Production and characterization of fusion proteins containing transferrin and nerve growth factor
Production and characterization of fusion proteins containing transferrin and nerve growth factor
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DOI：
10.3109/10611869808997881
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发表时间：
1998-01-01
影响因子：
4.5
通讯作者：
Putney, SD
中科院分区：
文献类型：
--
作者：
Park, E;Starzyk, RM;Putney, SD
为了探索使用转铁蛋白的基因融合物作为脑靶向和递送载体的能力，在哺乳动物细胞中产生了一系列含有人神经生长因子（NGF）和人转铁蛋白的融合蛋白。来自人IgG（3）的铰链区与NGF的羧基末端和转铁蛋白的氨基末端连接的蛋白质形成了共价同二聚体，与人转铁蛋白受体结合，并在PC 12细胞中保留了完整的NGF。相反，多肽二聚化未被诱导的蛋白质或NGF通过其氨基末端融合的蛋白质具有大大降低的NGF活性。作为融合蛋白的一部分维持生物活性的NGF和转铁蛋白的能力可能提供一种新的方式来将NGF和其他神经营养因子递送到中枢神经系统。
To explore the ability to use genetic fusions of transferrin as a carrier for brain targeting and delivery a series of fusion proteins containing both human nerve growth factor (NGF) and human transferrin was produced in mammalian cells. A protein in which the hinge region from human IgG(3) joined the carboxyl terminus of NGF and the amino terminus of transferrin formed a covalent homodimer, bound human transferrin receptor, and retained full NGF in PC12 cells. In contrast, proteins in which polypeptide dimerization was not induced or in which NGF was fused through its amino terminus had greatly reduced NGF activity. The ability to maintain both biologically active NGF and transferrin as part of a fusion protein may offer a novel way to deliver NGF and other neurotrophic factors to the central nervous system.