Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells
Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells
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DOI：
10.1074/jbc.m112188200
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发表时间：
2002-05-03
影响因子：
4.8
通讯作者：
Yamashita, K
中科院分区：
文献类型：
--
作者：
Hara-Kuge, S;Ohkura, T;Yamashita, K
VIP 36，一种识别高甘露糖型聚糖的细胞内凝集素（Hara-Ruge，S.，Ohkura，T.，Seko，A.，Yamashita，K.（1999）Glycobiology 9，833-839），显示不仅定位于早期分泌途径，而且定位于Madin-Darby犬肾（MDCK）细胞的质膜。在质膜中，VIP 36表现出顶端占优势的分布，顶端/基底侧的比例接近2。与VIP 36一样，VIP 36识别的质膜糖蛋白在顶膜和基底膜中的比例接近2：1。此外，VIP 36识别的分泌糖蛋白从顶膜分泌的效率比从基底膜高出2倍。因此，顶侧/基底侧比的VIP 36识别的糖蛋白的运输与VIP 36在MDCK细胞。在MDCK细胞中过量产生VIP 36后，VIP 36和VIP 36识别的糖蛋白的顶侧/底侧比率从接近2变为接近4，并且VIP 36识别的糖蛋白的分泌被极大地刺激。与VIP 36的过度生产相反，VIP 36的突变体版本没有凝集素活性，对糖蛋白在顶膜和基底膜的分布没有影响，并抑制VIP 36识别的糖蛋白的分泌。此外，VIP 36的过度生产极大地刺激了MDCK细胞的主要顶端分泌糖蛋白clusterin的分泌，clusterin被发现携带至少一个高甘露糖型聚糖并被VIP 36识别。与丛生蛋白的分泌相反，非糖基化的顶端分泌蛋白半乳糖凝集素-3的分泌没有通过过度产生VIP 36而受到刺激。这些结果表明VIP 36参与了携带高甘露糖型聚糖的糖蛋白的转运和分选。
VIP36, an intracellular lectin that recognizes high mannose-type glycans (Hara-Ruge, S., Ohkura, T., Seko, A., and Yamashita, K. (1999) Glycobiology 9, 833-839), was shown to localize not only to the early secretory pathway but also to the plasma membrane of Madin-Darby canine kidney (MDCK) cells. In the plasma membrane, VIP36 exhibited an apical-predominant distribution, the apical/basolateral ratio being similar to2. Like VIP36, plasma membrane glycoproteins recognized by VIP36 were found in the apical and basolateral membranes in the ratio of similar to2 to 1. In addition, secretory glycoproteins recognized by VIP36 were secreted similar to2-fold more efficiently from the apical membrane than from the basolateral membrane. Thus, the apical/basolateral ratio of the transport of VIP36-recognized glycoproteins was correlated with that of VIP36 in MDCK cells. Upon overproduction of VIP36 in MDCK cells, the apical/basolateral ratios of both VIP36 and VIP36-recognized glycoproteins were changed from similar to2 to similar to4, and the secretion of VIP36-recognized glycoproteins was greatly stimulated. In contrast to the overproduction of VIP36, that of a mutant version of VIP36, which has no lectin activity, was of no effect on the distribution of glycoproteins to apical and basolateral membranes and inhibited the secretion of VIP36-recognized glycoproteins. Furthermore, the overproduction of VIP36 greatly stimulated the secretion of a major apical secretory glycoprotein of MDCK cells, clusterin, which was found to carry at least one high mannose-type glycan and to be recognized by VIP36. In contrast to the secretion of clusterin, that of a non-glycosylated apical-secretion protein, galectin-3, was not stimulated through the overproduction of VIP36. These results indicated that VIP36 was involved in the transport and sorting of glycoproteins carrying high mannose-type glycan(s).