Laminin-5 gamma2 chain and matrix metalloproteinase-2 expression in the neoplastic changes of uterine cervical squamous epithelium.

Laminin-5 is an essential component of epithelial basal membranes. Matrix metalloproteinase-2 (MMP-2) changes laminin-5 from static to migratory substrate by cleaving the short arm of the gamma2 subunit of the laminin-5. Recently, the expression of laminin-5 gamma2 chain has been reported to be a marker of invasiveness of epithelial malignant tumors. We investigated the expression of laminin-5 gamma2 chain and MMP-2 in the neoplastic changes of uterine cervical squamous epithelium. Tissue samples of normal uterine cervix, cervical intraepithelial neoplasia-1, -3 (CIN-1, -3) and squamous cell carcinoma keratinizing (SCC-K) and non-keratinizing (SCC-NK) were analyzed for expression of the laminin-5 gamma2 chain and MMP-2 by immunohistochemistry. In normal uterine cervix and CIN-1, laminin-5 gamma2 chain was immunolocalized only in the basal membrane. In CIN-3, expression of laminin-5 gamma2 chain and MMP-2 became apparent at the epithelial-stromal interface of epithelial cells. In SCC-K and SCC-NK, laminin-5 gamma2 chain and MMP-2 expression were abundant at the epithelial-stromal interface of tumor clusters. These results suggest that the expression of laminin-5 gamma2 chain and MMP-2 may be involved in the process of neoplastic changes of uterine cervical squamous epithelium.