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. 2009 Jan;28(1):49-54.
doi: 10.1097/PGP.0b013e3181808021.

Relation between laminin-5 gamma 2 chain and cell surface metalloproteinase MT1-MMP in clear cell carcinoma of the ovary

Noriko Kato  1 , Teiichi Motoyama
Affiliations

Relation between laminin-5 gamma 2 chain and cell surface metalloproteinase MT1-MMP in clear cell carcinoma of the ovary

Noriko Kato et al. Int J Gynecol Pathol. 2009 Jan.

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 gamma 2 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 gamma 2 chain levels by Western blotting. Processed gamma 2 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 gamma 2 chain, especially in the area of papillary architecture. These results indicate that proteolytic processing of the LN-5 gamma 2 chain by MT1-MMP is involved in cell migration and subsequent architectural organization in ovarian CCC.

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