Relation Between Laminin-5 γ2 Chain and Cell Surface Metalloproteinase MT1-MMP in Clear Cell Carcinoma of the Ovary


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Abstract

Ovarian clear cell carcinoma (CCC) characteristically shows stromal accumulation of the basement membrane material laminin-5 (LN-5). LN-5 works not only as a substrate for cell anchorage but also as a stimulator for cell migration. Our previous study showed that CCC cell increased migration over excessive LN-5 in vitro. However, it remains unclear why LN-5 rather promotes cell migration than cell anchorage. A recent study has shown that the processing of the LN-5 γ2 chain by membrane type 1-matrix metalloproteinase (MT1-MMP) was responsible for increasing cell migration activity but reducing cell anchoring activity of LN-5. In the present study, 3 CCC cell lines were examined for LN-5 γ2 chain levels by Western blotting. Processed γ2 chain (105 kDa) was detected in the extracellular matrix of all 3 CCC cell lines in vitro. Immunocytochemically they expressed MT1-MMP on the cell surface. In surgical specimens, 22 of 30 (73%) CCCs showed membranous expression of MT1-MMP, and stromal accumulation of the LN-5 γ2 chain, especially in the area of papillary architecture. These results indicate that proteolytic processing of the LN-5 γ2 chain by MT1-MMP is involved in cell migration and subsequent architectural organization in ovarian CCC.

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