Glycosylation of high-affinity thrombin receptors appears necessary for thrombin binding.
Glycosylation of high-affinity thrombin receptors appears necessary for thrombin binding.
复制标题
高亲和力凝血酶受体的糖基化似乎是凝血酶结合所必需的。
DOI：
10.1016/s0006-291x(05)81299-9
复制
发表时间：
1991
影响因子：
3.1
通讯作者：
Carney,DH
中科院分区：
文献类型：
--
作者：
Frost,GH;Bergmann,JS;Carney,DH
单糖结合竞争、凝集素亲和层析和糖基化抑制剂已被用来确定糖基化是否在凝血酶-受体相互作用中发挥作用。甘露糖似乎可以特异性抑制凝血酶与小鼠胚胎 (ME) 和仓鼠成纤维细胞的结合。伴刀豆球蛋白 A 与抗体纯化的受体级分结合，并用作亲和配体来纯化保留凝血酶结合活性的受体级分。用衣霉素（6.25 ng/ml）处理细胞24小时，失去约35%的高亲和力凝血酶结合位点，但受体单克隆抗体TR-9的结合不受影响，表明受体存在于膜中，但无法结合凝血酶。因此，凝血酶受体糖基化可能直接参与凝血酶结合。
Monosaccharide binding competition, lectin affinity chromatography, and glycosylation inhibitors have been used to determine if glycosylation plays a role in thrombin-receptor interactions. Mannose appeared to specifically inhibit thrombin binding to mouse embryo (ME) and hamster fibroblasts. Concanavalin A bound to antibody-purified receptor fractions, and was used as an affinity ligand to purify receptor fractions that retained thrombin binding activity. Cells treated with tunicamycin (6.25 ng/ml) for 24 h lost ∼ 35% of their high-affinity thrombin binding sites, yet binding of receptor monoclonal antibody TR-9 was not affected, indicating that the receptor was present in the membrane, but unable to bind thrombin. Thus thrombin receptor glycosylation may be directly involved in thrombin binding.