Down-regulation of trypsinogen-2 expression by chemically modified tetracyclines: association with reduced cancer cell migration

Int J Cancer. 2000 May 15;86(4):577-81. doi: 10.1002/(sici)1097-0215(20000515)86:4<577::aid-ijc21>3.0.co;2-j.

Abstract

Many types of human tumor express trypsinogen-2, which may be a significant factor in the activation of pro-MMPs and the invasiveness of tumors. Prevention of trypsinogen-2 expression in cancer cells might be of benefit in cancer therapy. We describe here chemicals capable of down-regulating the expression of trypsinogen-2. Doxycycline (DOXY) and chemically modified tetracyclines (CMTs), previously known as inhibitors of the matrix metalloproteinase (MMP)-dependent proteinase cascade, down-regulated the mRNA and protein expression of trypsinogen-2 by COLO-205 human colon adenocarcinoma cells at therapeutically attainable concentrations (0. 1 to 1.0 microM). DOXY specifically inhibited the activation of pro-MMP-9 and cell migration induced by enteropeptidase, a specific activator of trypsinogen. Pro-MMP-9 activation and cell migration were also inhibited by tumor-associated trypsin inhibitor (TATI), which is a highly specific inhibitor of trypsin. CMT-3 as well as CMT-5 also inhibited cell migration, but an effect on the enteropeptidase-enhanced activation of pro-MMP-9 was not observed. Our results indicate that CMTs, DOXY and TATI inhibit cancer cell migration by down-regulating trypsinogen-2 expression or activity. Inhibition of trypsinogen-2 expression may represent a mechanism contributing to the ability of CMTs to suppress the pericellular proteolytic activity of some tumors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • Cell Division / drug effects
  • Cell Movement / drug effects
  • Down-Regulation
  • Enzyme Precursors / metabolism
  • Gene Expression Regulation / drug effects*
  • Humans
  • Matrix Metalloproteinase 9 / metabolism
  • Tetracyclines / pharmacology*
  • Trypsin Inhibitors / pharmacology
  • Trypsin*
  • Trypsinogen / antagonists & inhibitors*
  • Trypsinogen / genetics
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Enzyme Precursors
  • Tetracyclines
  • Trypsin Inhibitors
  • PRSS2 protein, human
  • Trypsinogen
  • Trypsin
  • Matrix Metalloproteinase 9