title: Characterization of extracellular matrix-degrading proteinase and its inhibitor in gynecologic cancer tissues with clinically different metastatic form.
abstract: BACKGROUND
  The authors conducted a comparison study of matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase-1 (TIMP-1) activities in clinically different metastatic types of ovarian cancer, cervical cancer, and endometrial cancer tissues.
  
  
  METHODS
  Gelatinase activity in culture medium obtained from each cancer tissue was detected by zymography and was quantitated by densitometer. Tissue inhibitor of metalloproteinase-1 activity was measured in culture medium by the human TIMP-1 enzyme immunoassay kit.
  
  
  RESULTS
  Six dominant gelatinases were detected in ovarian, cervical, and endometrial cancers: 200-kDa; 130-kDa; 92-kDa (MMP-9); 83-kDa, which is an active form of 92-kDa gelatinase; 72-kDa (MMP-2); and 66-kDa gelatinase, which is an active form of 72-kDa gelatinase. The 92-kDa and 72-kDa gelatinolytic bands were present in all samples. The expression rates of 200-, 130-, and 83-kDa gelatinase in endometrial cancer and cervical cancer tissues were higher than that observed in ovarian cancer tissue. Densitometric analysis showed that the 92-kDa/72-kDa ratio was significantly higher in cervical cancer tissue than in ovarian and endometrial cancer tissues (P < 0.05), and the 66-kDa/72-kDa ratio was significantly higher in endometrial cancer tissue than in ovarian cancer tissue (P < 0.01). Tissue inhibitor of metalloproteinase-1 activity was significantly lower in cervical cancer tissue than in ovarian and endometrial cancer tissues (P < 0.01).
  
  
  CONCLUSIONS
  These results reflect the difference of metastatic forms and are indicative of the possibility of the strong relationship to MMP activity in the invasion and metastasis of cervical cancer and endometrial cancer, compared with those of ovarian cancer.
authors.affiliation: Department of Obstetrics and Gynecology, Nagoya University School of Medicine, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Tamakoshi
authors.forename: F
authors.initials: F
authors.lastname: Kikkawa
authors.forename: A
authors.initials: A
authors.lastname: Nawa
authors.forename: H
authors.initials: H
authors.lastname: Ishikawa
authors.forename: K
authors.initials: K
authors.lastname: Mizuno
authors.forename: A
authors.initials: A
authors.lastname: Tamakoshi
authors.forename: S
authors.initials: S
authors.lastname: Yamagata
authors.forename: N
authors.initials: N
authors.lastname: Suganuma
authors.forename: Y
authors.initials: Y
authors.lastname: Tomoda
mesh_terms: D017364:Collagenases / Q000378:metabolism*; D016889:Endometrial Neoplasms / Q000201:enzymology / Q000473:pathology; D005260:Female; D018093:Gelatinases / Q000378:metabolism*; D005833:Genital Neoplasms, Female / Q000201:enzymology* / Q000473:pathology*; D006023:Glycoproteins / Q000037:antagonists & inhibitors*; D006801:Humans; D007124:Immunoenzyme Techniques; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9; D008666:Metalloendopeptidases / Q000378:metabolism*; D010051:Ovarian Neoplasms / Q000201:enzymology / Q000473:pathology; D011480:Protease Inhibitors / Q000378:metabolism*; D019714:Tissue Inhibitor of Metalloproteinases; D002583:Uterine Cervical Neoplasms / Q000201:enzymology / Q000473:pathology
chemical_list: D006023:Glycoproteins; D011480:Protease Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D017364:Collagenases; D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9