Analyses of matrix metalloproteinases and their inhibitors in cyst fluid of serous ovarian tumors

Citation
M. Furuya et al., Analyses of matrix metalloproteinases and their inhibitors in cyst fluid of serous ovarian tumors, PATHOBIOLOG, 68(6), 2000, pp. 239-244
Citations number
19
Categorie Soggetti
Medical Research Diagnosis & Treatment
Journal title
PATHOBIOLOGY
ISSN journal
10152008 → ACNP
Volume
68
Issue
6
Year of publication
2000
Pages
239 - 244
Database
ISI
SICI code
1015-2008(2000)68:6<239:AOMMAT>2.0.ZU;2-9
Abstract
Objectives: Expression of matrix metalloproteinases (MMPs) and tissue inhib itors of MMPs (TIMPs) in serous tumors of the ovary was investigated to det ermine whether and how these proteolytic enzymes are associated with the pr ogression of these tumors. Methods: Cyst fluid of 24 serous ovarian tumors (8 adenocarcinomas, 2 borderline tumors and 14 adenomas) was analyzed using gelatin/casein zymography and enzyme-linked immunosorbent assay. Results: Concentrations of MMP-9 and MMP-2 were statistically higher in serous adeno carcinomas than in serous adenomas (p < 0.01, p < 0.05, respectively), whil e the concentrations of TIMP-1 and TIMP-2 showed no significant difference between adenocarcinomas and adenomas. The molar ratio of TIMP-2/MMP-2 was l ower in adenocarcinomas than in adenomas (p < 0.05). With gelatin zymograph y, the MMP-9 band was detected in all serous adenocarcinomas, but only in 8 of 14 serous adenomas (p = 0.05). Using casein zymography, MMP-7 was more frequently detected in serous adenocarcinomas (7/8) than in serous adenomas (4/14; p < 0.05). Conclusions: These observations indicate that matriolyti c enzymes such as MMP-2, MMP-7 and MMP-9 are secreted into cyst fluid from serous adenocarcinoma tissues. In part, the aggressive invasion of serous c arcinoma cells may be explained by the expression of matriolytic enzymes. C opyright (C) 2001 S. Karger AG, Basel.