title: Characterization of matrix-degrading proteinases and their inhibitors secreted by human gynecological carcinoma cells.
abstract: Matrix-degrading proteinases secreted by tumor cells play crucial roles in tumor cell invasion and metastasis. Serum-free conditioned media of 7 human gynecological carcinoma cell lines were examined for proteinases and their inhibitors by using gelatin zymography, reverse zymography and immunoblotting. All of three ovarian adenocarcinoma cell lines secreted urokinase-type plasminogen activator. Among them, a mucinous cystadenocarcinoma cell line also secreted tissue-type plasminogen activator, plasmin-like enzyme and trypsinogen. On the other hand, two ovarian undifferentiated carcinoma cell lines mainly secreted glatinase A or B. A choriocarcinoma cell line secreted multiple metalloproteinases in the highest amount, whereas an endometrial adenocarcinoma cell line (HEC-1) derived from an early clinical stage hardly secreted any gelatinolytic enzyme. The five high proteinases producers hardly secreted the corresponding inhibitors, such as tissue inhibitor of metalloproteinases (TIMP)-1, -2 or plasminogen activator inhibitor-1. In contrast to these highly malignant cell lines, a poor proteinase producer, HEC-1, secreted a large amount of TIMPs. Therefore, an enhanced proteolytic tendency appears to be associated with gynecological cancer cells established from highly malignant tumors.
authors.affiliation: Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University.
authors.forename: E
authors.initials: E
authors.lastname: Miyagi
authors.forename: H
authors.initials: H
authors.lastname: Yasumitsu
authors.forename: F
authors.initials: F
authors.lastname: Hirahara
authors.forename: H
authors.initials: H
authors.lastname: Minaguchi
authors.forename: N
authors.initials: N
authors.lastname: Koshikawa
authors.forename: K
authors.initials: K
authors.lastname: Miyazaki
authors.forename: M
authors.initials: M
authors.lastname: Umeda
mesh_terms: D018262:Adenocarcinoma, Clear Cell / Q000378:metabolism; D002277:Carcinoma / Q000378:metabolism; D002822:Choriocarcinoma / Q000378:metabolism; D017364:Collagenases / Q000737:chemistry / Q000378:metabolism*; D016895:Culture Media, Serum-Free; D018282:Cystadenocarcinoma, Mucinous / Q000378:metabolism; D016889:Endometrial Neoplasms / Q000378:metabolism*; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D020780:Matrix Metalloproteinase 9; D061965:Matrix Metalloproteinase Inhibitors; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D010051:Ovarian Neoplasms / Q000378:metabolism*; D017395:Plasminogen Activator Inhibitor 1 / Q000378:metabolism; D017396:Plasminogen Activator Inhibitor 2 / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000378:metabolism; D019716:Tissue Inhibitor of Metalloproteinase-2; D019714:Tissue Inhibitor of Metalloproteinases; D014357:Trypsin / Q000378:metabolism; D014407:Tumor Cells, Cultured; D014568:Urokinase-Type Plasminogen Activator / Q000037:antagonists & inhibitors / Q000378:metabolism*
chemical_list: D016895:Culture Media, Serum-Free; D006023:Glycoproteins; D061965:Matrix Metalloproteinase Inhibitors; D009363:Neoplasm Proteins; D017395:Plasminogen Activator Inhibitor 1; D017396:Plasminogen Activator Inhibitor 2; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D019716:Tissue Inhibitor of Metalloproteinase-2; D012697:Serine Endopeptidases; D014357:Trypsin; D014568:Urokinase-Type Plasminogen Activator; D017364:Collagenases; D008666:Metalloendopeptidases; D020780:Matrix Metalloproteinase 9