Escherichia coli heat-stable enterotoxins and their receptors.
Escherichia coli heat-stable enterotoxins and their receptors.
复制标题
大肠杆菌热稳定肠毒素及其受体。
DOI：
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发表时间：
1987
期刊：
影响因子：
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通讯作者：
M. Thompson
中科院分区：
文献类型：
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作者：
M. Thompson
ST家族已经发展到包括由许多生物体产生的密切相关的毒素。这些毒素的核心序列可以特异性地和可逆地结合到在肠细胞刷状缘的微绒毛膜中发现的受体。作为特异性结合事件的结果，ST可以通过鸟苷酸环化酶的受体介导的刺激来刺激液体分泌。ST分子的结构已经通过各种技术部分获得。很明显，在不久的将来，这些毒素的关键氨基酸和序列区域将被发现，这将确定毒性的要求。ST无细胞毒性，是研究肠细胞分泌系统的理想探针。ST的受体已被广泛研究，其纯化和表征将产生重要的洞察毒素介导的前列腺增生的逆转，并可能进入非病理性分泌过程。迄今为止，通过交联研究鉴定的54，000 - 57，000和68，000 - 75，000道尔顿结合蛋白的性质尚不清楚。当纯化的ST结合肽和其他成分的分泌级联将成为可用的，他们将提供更好的洞察ST受体-鸟苷酸环化酶复合物分泌途径的实际动态。
The family of ST has grown to include closely related toxins produced by a number of organisms. The core sequence of these toxins can bind specifically and reversibly to a receptor found in the microvillus membranes of the intestinal cell brush border. As a result of a specific binding event, the ST can stimulate fluid secretion via receptor-mediated stimulation of guanylate cyclase. The structure of the ST molecule has been partially obtained through a variety of techniques. It is apparent that in the near future, key amino acids and sequence regions of these toxins will be found that will identify the requirements for toxicity. The ST are ideal probes to study the secretory system of intestinal cells since they are not cytotoxic. The receptor for ST has been extensively studied and its purification and characterization will yield important insight into the reversal of toxin-mediated diarrheas, and possibly into the nonpathological secretory process. As yet, the nature of the 54,000-57,000 and 68,000-75,000 dalton binding proteins identified by cross-linking studies are not known. When purified ST-binding peptides and other components of the secretory cascade will become available, they will provide better insight into the actual dynamics of the ST receptor-guanylate cyclase complex secretory pathway.