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Updated: Feb 5, 2026

Assaying β-amyloid Toxicity using a Transgenic C. elegans Model
Published on: October 9, 2010
A pectin from fruits of Lycium barbarum L. decreases β-amyloid peptide production through modulating APP processing
Lishuang Zhou1, Wenfeng Liao2, Hui Zeng2
1Glycochemistry and Glycobiology Lab, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zu Chong Zhi Road, Shanghai 201203, PR China; University of Chinese Academy of Sciences, No.19A Yuquan Road, Beijing 100049, PR China; School of Pharmacy, Zunyi Medical University, 201 Dalian Road, Zunyi 563000, PR China.
Abstract:
Here, a pectin LBP1C-2 with the molecular weight of 99.8 kDa was purified from fruits of Lycium barbarum L. Its structure was elucidated as a backbone of alternate 1, 2-linked α-Rhap and 1, 4-linked α-GalpA, with branches of terminal (T) -, 1, 3-, 1, 6- and 1, 3, 6-linked β-Galp, T-, 1, 5- and 1, 3, 5-linked α-Araf and T-linked β-Rhap substituted at C-4 of 1, 2, 4-linked α-Rhap. The cell-based experiments indicated that LBP1C-2 suppressed Aβ42 production in a dose-dependent manner with no cytotoxicity. Further study showed that expression of β-site APP cleaving enzyme 1 (BACE1) was attenuated by LBP1C-2, while expression of ADAM10 was up-regulated by LBP1C-2. Moreover, LBP1C-2 promoted the expression of insulin-degradation enzyme (IDE). These results suggested that LBP1C-2 might be a leading compound for anti-Alzheimer's disease therapy by decreasing Aβ42 production through mediating BACE1 and ADAM10 as well as IDE expression.
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