Matsushima H, Utani A, Endo H, Matsuura H, Kakuta M, Nakamura Y, Matsuyoshi N, Matsui C, Nakanishi H, Takai Y, Shinkai H
Department of Dermatology, School of Medicine, Chiba University, 1-8-1 Inohana-cho, Chuou-ku, Chiba 260-8677, Japan.
Br J Dermatol. 2003 Apr;148(4):755-62. doi: 10.1046/j.1365-2133.2003.05225.x.
A novel cell-cell adhesion system that consists of nectin and afadin has been identified at cadherin-based cell-cell adherens junctions. Nectin is a Ca2+-independent homophilic and heterophilic cell adhesion molecule that belongs to the immunoglobulin superfamily. Nectin has recently been shown to serve as an alpha-herpesvirus entry and cell-cell spread mediator. In spite of the ubiquitous expression of nectin-1alpha, its detailed localization in human skin has not been examined so far.
To investigate the localization of nectin-1alpha in normal human skin and the alteration of its expression in malignant skin tumours.
Immunohistochemistry was employed to determine the expression of nectin-1alpha and other adhesion molecules.
We detected nectin-1alpha in normal human epidermis, follicles and eccrine ducts. Nectin-1alpha was colocalized with E-cadherin at cell-cell adherens junctions of the epidermis. The concentration of the nectin-afadin system at cell-cell adherens junctions was reduced in the early stage of malignant transformation of keratinocytes, such as in basal cell carcinomas and squamous cell carcinomas, where the cadherin-catenin system was preserved. Nectin-1alpha at cell-cell adherens junctions was reduced in human epithelial cancer cells located at the advancing border of the tumour.
Our results showed that nectin-1alpha is located at cell-cell adherens junctions in human skin and that reduction of nectin-1alpha at cell-cell adherens junctions may be involved in the invasion of squamous cell tumours.
在基于钙黏蛋白的细胞间黏附连接中，已鉴定出一种由nectin和afadin组成的新型细胞间黏附系统。Nectin是一种不依赖Ca2+的同嗜性和异嗜性细胞黏附分子，属于免疫球蛋白超家族。最近研究表明，Nectin可作为α-疱疹病毒的进入和细胞间传播介质。尽管nectin-1α广泛表达，但其在人皮肤中的详细定位迄今尚未研究。
研究nectin-1α在正常人体皮肤中的定位及其在恶性皮肤肿瘤中表达的变化。
采用免疫组织化学法检测nectin-1α和其他黏附分子的表达。
我们在正常人体表皮、毛囊和小汗腺导管中检测到nectin-1α。Nectin-1α与E-钙黏蛋白在表皮的细胞间黏附连接处共定位。在角质形成细胞恶性转化的早期阶段，如基底细胞癌和鳞状细胞癌中，细胞间黏附连接处的nectin-afadin系统浓度降低，而钙黏蛋白-连环蛋白系统得以保留。在肿瘤前沿的人上皮癌细胞中，细胞间黏附连接处的nectin-1α减少。
我们的结果表明，nectin-1α位于人皮肤的细胞间黏附连接处，细胞间黏附连接处nectin-1α的减少可能与鳞状细胞瘤的侵袭有关。
