ACTIVATION OF HUMAN NEUTROPHILS BY ARG-GLY-ASP-SER IMMOBILIZED ON MICROSPHERES

被引:7
作者
KASUYA, Y
FUJIMOTO, K
MIYAMOTO, M
KAWAGUCHI, H
机构
[1] KEIO UNIV, FAC SCI & TECHNOL, DEPT APPL CHEM, KOHOKU KU, YOKOHAMA, KANAGAWA 223, JAPAN
[2] JAPANESE RED CROSS, CTR CENT BLOOD, DEPT RES, SHIBUYA KU, TOKYO, TOKYO 150, JAPAN
来源
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH | 1994年 / 28卷 / 03期
关键词
D O I
10.1002/jbm.820280315
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
The adhesive interaction of cells with extracellular matrix components is essential for a variety of cellular functions, and is frequently mediated by a tetra peptide, Arg-Gly-Asp-Ser (RGDS), located within fibronectin and other proteins. In this study, the RGDS-mediated activation of polymorphonuclear leukocytes accompanied by phagocytosis was investigated using monodisperse polymeric microspheres carrying RGDS. The parent and Arg-Gly-Glu-Ser (RGES)-carrying microspheres, which have no adhesion activity, were employed as controls. The ingestion of microspheres into PMN was not enhanced by immobilizing RGDS. However, PMNs exhibited unique oxygen consumption and enhanced Liberation of reactive oxygen when RGDS-carrying microspheres were phagocytosed. These PMN responses disappeared with the addition of soluble RGDS. Furthermore, cytochalasin D, which inhibits actin polymerization, showed a marked inhibitory effect on oxygen consumption in the RGDS-carrying microsphere system, as compared with those in other systems. These findings show that RGDS-carrying microspheres induced the biospecific activation of PMNs by the signal transduction via RGDS-integrin binding without alteration in the degree of phagocytosis. (C) 1994 John Wiley and Sons, Inc.
引用
收藏
页码:397 / 404
页数:8
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