首页    期刊浏览 2024年11月08日 星期五
登录注册

文章基本信息

  • 标题:Inhibition of intercellular adhesion molecule 1-dependent biological activities by a synthetic peptide analog.
  • 本地全文:下载
  • 作者:J V Fecondo ; S B Kent ; A W Boyd
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1991
  • 卷号:88
  • 期号:7
  • 页码:2879-2882
  • DOI:10.1073/pnas.88.7.2879
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:We have used a combination of hydropathy analysis of the intercellular adhesion molecule 1 (ICAM-1) sequence and dot-matrix comparison of the sequence with the homologous, but functionally distinct, protein myelin-associated glycoprotein to identify a putative functional binding region. One polar, and presumably surface-exposed, region of ICAM-1 showed no significant identity with myelin-associated glycoprotein. A synthetic peptide analog based on the sequence of this region (JF9) mimicked the inhibitory effects of the anti-ICAM-1 monoclonal antibody WEHI-CAM-1. These included inhibition of ICAM-1-dependent homotypic aggregation of Raji Burkitt lymphoma and phorbol-ester treated U937 cells at concentrations as low as 80 micrograms/ml (24 microM). In addition, at a concentration of 100 micrograms/ml, the peptide analog effectively inhibited cytotoxic cell activity, an ICAM-1-dependent effector function of the immune response. This simple method of sequence analysis may have general applicability to the identification of functional domains in homologous, but functionally distinct, proteins such as the translated products of gene families.
国家哲学社会科学文献中心版权所有