Expression of a novel beta 1 integrin in the dysplastic progression of the cervical epithelium.

Epithelial cell interactions with matrices and basal membranes are central for tissue organization, and integrins are a family of adhesion molecules that play a major role in these interactions. We have analyzed the expression of a novel integrin alpha chain, alpha 10.1.2, in the squamous epithelium of the portio vaginalis uteri from patients with cervical intraepithelial neoplasia (CIN) and from control samples without apparent cervical abnormalities. The localization of beta 1 and alpha 6 chains was also investigated, together with the distribution of intraepithelial HLA-DR and CD1c-positive Langerhans cells. In the normal cervical epithelium, all of the integrin chains were detected in the basal cell layer, albeit with a different localization in the apical, lateral, and basal cell surfaces. Langerhans cells were evenly distributed in the deep 2/3 of the squamous epithelium. Expression of alpha 10.1.2 was reduced or absent in all of the CIN 1 specimens in which the other integrin chains were either normal or slightly reduced. CIN 2 was characterized by overexpression of integrins, namely of beta 1 and of alpha 10.1.2 chains which were consistently detected also in suprabasal cell layers. None of the integrin chains was found in CIN3 samples in which Langerhans cells were also absent. Thus, modulation and redistribution of integrins occur in the progression of cervical dysplasia, and lack of integrin expression characterizes high-grade lesions. As in other dysplasias and cancers of squamous epithelia, the localization of alpha 10.1.2 chains provides reliable diagnostic and possibly prognostic criteria.