Send to

Choose Destination
See comment in PubMed Commons below
Biol Pharm Bull. 2012;35(10):1836-40.

Naringenin inhibits the aggregation of expanded polyglutamine tract-containing protein through the induction of endoplasmic reticulum chaperone GRP78.

Author information

  • 1Department of Biochemistry & Molecular Biology, Division of Biological Sciences, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi, Yamashina-ku, Kyoto 607-8414, Japan.


Polyglutamine (polyQ) diseases are inherited neurodegenerative diseases characterized by the aggregation of proteins containing expanded polyQ tract. Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluorescent protein with a pathological-length polyQ tract (EGFP-polyQ97), but not with a non-pathological-length polyQ tract (EGFP-polyQ24), and the expression levels of GRP78 were inversely related to the aggregation of EGFP-polyQ97. In this study, we performed the screening for compounds that modulate the GRP78 expression in herbal medicines, and found that naringenin, one of the major constitutions of Kanzo (Glycyrrhizae Radix), induced the expression of GRP78 in several mammalian cells. Furthermore, naringenin suppressed the protein aggregation caused by EGFP-polyQ97 in mammalian cells. These findings suggested that naringenin seemed to be a new inducer of GRP78 in mammalian cells, and may be a potential therapeutic agent for diseases caused by ER stress such as polyQ diseases.

[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
    Loading ...
    Support Center