期刊论文详细信息
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.
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【 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.

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