Mucin-type glycoproteins carrying sialylLeA antigens (SL-GP) were isolated from the ascites fluid of a patient with colorectal cancer. SL-GP bound to E-selectin on endothelial cells in Ca2+- and sialylLeA antigen-dependent manners. To examine the metabolic change in E-selectin caused by ligation, endothelial cells were labeled with 32P-phosphate or 35S-Met and 35S-Cys. Phosphorylation at one or more serine residues of E-selectin was elevated by ligation with SL-GP but not with sialylLeA hexasaccharide. Pulse-labeling of E-selectin with 35S-Met and 35S-Cys in the presence of SL-GP indicated that the degradation of E-selectin was accelerated by SL-GP ligation, but labeling after pre-ligation with SL-GP revealed an increase in the synthesis of E-selectin. The synthesis may reflect compensation for the E-selectin degraded on pre-ligation. These results indicate that the overall metabolism of E-selectin was enhanced by the ligation of SL-GP, with degradation and synthesis being apparently balanced.

译文

从患有结肠直肠癌的患者的腹水中分离出带有唾液酸LeA抗原的粘蛋白型糖蛋白(SL-GP)。 SL-GP以Ca2-和sialylLeA抗原依赖性方式与内皮细胞上的E-选择素结合。为了检查由连接引起的E-选择蛋白的代谢变化,用32P-磷酸或35S-Met和35S-Cys标记内皮细胞。通过与SL-GP而非唾液酸LeA六糖连接,可增强E-选择蛋白一个或多个丝氨酸残基的磷酸化作用。在SL-GP存在下用35S-Met和35S-Cys脉冲标记E-选择素表明SL-GP连接可加速E-选择素的降解,但与SL-GP预连接后的标记显示E-选择素的降解E-选择素的合成增加。该合成可以反映对在预连接时降解的E-选择蛋白的补偿。这些结果表明SL-GP的连接增强了E-选择蛋白的整体代谢,降解和合成明显平衡。

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