STREPTAVIDIN CONTAINS AN RYD SEQUENCE WHICH MIMICS THE RGD RECEPTOR DOMAIN OF FIBRONECTIN
STREPTAVIDIN CONTAINS AN RYD SEQUENCE WHICH MIMICS THE RGD RECEPTOR DOMAIN OF FIBRONECTIN
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DOI：
10.1016/0006-291x(90)90526-s
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发表时间：
1990-08-16
影响因子：
3.1
通讯作者：
WILCHEK, M
中科院分区：
文献类型：
--
作者：
ALON, R;BAYER, EA;WILCHEK, M
链霉亲和素以低水平和高亲和力与细胞表面结合，其原因可以追溯到蛋白质分子中含有赖德（Arg-Tyr-Asp）的序列的出现。这种结合在生物素存在下增强。细胞结合的链霉亲和素可以被纤连蛋白以及含有RGD和RYD的肽取代。此外，链霉亲和素可以从细胞表面置换纤连蛋白。因此，链霉亲和素的赖德序列模拟RGD（Arg-Gly-Asp），其是存在于纤连蛋白和其他粘附相关分子中的通用识别结构域。观察到的细胞粘附与生物素结合无关，因为赖德序列不是链霉亲和素的生物素结合位点的一部分。由于链霉亲和素在亲和素-生物素技术中的使用是基于其生物素结合特性，因此研究人员在此警告不要在组织化学和细胞化学研究中不加选择地使用它。
Streptavidin binds at low levels and high affinity to cell surfaces, the cause of which can be traced to the occurrence of a sequence containing RYD (Arg-Tyr-Asp) in the protein molecule. This binding is enhanced in the presence of biotin. Cell-bound streptavidin can be displaced by fibronectin, as well as by RGD- and RYD-containing peptides. In addition, streptavidin can displace fibronectin from cell surfaces. The RYD sequence of streptavidin thus mimics RGD (Arg-Gly-Asp), the universal recognition domain present in fibronectin and other adhesion-related molecules. The observed adhesion to cells has no relevance to biotin-binding since the RYD sequence is not part of the biotin-binding site of streptavidin. Since the use of streptavidin in avidin-biotin technology is based on its biotin-binding properties, researchers are hereby warned against its indiscriminate use in histochemical and cytochemical studies.