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缝隙连接与细胞极性:在极化的甲状腺上皮细胞中表达的连接蛋白32和连接蛋白43组装成独立的缝隙连接,它们位于外侧质膜结构域的不同区域。

Gap junctions and cell polarity: connexin32 and connexin43 expressed in polarized thyroid epithelial cells assemble into separate gap junctions, which are located in distinct regions of the lateral plasma membrane domain.

作者信息

Guerrier A, Fonlupt P, Morand I, Rabilloud R, Audebet C, Krutovskikh V, Gros D, Rousset B, Munari-Silem Y

机构信息

Institut National de la Santé et de la Recherche Médicale U369, Faculté de Médecine Alexis Carrel, Lyon, France.

出版信息

J Cell Sci. 1995 Jul;108 ( Pt 7):2609-17. doi: 10.1242/jcs.108.7.2609.

Abstract

Epithelial cells of the thyroid gland present an uncommon connexin expression pattern, they coexpress connexin32 and connexin43. In the present work, we have analyzed the membrane distribution of these two connexins to determine: (i) whether they co-assemble in the same gap junctions or form separate gap junctions; and (ii) whether their location is somehow related to the thyroid cell polarity. Immunofluorescence analyses of the localization of the two connexins in thyroid tissue sections revealed that connexin32 and connexin43 are located in different regions of the plasma membrane. We further analyzed the location of each of the two connexins with regard to that of the tight junction-associated protein, ZO1. Laser scanning confocal microscope observations of connexin32 or connexin43 and ZO1 double-immunolabelled thyroid cells, gave evidence for a separate localization of gap junctions made of each of these two connexins. Connexin32 gap junctions appeared as fluorescent spots scattered over the lateral membrane domain, while connexin43 gap junctions formed a meshed network superimposable with that of tight junctions in the subapical region of the cells. Western blot analyses of the distribution of connexins in thyroid plasma membrane subfractions obtained by ultracentrifugation on a sucrose gradient led to the identification of membrane sub-populations enriched in either connexin32 gap junctions or connexin43 gap junctions. Connexin32 gap junctions and connexin43 gap junctions were found to differ in their resistance to solubilization by N-lauroylsarcosine. Increasing concentrations of this detergent from 0.12% to 0.42% caused a progressive solubilization of connexin43 while connexin32 remained membrane-bound.(ABSTRACT TRUNCATED AT 250 WORDS)

摘要

甲状腺上皮细胞呈现出一种不常见的连接蛋白表达模式,它们共同表达连接蛋白32和连接蛋白43。在本研究中,我们分析了这两种连接蛋白的膜分布情况,以确定:(i)它们是否在同一缝隙连接中共同组装或形成单独的缝隙连接;以及(ii)它们的定位是否与甲状腺细胞极性存在某种关联。对甲状腺组织切片中两种连接蛋白定位的免疫荧光分析显示,连接蛋白32和连接蛋白43位于质膜的不同区域。我们进一步分析了这两种连接蛋白各自相对于紧密连接相关蛋白ZO1的定位。对连接蛋白32或连接蛋白43与ZO1双免疫标记的甲状腺细胞进行激光扫描共聚焦显微镜观察,结果表明由这两种连接蛋白各自形成的缝隙连接定位是分开的。连接蛋白32缝隙连接表现为散布在侧膜区域的荧光斑点,而连接蛋白43缝隙连接在细胞顶端下区域形成了与紧密连接网络重叠的网状网络。通过在蔗糖梯度上超速离心获得的甲状腺质膜亚组分中连接蛋白分布的蛋白质印迹分析,鉴定出了富含连接蛋白32缝隙连接或连接蛋白43缝隙连接的膜亚群。发现连接蛋白32缝隙连接和连接蛋白43缝隙连接在对N-月桂酰肌氨酸溶解的抗性方面存在差异。将这种去污剂的浓度从0.12%增加到0.42%会导致连接蛋白43逐渐溶解,而连接蛋白32仍与膜结合。(摘要截短于250字)

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