趋化因子(趋化蛋白)及其受体的研究近年来取得了令人瞩目的进展。这一类结构相似的小分子蛋白均对白细胞有化学趋化作用,一些趋化蛋白还能促进血管生成,刺激某些肿瘤如黑素瘤细胞的生长、以及对造血系统中的祖细胞有抑制作用。趋化蛋白通过与G蛋白偶联受体的结合而传导信息和活化细胞功能。近年来发现数种趋化蛋白受体是艾滋病毒入侵人体细胞的辅助受体。1 趋化因子(蛋白)的结构及分类 趋化因子(chemokine)为一组单链、小分子量(8-10kD)、对白细胞具有正向化学趋化作用的蛋白质。趋化因子在一级结构上具相似性,并由分子内二硫键连接成一定的三级结构。趋化因子在其合成过程中往往受其它炎症因子的调控,其调控一般发生在转录和翻译的水平。所有这些特征表明,趋化因子和传统上所称的“化学趋化因子”(chemoattrac-tant)有所不同。后者并不具备特定的分子内二硫键结构,并可为非蛋白小分子。为准确地反映出这两类同具白细胞趋化作用的因子的不同性质,笔者建议 Research on chemokines (chemotactic proteins) and their receptors has made remarkable progress in recent years. Small molecules of this class have chemical chemotaxis to leukocytes. Some chemotactic proteins also promote angiogenesis, stimulate the growth of certain tumors such as melanoma cells, and inhibit progenitor cells in the hematopoietic system effect. Chemotactic proteins transduce information and activate cellular functions by binding to G-protein coupled receptors. In recent years, several chemotactic protein receptors have been found to be auxiliary receptors for HIV invasion of human cells. Structure and classification of chemokines (chemokines) Chemokine is a group of single chain, small molecular weight (8-10kD) proteins that have a positive chemotactic effect on leukocytes. Chemokines are similar in primary structure and are connected to a certain tertiary structure by intramolecular disulfide bonds. Chemokines are often regulated by other inflammatory factors during their synthesis, and their regulation generally occurs at the transcriptional and translational levels. All of these features suggest that chemokines are different from the so-called “chemoattrac-tant.” The latter does not have a specific intramolecular disulfide bond structure and may be a non-protein small molecule. In order to accurately reflect the different nature of these two types of factors with leukocyte chemotaxis, the author suggests