Activation of macrophages by a laccase-polymerized polyphenol is dependent on phosphorylation of Rac1

Biochem Biophys Res Commun. 2018 Jan 15;495(3):2209-2213. doi: 10.1016/j.bbrc.2017.12.095. Epub 2017 Dec 18.

Abstract

Various physiologically active effects of polymerized polyphenols have been reported. In this study, we synthesized a polymerized polyphenol (mL2a-pCA) by polymerizing caffeic acid using mutant Agaricus brasiliensis laccase and analyzed its physiological activity and mechanism of action. We found that mL2a-pCA induced morphological changes and the production of cytokines and chemokines in C3H/HeN mouse-derived resident peritoneal macrophages in vitro. The mechanisms of action of polymerized polyphenols on in vitro mouse resident peritoneal cells have not been characterized in detail previously. Herein, we report that the mL2a-pCA-induced production of interleukin-6 (IL-6) and monocyte chemotactic protein-1 (MCP-1) in C3H/HeN mouse-derived resident peritoneal cells was inhibited by treatment with the Rac1 inhibitor NSC23766 trihydrochloride. In addition, we found that mL2a-pCA activated the phosphorylation Rac1. Taken together, the results show that mL2a-pCA induced macrophage activation via Rac1 phosphorylation-dependent pathways.

Keywords: Agaricus brasiliensis; Laccase; Macrophage; Polymerized polyphenol; Rac1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Laccase / chemistry*
  • Macrophage Activation / drug effects
  • Macrophage Activation / immunology*
  • Macrophages / drug effects
  • Macrophages / immunology*
  • Macrophages / pathology*
  • Male
  • Mice
  • Mice, Inbred C3H
  • Neuropeptides / immunology*
  • Phosphorylation / drug effects
  • Polyphenols / administration & dosage*
  • Polyphenols / chemistry*
  • rac1 GTP-Binding Protein / immunology*

Substances

  • Neuropeptides
  • Polyphenols
  • Rac1 protein, mouse
  • Laccase
  • rac1 GTP-Binding Protein