ACCUMULATION OF A NONDEGRADABLE MANNOSE LIGAND WITHIN RABBIT ALVEOLAR MACROPHAGES - RECEPTOR REUTILIZATION IS INDEPENDENT OF LIGAND DEGRADATION
ACCUMULATION OF A NONDEGRADABLE MANNOSE LIGAND WITHIN RABBIT ALVEOLAR MACROPHAGES - RECEPTOR REUTILIZATION IS INDEPENDENT OF LIGAND DEGRADATION
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DOI：
10.1021/bi00303a022
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发表时间：
1984-01-01
期刊：
影响因子：
2.9
通讯作者：
LEE, YC
中科院分区：
文献类型：
--
作者：
HOPPE, CA;LEE, YC
合成的新糖蛋白是通过使5-（叠氮基羰基）戊基1-硫代-α- D-吡喃甘露糖苷与聚（L-赖氨酸）和聚（D-赖氨酸）。125 I-Man 90-poly-D-Lys和125 I-Man 104-poly-L-Lys在2 °处紧密结合。C通过兔肺巨噬细胞的甘露糖受体（Kd = 0.66 ± 0.05）。0.18和0.59 ±。0.26 nM）。在寒冷的饱和条件下，巨噬细胞结合了98，200. 7000和84,200。对于D-和L-聚赖氨酸衍生物，每个细胞分别有10，500个配体分子。细胞表面结合的配体可被EDTA和甘露糖在2.0 ℃下解离。C.在37度。C，巨噬细胞有效地内化125 I-Man 90-poly-D-Lys和125 I-Man 104-poly-L-Lys。虽然内化的125 I-Man 104-poly-L-Lys被巨噬细胞迅速降解为小的放射性标记肽，但内化的125 I-Man 90-H-poly-D-Lys显然不能被降解或胞吐。在细胞内积累的125 I-Man 90-poly-D-Lys的量比表面和细胞内甘露糖受体的总量高7倍，强烈表明受体的再利用与配体的降解无关。
Synthetic neoglycoproteins were made by reacting 5-(azidocarbonyl)pentyl 1-thio-.alpha.-D-mannopyranoside with poly(L-lysine) and poly(D-lysine). The 125I-Man90-poly-D-Lys and 125I-Man104-poly-L-Lys were tightly bound at 2.degree. C by the mannose receptor of the rabbit lung macrophage (Kd = 0.66 .+-. 0.18 and 0.59 .+-. 0.26 nM, respectively). Under saturating conditions in the cold, the macrophage bound 98,200 .+-. 7000 and 84,200 .+-. 10,500 ligand molecules per cell for the D- and L-polylysine derivatives, respectively. The cell-surface-bound ligands were dissociable by EDTA and mannose at 2.degree. C. At 37.degree. C, the macrophages internalized both 125I-Man90-poly-D-Lys and 125I-Man104-poly-L-Lys efficiently. Although the internalized 125I-Man104-poly-L-Lys was degraded quickly by the macrophage to small radiolabeled peptide, the internalized 125I-Man90-H-poly-D-Lys apparently could not be degraded or exocytosed. The amount of 125I-Man90-poly-D-Lys which accumulated within the cell was 7-fold higher than the combined amount of surface and intracellular mannose receptors, strongly indicating reutilization of the receptors independent of degradation of the ligand.