RT Journal Article
ID 44ab31e9573a147f
A1 Bennett, Louise
A1 Sheean, Paul
A1 Zabaras, Dimitrios
A1 Head, Richard
T1 Heat-Stable Components of Wood Ear Mushroom, Auricularia polytricha (Higher Basidiomycetes), Inhibit In Vitro Activity of Beta Secretase (BACE1)
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2013
FD 2013-04-26
VO 15
IS 3
SP 233
OP 249
K1 medicinal mushrooms
K1 beta secretase
K1 BACE1
K1 food processing
K1 Maillard
K1 Auricularia polytricha
K1 Agaricus bisporus
K1 Flammulina velutipes
K1 Lentinus edodes
AB The consumption of mushrooms has been linked with protection against dementia, including Alzheimer's disease (AD), by several biological pathways including inhibiting beta-site APP-cleaving enzyme (BACE1), which is responsible for releasing toxic β-amyloid peptide in the brain. We have investigated the capacity of several medicinal mushroom species−Auricularia polytricha (wood ear mushroom), Agaricus bisporus (button mushroom), Flammulina velutipes (winter or enoki mushroom), and Lentinus edodes (shiitake mushroom)−in the regulation of BACE1. Mushrooms were subjected to a generic food-compatible processing method to detect process-stable or process-modified products; the effects of processing were interpreted to infer the chemical classes associated with bioactivity. We have shown previously that in addition to enzyme inhibition, in the presence of the BACE1 proenzyme, heteropolymeric species such as heparin can activate BACE1 by modulating access to the catalytic site. We observed both inhibitory and activating components of the various mushrooms. Only BACE1 inhibitory species were detected in unprocessed and processed forms of A. polytricha, whereas the dominant extracted species from A. bisporus, F. velutipes, and L. edodese were activators of BACE1. It is not known whether activating species were masking the presence of inhibitory species in A. bisporus, F. velutipes, and L. edodes. Inhibitory species were attributed to hispidin-derived polyphenols, whereas activating species were attributed to soluble polysaccharides and possibly low-mass Maillard products produced during processing. Larger molecular BACE1-activating species are unlikely to be bioavailable to brain in contrast with possible brain bioavailability of smaller, lipophilic hispidins.
PB Begell House
LK https://www.dl.begellhouse.com/journals/708ae68d64b17c52,3a24b2df76f12ae0,44ab31e9573a147f.html