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大鼠肝上皮细胞具有能识别溶酶体酶上磷酸化碳水化合物的细胞表面受体。

Epithelial rat liver cells have cell surface receptors recognizing a phosphorylated carbohydrate on lysosomal enzymes.

作者信息

Ullrich K, Mersmann G, Fleischer M, von Figura K

出版信息

Hoppe Seylers Z Physiol Chem. 1978 Nov;359(11):1591-8. doi: 10.1515/bchm2.1978.359.2.1591.

Abstract

Receptor-mediated endocytosis of alpha-N-acetylglucosaminidase by cultured epithelial rat liver cells is inhibited by mannose, L-fucose and most effectively by mannose 6-phosphate. Endocytosis of alpha-N-acetylglucosaminidase is lost after treatment of the enzyme with alkaline phosphatase. These findings indicate that epithelial rat liver cells possess cell surface receptors that recognize a phosphorylated carbohydrate on alpha-N-acetylglucosaminidase, as was previously reported for cell surface receptors of human skin fibroblasts. Inhibition of alpha-mannosidase endocytosis by epithelial rat liver cells in the presence of mannose 6-phosphate and loss of enzyme endocytosis after treatment with alkaline phosphatase suggest that this enzyme is recognized by the same receptor.

摘要

培养的大鼠肝上皮细胞对α-N-乙酰葡糖胺酶的受体介导内吞作用受到甘露糖、L-岩藻糖的抑制,最有效的抑制剂是6-磷酸甘露糖。用碱性磷酸酶处理该酶后,α-N-乙酰葡糖胺酶的内吞作用丧失。这些发现表明,大鼠肝上皮细胞具有细胞表面受体,该受体可识别α-N-乙酰葡糖胺酶上的磷酸化碳水化合物,正如先前关于人皮肤成纤维细胞的细胞表面受体的报道。在6-磷酸甘露糖存在的情况下,大鼠肝上皮细胞对α-甘露糖苷酶内吞作用的抑制以及用碱性磷酸酶处理后酶内吞作用的丧失表明,该酶被相同的受体识别。

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