中文摘要：

asparagine-proline-alanine 序列(NPA 主题) 是高度保存的 inaquaporin 水隧道家庭。AQP1 结构的结晶的研究证明二个 NPA 主题在隧道的狭窄的中央收缩，服务绑为选择、有效的水经过的水分子。在 aquaporin 水隧道的结构，功能和生物的续生说调查二 NPAmotifs 的重要性，我们与 NPA1 删除， NPA2 删除和 NPA1,2 产生了 AQP1mutations 两倍删除。三的编码序列变异 cDNAs 是克隆进哺乳动物的表示向量 pcDNA3.1 形成 expressionplasmids 的潜水艇。我们稳定地证实表示这些 AQP1 mutants.Immunofluorescence 的 transfected CHO 房间行显示都，三变异 AQP1 蛋白质在血浆膜上通常被表示稳定地 transfected。CHO 房间，建议 NPA 主题的那删除不影响表示并且 AQP1 的细胞内部的处理。功能的分析证明分别地， thatNPA1 或 NPA2 删除在 49.6% 和 46.7% 减少了 AQP1 水渗透两倍删除有的 whileNPA1,2 AQP1 上的小效果流水渗透。这些结果提供 NPA 主题为表示，细胞内部的处理和 AQP1 水隧道的基本结构为水浸透然而并非必需品是重要的证据。

英文摘要：

The asparagine.proline-alanine sequences （NPA motifs） are highly conserved in aquaporin water channel family. Crystallographlc studies of AQP1 structure demonstrated that the two NPA motlfs are in the narrow central constriction of the channel, serving to bind water molecules for selective and efficlent water passage. To investigate the importance of the two NPA motifs in the structure, function and biogenesis of aquaporin water channels, we generated AQP1 mutations with NPAI deletion, NPA2 deletion and NPA1,2 double deletion. The coding sequences of the three mutated cDNAs were subcloned into the mammalian expression vector pcDNA3.1 to form expression plasmids. We established stably transfected CHO cell lines expressing these AQP1 mutants. Immunofluorescence indicated that all the three mutated AQP1 proteins are expressed normally on the plasma membrane of stably transfected CHO cells, suggestlng that deletion of NPA motifs does not influence the expression and intracellular processing of AQP1. Functional analysis demonstrated that NPA1 or NPA2 deletion reduced AQP1 water permeabllity by 49.6% and 46.7%, respectively, while NPA1,2 double deletion had little effect on AQP1 water permeability. These results provide evidence that NPA motifs are important for water permeatlon but not essential for the expression, intracellular processing and the basic structure of AQP1 water channel.