Shared antigenic epitopes and pathobiological functions of anti-p185her2/neu monoclonal antibodies

被引:40
作者
Zhang, HT
Wang, Q
Montone, KT
Peavey, JE
Drebin, JA
Greene, MI
Murali, R
机构
[1] Univ Penn, Sch Med, Dept Pathol, Philadelphia, PA 19104 USA
[2] Abington Mem Hosp, Dept Pathol, Abington, PA 19001 USA
[3] Washington Univ, Dept Surg, St Louis, MO 63110 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1006/exmp.1999.2266
中图分类号
R36 [病理学];
学科分类号
100104 ;
摘要
We have studied two anti-p185 antibodies: the monoclonal antibody 7.16.4 and rhuMAb 4D5, which were raised against the the ectodomain of rat (p185(neu)), and the human (p185(her2/neu)) homolog, respectively. Studies on the structure of these two antibodies indicate that they share structural similarity in the variable region, especially the CDR3 region, which determines the antibody-antigen interaction. Further studies by flow cytometry revealed that 7.16.4 can compete with rhuMAb4DS for binding to the cell surface p185(her2/neu), suggesting that these two antibodies share an epitope on the p185 receptor. Furthermore, 7.16.4 can also inhibit proliferation and transformation caused by p185(her2/neu). Moreover the rhuMAb 4D5 binds to the rat p185(neu). With the observation that 7.16.4 positively stains human breast cancer tissues that overexpress p185(her2/neu), 7.16.4 may be useful for the pathological diagnosis and therapy of human tumors. (C) 1999 Academic Press.
引用
收藏
页码:15 / 25
页数:11
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