人多形核白细胞对促吞噬素的受体介导内吞作用。

Receptor-mediated internalization of tuftsin by human polymorphonuclear leukocytes.

作者信息

Amoscato A A, Davies P J, Babcock G F, Nishioka K

出版信息

J Reticuloendothel Soc. 1983 Jul;34(1):53-67.

Abstract

A high-performance liquid chromatography (HPLC) purified fluorescein-labeled analogue of tuftsin was prepared, which retains the full biological activity of the native molecule. Characterization of the derivatization site by amino acid analysis, N-terminal cleavage, and dansylation revealed a monofluorescinated derivative at the alpha-amino terminus. Binding of the fluorescent tuftsin to living polymorphonuclear leukocytes (PMN) was observed by means of video intensification microscopy. At 37 degrees C, diffuse membrane fluorescence was seen initially, followed by rapid aggregation and internalization. The latter was demonstrated by saltation of intracellular fluorescent aggregates. These processes are temperature-dependent and rely on specific binding to the tuftsin receptor.

摘要

制备了一种经过高效液相色谱（HPLC）纯化的、保留天然分子全部生物活性的荧光素标记的促吞噬素类似物。通过氨基酸分析、N端裂解和丹磺酰化对衍生化位点进行表征，结果显示在α-氨基末端有一个单荧光素化衍生物。通过视频增强显微镜观察到荧光促吞噬素与活的多形核白细胞（PMN）的结合。在37℃时，最初可见弥漫性膜荧光，随后迅速聚集并内化。后者通过细胞内荧光聚集体的跳跃运动得以证明。这些过程依赖于温度，并且依赖于与促吞噬素受体的特异性结合。