The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins.
The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins.
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DOI：
10.1016/s0021-9258(17)38407-7
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发表时间：
1986-06
期刊：
影响因子：
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通讯作者：
M. Lehrman;Salvatore;PizzoV;Michael;Imber;R. Hill
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文献类型：
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作者：
M. Lehrman;Salvatore;PizzoV;Michael;Imber;R. Hill
通过糖蛋白中寡糖非还原末端的岩藻糖结合糖蛋白的肝受体的性质已经通过三种不同的方法进行了研究。首先，借助于牛血清白蛋白（BSA）的新糖蛋白，在小鼠中检查静脉注射的糖蛋白从血液中的清除。岩藻糖基-BSA的清除是快速的，并且不被抑制由半乳糖或肝脏的甘露糖/N-乙酰葡糖胺受体介导的清除的糖蛋白强烈抑制。Fuc alpha 1，3（Gal beta 1，4）GlcNAc-BSA（其中Fuc为岩藻糖）的清除受到Fuc-BSA或Gal beta 1，4GlcNAc-BSA的微弱抑制，但受到两种新糖蛋白混合物的强烈抑制，表明其清除由肝半乳糖受体以及岩藻糖结合受体介导。第二，检查新糖蛋白与小鼠肝脏的膜部分的结合。Fuc-BSA与膜的结合是Ca 2+依赖性的，但不受抑制半乳糖或甘露糖/N-乙酰葡糖胺受体的糖蛋白的抑制。此外，Fuc-BSA和Gal β 1，4GlcNAc-BSA的结合作为pH的函数而不同，与Fuc-BSA通过岩藻糖特异性肝受体的结合雅阁。最后，检查了新糖蛋白与来自大鼠肝脏的纯半乳糖凝集素的结合。Fuc-BSA和Fuc α 1，2Gal β 1，4GlcNAc-BSA都不结合半乳糖凝集素，尽管Fuc α 1，3（Gal β-1，4）GlcNAc-BSA强烈结合。总之，这些研究表明，岩藻糖结合受体，不同于半乳糖和甘露糖/N-乙酰葡糖胺受体可能存在于大鼠和小鼠肝脏。
The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fuc alpha 1,3(Gal beta 1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Gal beta 1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, suggesting that its clearance was mediated by hepatic galactose receptors as well as by a fucose-binding receptor. Second, the binding of neoglycoproteins to a membrane fraction of mouse liver was examined. Fuc-BSA binding to membranes was Ca2+ dependent but was not inhibited by glycoproteins that would inhibit the galactose or the mannose/N-acetylglucosamine receptors. In addition, the binding of Fuc-BSA and Gal beta 1,4GlcNAc-BSA differed as a function of pH, in accord with binding of Fuc-BSA through fucose-specific hepatic receptors. Finally, the binding of neoglycoproteins to the pure galactose lectin from rat liver was examined. Neither Fuc-BSA nor Fuc alpha 1,2Gal beta 1,4GlcNAc-BSA bound the galactose lectin, although Fuc alpha 1,3(Gal beta-1,4) GlcNAc-BSA bound avidly. Taken together, these studies suggest that a fucose-binding receptor that differs from the galactose and the mannose/N-acetylglucosamine receptors may exist in rat and mouse liver.