Activation of CEA‐CAM‐1‐mediated cell adhesion via CD98: involvement of PKCδ

FEBS Letters

Minato, Nagahiro¹  Beauchemin, Nicole²  Hattori, Masakazu¹  Kakugawa, Kiyokazu³ 

[1] Department of Immunology and Cell Biology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan;McGill Cancer Centre, McGill University, Montreal, QC, Canada H3G 1Y6;Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan

关键词: CD98;    CEA-CAM-1;    Cell adhesion;    Protein kinase Cδ;    Embryonic carcinoma;    mAb;    monoclonal antibody;    PI3K;    phosphatidylinositol 3-kinase;    CD98-H;    -L;    CD98 heavy and light chains;   

DOI  :  10.1016/S0014-5793(03)00924-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

CD98 is a multifunctional protein involved in amino acid transport and regulation of integrin-mediated cell adhesion. Herein, we demonstrated that CD98 stimulation by anti-CD98 antibodies induced CEA-CAM-1-mediated cell adhesion in BaF3 cells expressing CEA-CAM-1, and suggest that this might be responsible for compact clumping of F9 embryonic carcinoma cells by CD98 stimulation. CEA-CAM-1 was co-immunoprecipitated by anti-CD98 antibody. CD98 stimulation induced the translocation of cytoplasmic protein kinase Cδ (PKCδ) to the cell adhesion sites, and rottlerin that inhibited the PKCδ translocation abolished the cell aggregation without affecting integrin activation. The results suggested that CD98 stimulation could activate CEA-CAM-1-mediated cell adhesion independently of integrins.

【 授权许可】

Unknown