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Background: The root and bark of Cercis chinensis Bunge have been used as Chinese herbal medicines for stroke, hypertension, and gynecological diseases. The seed of C. chinensis is classified as a food ingredient in the Food Public Code. In this study, the inhibitory activities of Cercis chinensis Bunge seed against beta-amyloid (Aβ) secretion and acetylcholinesterase (AChE) were investigated.
Methods and Results: The effect of 50% ethanolic extract of C. chinensis Bunge seed (CCS) on Aβ secretion in APPswe cells was analyzed by Aβ enzyme-linked immunosorbent assay (ELISA). CCS dose-dependently decreased Aβ1-42 secretion at 50 and 100 ㎍/㎖. The half-maximal inhibitory concentration (IC50) values of CCS were 45.02 ㎍/㎖ in Aβ1-40 and 43.48 ㎍/㎖ in Aβ1-42. To analyze the metabolism of amyloid precursor protein (APP) via β-secretase, the beta-carboxyl-terminal fragment (β-CTF) level was measured via ELISA and was found to be dose-dependently increased upon CSS treatment. Additionally, western blot analysis was performed to check the protein expression level of APP, soluble alpha (sAPPα), and CTF. The APP protein level did not change upon CCS treatment but sAPPα secretion level increased, indicating a tendency to increase both α- and β-CTF. These results suggest that CCS reduces Aβ secretion by targeting γ-secretase. Additionally, CCS showed a strong AChE inhibitory activity at an IC50 value of 8.37 ㎍/㎖.
Conclusions: CCS exhibited Aβ reduction via γ-secretase and AChE inhibition and may be used as a material to develop healthy functional foods and medicine for Alzheimer"s disease treatment.
Methods and Results: The effect of 50% ethanolic extract of C. chinensis Bunge seed (CCS) on Aβ secretion in APPswe cells was analyzed by Aβ enzyme-linked immunosorbent assay (ELISA). CCS dose-dependently decreased Aβ1-42 secretion at 50 and 100 ㎍/㎖. The half-maximal inhibitory concentration (IC50) values of CCS were 45.02 ㎍/㎖ in Aβ1-40 and 43.48 ㎍/㎖ in Aβ1-42. To analyze the metabolism of amyloid precursor protein (APP) via β-secretase, the beta-carboxyl-terminal fragment (β-CTF) level was measured via ELISA and was found to be dose-dependently increased upon CSS treatment. Additionally, western blot analysis was performed to check the protein expression level of APP, soluble alpha (sAPPα), and CTF. The APP protein level did not change upon CCS treatment but sAPPα secretion level increased, indicating a tendency to increase both α- and β-CTF. These results suggest that CCS reduces Aβ secretion by targeting γ-secretase. Additionally, CCS showed a strong AChE inhibitory activity at an IC50 value of 8.37 ㎍/㎖.
Conclusions: CCS exhibited Aβ reduction via γ-secretase and AChE inhibition and may be used as a material to develop healthy functional foods and medicine for Alzheimer"s disease treatment.
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UCI(KEPA) : I410-ECN-0101-2021-524-002145350
