Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.23 (MMP)
 4,246 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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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PMID:Relation between laminin-5 gamma 2 chain and cell surface metalloproteinase MT1-MMP in clear cell carcinoma of the ovary. 1904 8