Inhibition of Df-protease associated with allergic diseases by polyphenol

J Agric Food Chem. 1999 Aug;47(8):2969-72. doi: 10.1021/jf9812073.

Abstract

It was reported that Df-protease from house dust mite (Dermatophagoides farinae) catalyzes the activation of the kallikrein-kinin system in human plasma and is closely associated with mite-induced allergy. Therefore, to prevent the release of kinin by Df-protease, the inhibitory activity of polyphenols including catechins and flavonols was tested in vitro and in vivo. Among them, myricetin and epigallocatechin gallate (EGCg) effectively inhibited the amidase activity of Df-protease with K(i) values of 1 x 10(-)(8) and 6 x 10(-)(4) M, respectively. The kinin release in human plasma was extensively inhibited by the addition of EGCg in comparison with myricetin. Enhancement of vascular permeability in guinea pigs caused by Df-protease was markedly suppressed by EGCg.

MeSH terms

  • Animals
  • Catechin / analogs & derivatives
  • Catechin / pharmacology*
  • Flavonoids / pharmacology*
  • Humans
  • Hypersensitivity / prevention & control*
  • Kinetics
  • Kinins / blood
  • Mites / enzymology*
  • Mites / immunology*
  • Phenols / pharmacology*
  • Polymers / pharmacology*
  • Protease Inhibitors / pharmacology*
  • Serine Endopeptidases / immunology*
  • Serine Endopeptidases / metabolism

Substances

  • Flavonoids
  • Kinins
  • Phenols
  • Polymers
  • Protease Inhibitors
  • Catechin
  • epigallocatechin gallate
  • Df protease
  • Serine Endopeptidases