Antioxidant and semicarbazide-sensitive amine oxidase inhibitory activities of glucuronic acid hydroxamate

Yuh-Hwa Liu; Wen-Li Liang; Chi-Ching Lee; Yow-Fu Tsai; Wen-Chi Hou

doi:10.1016/j.foodchem.2011.04.094

Antioxidant and semicarbazide-sensitive amine oxidase inhibitory activities of glucuronic acid hydroxamate

Food Chem. 2011 Nov 15;129(2):423-428. doi: 10.1016/j.foodchem.2011.04.094. Epub 2011 May 4.

Authors

Yuh-Hwa Liu¹, Wen-Li Liang², Chi-Ching Lee³, Yow-Fu Tsai⁴, Wen-Chi Hou⁵

Affiliations

¹ Division of Gastroenterology, Shin Kong Wu Ho-Su Memorial Hospital, Taipei, Taiwan; Department of Primary Care Medicine, Taipei Medical University, Taipei, Taiwan.
² School of Pharmacy, Taipei Medical University, Taipei, Taiwan; Graduate Institute of Pharmacognosy, Taipei Medical University, Taipei, Taiwan.
³ Graduate Institute of Pharmacognosy, Taipei Medical University, Taipei, Taiwan.
⁴ Department of Chemistry, Chung Yuan Christian University, Chung-Li, Taiwan.
⁵ Graduate Institute of Pharmacognosy, Taipei Medical University, Taipei, Taiwan; Traditional Herbal Medicine Research Center, Taipei Medical University Hospital, Taipei, Taiwan. Electronic address: wchou@tmu.edu.tw.

PMID: 30634247
DOI: 10.1016/j.foodchem.2011.04.094

Abstract

The antioxidant and inhibitory activities of glucuronic acid (GluA) and its synthesized 1-methoxyl-6-glucuronic acid hydroxamate (GluA-NHOH) against semicarbazide-sensitive amine oxidase (SSAO) were investigated. The scavenging activities of GluA-NHOH against 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) radicals (half-inhibition concentration [IC₅₀], 152μM) and hydroxyl radicals (IC₅₀, 70nM) were determined. The protective activities of GluA-NHOH against hydroxyl radical-mediated calf thymus DNA damage and peroxynitrite-mediated dihydrorhodamine oxidation were also investigated. GluA-NHOH, but not GluA, exhibited dose-dependent protective activities. GluA-NHOH, but not GluA, effectively inhibited bovine SSAO activities in a dose-dependent manner, and was further confirmed by AO activity stains on an acrylamide gel. GluA-NHOH showed mixed noncompetitive inhibition of bovine SSAO with respect to benzylamine (substrate) and benzylamine-SSAO (substrate-enzyme complex). The V_max^' and K_m^' values were reduced in the presence of GluA-NHOH (0.04mM).

Keywords: 1-Methoxyl-6-glucuronic acid hydroxamate (GluA-NHOH); Antioxidant activity; Electron spin resonance (ESR).