparent dissociation constants of 2.2 and 1.9 nM, respectively, and specific binding of collagens type II and VI was almost completely inhibited by anti-CD18, but not by control antibodies. These data indicate that Mac-1 function is required for binding of human PMN to collagens.
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U2 - 10.1006/excr.1995.1127
DO - 10.1006/excr.1995.1127
M3 - Article
AN - SCOPUS:0029034439
SN - 0014-4827
VL - 218
SP - 28
EP - 38
JO - Experimental Cell Research
JF - Experimental Cell Research
IS - 1
ER -