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Malignant cell‐specific gelatinase activity in human endometrial carcinoma
Author(s) -
Takemura Masahiko,
Kimura Tadashi,
Tokugawa Yoshihiro,
Miki Mariko,
Ono Masaaki,
Saji Fumifaka,
Tanizawa Osamu,
Azuma Chihiro
Publication year - 1992
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19920701)70:1<147::aid-cncr2820700124>3.0.co;2-w
Subject(s) - endometrial cancer , gelatinase , enzyme assay , carcinoma , enzyme , endometrium , medicine , coomassie brilliant blue , polyacrylamide gel electrophoresis , staining , sodium dodecyl sulfate , extracellular matrix , cancer cell , cancer , matrix metalloproteinase , pathology , biochemistry , chemistry
Background . The protease activity leading to degradation of the extracellular matrix was compared between human endometrial cancer and normal uterine endometrium. Methods . Conditioned medium from tumor cells and normal endometrial cells was subjected to electrophore‐sis on sodium dodecyl sulfate (SDS)‐polyacrylamide gel containing gelatin as a substrate. After electrophoresis, the gel was stained with Coomassie blue, and then the enzyme activity, expressed as the zone of dye clearing, was analyzed by densitometry. Results . Densitometric analysis showed that all the endometrial cancers expressed a very high molecular weight enzyme activity (Mr 220,000), which was not detected in medium from normal endometrial cells. The analysis also showed that in endometrial cancer the activity of a Mr 92,000 enzyme was always superior to that of a Mr 64,000 enzyme, which was in contrast to the situation for normal endometrium. Conclusions . These results indicate that the expression of Mr 220,000 enzyme activity and the higher activity of the Mr 92,000 enzyme than the Mr 64,000 enzyme are involved in the malignant phenotype of native endometrial cancer.