Galactose-specific elimination of human asialotransferrin by the bone marrow in the rabbit.
Galactose-specific elimination of human asialotransferrin by the bone marrow in the rabbit.
复制标题
兔骨髓对人脱唾液酸转铁蛋白的半乳糖特异性消除。
DOI：
10.1016/0003-9861(80)90085-5
复制
发表时间：
1980
影响因子：
3.9
通讯作者：
L. Berry
中科院分区：
文献类型：
--
作者：
E. Regoeczi;P. Chindemi;M. Hatton;L. Berry
兔骨髓通过识别糖蛋白中暴露的半乳糖基团的机制在体内吸收并降解人无唾液酸转铁蛋白。继肝脏之后，兔骨髓是第二个被鉴定为具有消除血浆蛋白的半乳糖特异性途径的哺乳动物组织。然而，对含有双触角、三触角和四触角聚糖的去唾液酸化糖蛋白（无唾液酸胎球蛋白、无唾液酸类粘蛋白、鸡α1-酸性糖蛋白和兔转铁蛋白）的比较研究表明，骨髓识别的聚糖结构少于肝脏。骨髓对去唾液酸糖蛋白的最佳吸收和降解需要双触角聚糖的存在。
Rabbit bone marrow accretes and degrades human asialotransferrinin vivothrough a mechanism that recognizes the exposed galactose groups in this glycoprotein. After the liver, rabbit bone marrow is the second mammalian tissue now being identified as possessing a galactose-specific pathway for the elimination of a plasma protein. However, comparative studies with desialylated glycoproteins containing bi-, tri-, and tetraantennary glycans (asialofetuin, asialoorosomucoid, chickenα1-acid glycoprotein, and rabbit transferrin) indicate that the bone marrow recognizes fewer glycan structures than does the liver. Optimal uptake and degradation of an asialoglycoprotein by the bone marrow requires the presence of biantennary glycans.