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Tenuifolin, an extract derived from tenuigenin , inhibits amyloid‐β secretion in vitro
Author(s) -
Lv J.,
Jia H.,
Jiang Y.,
Ruan Y.,
Liu Z.,
Yue W.,
Beyreuther K.,
Tu P.,
Zhang D.
Publication year - 2009
Publication title -
acta physiologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.591
H-Index - 116
eISSN - 1748-1716
pISSN - 1748-1708
DOI - 10.1111/j.1748-1716.2009.01961.x
Subject(s) - secretion , in vitro , transfection , cell culture , chemistry , enzyme , biochemistry , pharmacology , biology , microbiology and biotechnology , gene , genetics
Aim: Previous studies have shown that tenuigenin , a crude extract of Polygala tenuifolia Willd. that is commonly used in traditional Chinese herbal medicine for memory loss, can reduce the secretion of Aβ from cultured cells. However, the mechanism underlying this effect and the active compound derived from tenuigenin is unknown. In this study, a purified component of tenuigenin , tenuifolin, was examined and revealed to be an effective compound in vitro. Methods: Aβ secretion from three sets of COS‐7 cells, each carrying a plasmid expressing a different form of APP was examined following the treatment with tenuifolin. Initially, tenuifolin was determined to have no inherent toxicity to either the transfected or wild type cells at the effective concentrations. Cells were then treated with 0.5–2.0 μg mL −1 tenuifolin for 12 h and their media were examined via an ELISA for Aβ1‐40 and Aβ‐42. Results: We found that treatment with 2.0 μg mL −1 tenuifolin significantly decreased Aβ secretion from COS‐7 cells without altering the ratio of Aβ1‐40 and Aβ‐42. This effect is most probably due to inhibition of the β‐site APP cleaving enzyme as Aβ secretion was not inhibited from cells expressing the C99 fragment. Conclusion: Tenuifolin is an effective compound from tenuigenin . We believe that this finding should lead the way for future experiments to determine the exact mechanism for tenuifolin’s effect on Aβ secretion.