The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy.
The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy.
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DOI：
10.1083/jcb.121.3.491
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发表时间：
1993-05
期刊：
影响因子：
--
通讯作者：
Tsukita S
中科院分区：
文献类型：
--
作者：
Itoh M;Nagafuchi A;Yonemura S;Kitani-Yasuda T;Tsukita S;Tsukita S
我们先前鉴定了质膜底涂层的220-kD组成性蛋白，其在免疫荧光显微镜水平上与钙粘蛋白共定位，并且不仅发生在上皮M.，S. Yonemura，A.长渊山Tsukita和Sh.月田1991. 115：1449-1462）。为了阐明该蛋白的性质和可能的功能，我们克隆了其全长cDNA并进行了序列测定，结果发现小鼠220-kD蛋白与大鼠ZO-1蛋白高度同源，而大鼠ZO-1蛋白只有部分序列已被测定。通过用抗ZO-1抗体的免疫印迹证实了这种关系。由于ZO-1蛋白最初被鉴定为上皮细胞紧密连接的一个组成部分，钙粘蛋白不被认为是本地化的，我们分析了钙粘蛋白和220 kD蛋白的分布，通过冷冻切片免疫电子显微镜。我们发现，在缺乏紧密连接的非上皮细胞中，钙粘蛋白和220-kD蛋白共定位，而在上皮细胞中（例如，携带发育良好的紧密连接钙粘蛋白和220-kD蛋白的肠上皮细胞）分别清楚地分离成粘附蛋白和紧密连接。有趣的是，在上皮细胞，如肝细胞，其紧密连接不是那么发达，220-kD蛋白不仅在紧密连接区，而且在粘附连接检测。此外，我们表明，在小鼠L细胞转染的cDNA编码的N-，P-，E-钙粘蛋白，钙粘蛋白直接或间接地与220 kD的蛋白质相互作用。220 kD蛋白（ZO-1）的可能功能进行了讨论，特别是参考粘附和紧密连接形成的分子机制。
We previously identified a 220-kD constitutive protein of the plasma membrane undercoat which colocalizes at the immunofluorescence microscopic level with cadherins and occurs not only in epithelial M., S. Yonemura, A. Nagafuchi, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 115:1449-1462). To clarify the nature and possible functions of this protein, we cloned its full-length cDNA and sequenced it. Unexpectedly, we found mouse 220-kD protein to be highly homologous to rat protein ZO-1, only a part of which had been already sequenced. This relationship was confirmed by immunoblotting with anti-ZO-1 antibody. As protein ZO-1 was originally identified as a component exclusively underlying tight junctions in epithelial cells, where cadherins are not believed to be localized, we analyzed the distribution of cadherins and the 220-kD protein by ultrathin cryosection immunoelectron microscopy. We found that in non-epithelial cells lacking tight junctions cadherins and the 220-kD protein colocalize, whereas in epithelial cells (e.g., intestinal epithelial cells) bearing well-developed tight junctions cadherins and the 220-kD protein are clearly segregated into adherens and tight junctions, respectively. Interestingly, in epithelial cells such as hepatocytes, which tight junctions are not so well developed, the 220-kD protein is detected not only in the tight junction zone but also at adherens junctions. Furthermore, we show in mouse L cells transfected with cDNAs encoding N-, P-, E-cadherins that cadherins interact directly or indirectly with the 220-kD protein. Possible functions of the 220-kD protein (ZO-1) are discussed with special reference to the molecular mechanism for adherens and tight junction formation.
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影响因子：
11.4
作者：
NOSE, A;NAGAFUCHI, A;TAKEICHI, M
通讯作者：
TAKEICHI, M
DOI：
10.1083/jcb.115.5.1449
发表时间：
1991-12
期刊：
The Journal of cell biology
影响因子：
--
作者：
Itoh M;Yonemura S;Nagafuchi A;Tsukita S;Tsukita S
通讯作者：
Tsukita S
DOI：
10.1083/jcb.107.4.1575
发表时间：
1988-10
期刊：
The Journal of cell biology
影响因子：
--
作者：
Gumbiner B;Stevenson B;Grimaldi A
通讯作者：
Grimaldi A
影响因子：
64.5
作者：
NAGAFUCHI, A;TAKEICHI, M;TSUKITA, S
通讯作者：
TSUKITA, S
编码神经钙依赖性细胞粘附分子的cDNA的克隆和表达：其在钙粘蛋白基因家族中的身份。
DOI：
10.1083/jcb.106.3.873
发表时间：
1988-03
期刊：
The Journal of cell biology
影响因子：
--
作者：
Hatta K;Nose A;Nagafuchi A;Takeichi M
通讯作者：
Takeichi M