论文摘要
朊病毒是Prion病的病原体,朊蛋白(PrPc)是朊病毒在细胞内的正常表现形式,它以GPI锚定的方式定位在细胞膜上,在各物种间高度保守。PrPc在大脑组织中表达最为丰富,在许多非神经组织包括肌肉、淋巴组织和皮肤中也有表达。尽管在正常的胃粘膜上皮PrPc不表达,但在幽门螺旋杆菌感染后再生的胃粘膜中有PrPc表达的上调。我们先前的研究发现PrPc在胃癌细胞中的表达显著高于癌旁组织,提示PrPc在胃癌的发生发展中可能发挥重要作用。 尽管在过去的许多年中对Prion病的研究取得了很多进展,但与Prion病发病关系密切的PrPc的功能目前还知道不多。PrPc定位在细胞膜的脂筏结构上,这一特殊的细胞膜结构区域包含有大量的细胞膜表面受体和信号传递分子。PrPc有粘附分子的特性,脂筏上的PrPc能与一些细胞外基质和粘附分子相互作用,包括层粘连蛋白、粘多糖分子、层粘连蛋白受体和神经细胞粘附分子等;PrPc还能通过其八肽重复序列结构域与C末端结构域相互作用识别自身。PrPc的粘附特性与它对细胞粘附、神经元生长和细胞存活的调节有关。过表达PrPc能够诱导神经纤维母细胞瘤细胞的粘附和聚集。 既往的研究表明,粘附分子在肿瘤转移的过程中发挥了重要的作用。很多粘附分子,如Integrin、E-selectin和E-cadherin等都与肿瘤的转移密切相关。然而,在胃癌中过表达的PrPc是否与胃癌的转移有关尚不清楚,本课题将对此进行探讨。
论文目录
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