在PSGL-1的氨基末端的硫酸片段对于P-选择素结合至关重要
D Sako1, K M Comess, K M Barone
1Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140, USA.
Cell
|October 20, 1995
概括
与P-选择蛋白结合的P-选择蛋白糖蛋白连接物1 (PSGL-1) 不仅仅涉及它的糖结构. 聚片段中的硫酸铁对于高亲和度相互作用至关重要.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 免疫学 免疫学 免疫学
背景情况:
- P-选择蛋白糖蛋白连接体1 (PSGL-1) 是细胞粘附中的关键分子,特别是在髓状细胞中.
- PSGL-1调解了与P-选择素的高亲和度结合,这是免疫细胞贩运的关键过程.
- 众所周知,这种相互作用依赖,并且需要PSGL-1上的特定碳水化合物结构 (sialyl-Lewisx).
研究的目的:
- 确定有助于PSGL-1与P-selectin高亲和度结合的非碳水化合物成分.
- 为了阐明PSGL-1-P-选择因子相互作用的精确分子决定因素.
主要方法:
- 这项研究涉及生物化学分析,以确定关键的结合决定因素.
- 可能使用了PSGL-1的氨基酸测序和表征.
主要成果:
- 确定了一个非碳水化合物成分,PSGL-1的前19个氨基酸中的一个阳离子多片段.
- 该部分至少含有一种硫酸铁残留物,该残留物对于高亲和度结合至关重要.
- 含硫氨酸的细分部分与sialyl-Lewisx结构协同起作用.
结论:
- 在PSGL-1上,P-选择素的高亲和度结合点由碳水化合物 (sialyl-Lewisx) 和非碳水化合物 (含硫氨酸的多) 元素组成.
- 这一发现扩大了我们对选择中介细胞粘附的分子基础的理解.
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