Characterization of matrix-degrading proteinases and their inhibitors secreted by human gynecological carcinoma cells

Jpn J Cancer Res. 1995 Jun;86(6):568-76. doi: 10.1111/j.1349-7006.1995.tb02436.x.

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.

MeSH terms

  • Adenocarcinoma, Clear Cell / metabolism
  • Carcinoma / metabolism
  • Choriocarcinoma / metabolism
  • Collagenases / chemistry
  • Collagenases / metabolism*
  • Culture Media, Serum-Free
  • Cystadenocarcinoma, Mucinous / metabolism
  • Endometrial Neoplasms / metabolism*
  • Female
  • Glycoproteins / metabolism
  • Humans
  • Immunoblotting
  • Matrix Metalloproteinase 9
  • Matrix Metalloproteinase Inhibitors
  • Metalloendopeptidases / antagonists & inhibitors
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / metabolism*
  • Molecular Weight
  • Neoplasm Proteins / antagonists & inhibitors
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / metabolism*
  • Ovarian Neoplasms / metabolism*
  • Plasminogen Activator Inhibitor 1 / metabolism
  • Plasminogen Activator Inhibitor 2 / metabolism
  • Proteins / metabolism
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / metabolism
  • Tissue Inhibitor of Metalloproteinase-2
  • Tissue Inhibitor of Metalloproteinases
  • Trypsin / metabolism
  • Tumor Cells, Cultured
  • Urokinase-Type Plasminogen Activator / antagonists & inhibitors
  • Urokinase-Type Plasminogen Activator / metabolism*

Substances

  • Culture Media, Serum-Free
  • Glycoproteins
  • Matrix Metalloproteinase Inhibitors
  • Neoplasm Proteins
  • Plasminogen Activator Inhibitor 1
  • Plasminogen Activator Inhibitor 2
  • Proteins
  • Serine Proteinase Inhibitors
  • Tissue Inhibitor of Metalloproteinases
  • Tissue Inhibitor of Metalloproteinase-2
  • Serine Endopeptidases
  • Trypsin
  • Urokinase-Type Plasminogen Activator
  • Collagenases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 9