The 10.1.2 MoAb reacts with a novel α chain that associates with the β1 integrin chain and is widely distributed among epithelial and endothelial cells of human adult and fetal tissues. In the epidermis and in other squamous epithelia, α10.1.2 chains are expressed exclusively in the basal cell layer. Here we describe the immunohistochemical localization of α10.1.2 in human epidermis, in other scuamous epithelia, as well as in cultured keratinocytes. α10.1.2 gain localization has also been investigated in a variety of non-neoplastic and neoplastic lesions of the skin, the uterine cervix, and the lung. We show that α10.1.2 chains retain their basal keratinocyte localization in hyperplastic skin diseases and in benign tumors of the epidermis and that they are strongly expressed in basal cell carcinomas. In contrast, α10.1.2 expression is decreased in keratinocytes that differentiate in vitro and is lost in epidermal dysplastic conditions, in the invading front of squamous cell carcinomas of the epidermis, in microinvasive cervical cancers, and in well-differentiated squamous lung tumors. These findings indicate that α10.1.2 β1 integrin is downregulated during keratinocyte differentiation in vitro and in vivo. Moreover, lack of α10.1.2 expression in basal cells of squamous epithelia is associated with early dysplastic changes and with the acquisition of invasive capacity.
|Number of pages||6|
|Journal||Journal of Investigative Dermatology|
|Publication status||Published - Feb 1994|
- adhesion molecules
- skin cancer
- tumor invasion
ASJC Scopus subject areas