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Adhesiveness for Extracellular Matrices and Lysosomal Enzyme Release from Normal and β 2 Integrin‐Deficient Bovine Neutrophils
Author(s) -
Nagahata Hajime,
Higuchi Hidetoshi,
Noda Hiroshi,
Tamoto Koichi,
Kuwabara Mikinori
Publication year - 1996
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1996.tb01142.x
Subject(s) - cd18 , fibronectin , biology , integrin , opsonin , receptor , extracellular , zymosan , laminin , microbiology and biotechnology , immunology , biochemistry , antibody , extracellular matrix , in vitro
The adhesiveness of control and CD18‐deficient bovine neutrophils on culture plates precoated with collagen I, collagen IV, fibronectin and laminin was measured to evaluate the possible factors for adherence to extracellular matrices. The release of N ‐acetyl‐β‐ D ‐glucosaminidase (NAG ase ) from control and CD18‐deficient neutrophils stimulated with complement receptor type 3 (CR3) or Fc receptor dependent stimuli was also evaluated. The adhesive activities of CD18‐deficient neutrophils to collagen I, collagen IV and fibronectin were significantly diminished ( P < 0.05); however, similar adhesion to laminin was observed in CD18‐deficient neutrophils and control neutrophils. The adhesive activity of control neutrophils on uncoated plates increased 2.5 times ( P < 0.05) with the presence of PMA. The mean activities for NAG ase release from CD18‐deficient neutrophils stimulated with opsonized zymosan and aggregated bovine immunoglobulin G (Agg‐IgG) were 46.7 and 82.7% that of the control neutrophils, respectively. The Agg‐IgG‐induced NAG ase release from control and CD18‐deficient neutrophils was eliminated by H7, a protein kinase C inhibitor. These results support that an association between CR3 and Fc receptors on neutrophils appears to play an essential role in neutrophil functions.