Proteinase-3 directly activates MMP-2 and degrades gelatin and Matrigel; differential inhibition by (-)epigallocatechin-3-gallate

Elga Pezzato, Massimo Donà, Luigi Sartor, Isabella Dell'Aica, Roberto Benelli, Adriana Albini, Spiridione Garbisa

Research output: Contribution to journalArticle

Abstract

Proteinase-3 (PR-3), a serine-proteinase mainly expressed by polymorphonuclear leukocytes (PMNs), can degrade a variety of extracellular matrix proteins and may contribute to a number of inflammation-triggered diseases. Here, we show that in addition to Matrigel™ components, PR-3 is also able to degrade denatured collagen and directly activate secreted but not membrane-bound pro-MMP-2, a matrix metallo-proteinase instrumental to cellular invasion. In contrast, following addition of purified PR-3 or PMNs to HT1080 tumor cells, dose-dependent inhibition of in vitro Matrigel™ invasion is registered. (-)Epigallocatechin-3-gallate (EGCG), the main flavanol in green tea and known to inhibit inflammation and tumor invasion, exerts dose-dependent inhibition of degradation of gelatin (IC50

Original languageEnglish
Pages (from-to)88-94
Number of pages7
JournalJournal of Leukocyte Biology
Volume74
Issue number1
DOIs
Publication statusPublished - Jul 2003

Keywords

  • EGCG
  • Gelatinolysis
  • Neutrophils

ASJC Scopus subject areas

  • Cell Biology

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