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The expression of nectin-1alpha in normal human skin and various skin tumours
H Matsushima1, A Utani, H Endo
1Department of Dermatology, School of Medicine, Chiba University, 1-8-1 Inohana-cho, Chuou-ku, Chiba 260-8677, Japan.
Background:
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.
Objectives:
To investigate the localization of nectin-1alpha in normal human skin and the alteration of its expression in malignant skin tumours.
Methods:
Immunohistochemistry was employed to determine the expression of nectin-1alpha and other adhesion molecules.
Results:
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.
Conclusions:
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.