Mitochondrial Dysfunction Leads to Deconjugation of Quercetin Glucuronides in Inflammatory Macrophages
Figure 9
Scheme for the proposed mechanism of the deconjugation of quercetin glucuronides by macrophages.
Quercetin glucuronides (Q-GA) bound to the DIDS-sensitive cell surface proteins of macrophages were readily doconjugated into the aglycone (Q) by the β-glucuronidase (β-G) activity under acidic conditions derived from increased lactate secretion associated with mitochondria dysfunction. The β-glucuronidase secretion was promoted by increased intracellular calcium ions (Ca2+). The deconjugated aglycones (Q and the methylated form, MeQ) accumulated in the cells could be the active form for the anti-inflammatory and anti-atherosclerotic activities.
