通过CD98激活CEA-CAM-1介导的细胞黏附：蛋白激酶Cδ的参与

Activation of CEA-CAM-1-mediated cell adhesion via CD98: involvement of PKCdelta.

作者信息

Kakugawa Kiyokazu, Hattori Masakazu, Beauchemin Nicole, Minato Nagahiro

机构信息

Department of Biophysics, Graduate School of Science, Kyoto University, 606-8502 Kyoto, Japan.

出版信息

FEBS Lett. 2003 Sep 25;552(2-3):184-8. doi: 10.1016/s0014-5793(03)00924-4.

DOI:10.1016/s0014-5793(03)00924-4

PMID:14527684

Abstract

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 Cdelta (PKCdelta) to the cell adhesion sites, and rottlerin that inhibited the PKCdelta 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.

摘要

CD98是一种多功能蛋白，参与氨基酸转运以及整合素介导的细胞黏附调节。在此，我们证明抗CD98抗体刺激CD98可在表达癌胚抗原相关细胞黏附分子1（CEA-CAM-1）的BaF3细胞中诱导CEA-CAM-1介导的细胞黏附，并表明这可能是CD98刺激导致F9胚胎癌细胞紧密聚集的原因。抗CD98抗体可共免疫沉淀CEA-CAM-1。CD98刺激诱导细胞质蛋白激酶Cδ（PKCδ）转位至细胞黏附位点，而抑制PKCδ转位的罗勒素可消除细胞聚集，且不影响整合素激活。结果表明，CD98刺激可独立于整合素激活CEA-CAM-1介导的细胞黏附。