FEBS Letters | |
Dual pertussis toxin‐sensitive pathway of zymosan‐induced activation in guinea pig macrophages | |
Tamoto, Koichi2  Hazeki, Kaoru2  Ui, Michio1  Mori, Yoki2  | |
[1] Ui Laboratory, the Institute of Physical and Chemical Research, Wako-shi 351-01, Japan;Department of Microbiology, Faculty of Pharmaceutical Sciences, Higashi-Nippon-Gakuen University, Ishikari-Tobetsu 061-02, Japan | |
关键词: GTP-binding protein; CR3; Zymosan; Superoxide; Phagocytosis; Phospholipase A2; CR3; complement receptor type 3; C3bi; C3b treated with C3b inactivator; SOZ; serum-opsonized zymosan; PT; pertussis toxin; PMA; phorbol-12-myristate-13-acetate; fMLP; formyl-Met-Leu-Phe; BSA; bovine serum albumin; KRH; Krebs-Ringer HEPES; E; sheep red blood cell; EIgG; E coated with rabbit anti-sheep red blood cell; LFA-1; leukocyte function associated protein-1; C kinase; | |
DOI : 10.1016/0014-5793(94)80578-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Complement receptor type 3 (CR3)-mediated cellular responses in guinea pig macrophages were investigated by using zymosan and serum-opsonized zymosan (SOZ) as the multivalent ligand for CR3. The ingestion of zymosan and SOZ was accompanied by O2 − generation and arachidonate release. These responses were suppressed by prior exposure of macrophages to pertussis toxin (PT). Opsonization of zymosan gave rise to more than 6-fold activation of the ingestion, whereas the magnitude of either arachinonate release or O2 − generation was unchanged. The Fab' fragment of anti-Z-1, a monoclonal antibody specific for the α chain of guinea pig CR3, inhibited the ingestion of zymosan by 60% without affecting zymosan-induced arachidonate release and O2 − generation. These data suggested that there might be at least two functionally distinct binding sites for zymosan. O2 − generation and arachidonate release might be regulated through one site and phagocytosis another. Both sites should be coupled to PT-sensitive GTP binding protein.
【 授权许可】
Unknown
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