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Journal of Biochemistry Advance Access published online on October 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp163
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Inhibition of Calcineurin by Quercetin in vitro and in Jurkat cells

Hu Wanga,b, Chun-Lei Zhoua, Hong Leia and Qun Wei*

aDepartment of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, Beijing, P R China; bDepartment of Products Development, GuangZhou Zhongyi Pharmaceutical Company Ltd, Guangzhou, P R China

* Address correspondence to: Prof. Qun Wei, Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing, 100875, China. Tel/Fax: +86 10 5880 7365 E-mail: weiq{at}bnu.edu.cn

Received September 14, 2009; Accepted September 23, 2009


  Abstract

Calcineurin (CN), the Ca2+/calmodulin (CaM)-dependant protein phosphatase, is an integral enzyme involved in activation of T cells. It is also the target of various inhibitors such as cyclosporine A (CsA) and FK506 both of which have been widely used as immunosuppressants. We show that the novel CN inhibitor, quercetin (QC), associates with CN both in vitro and in Jurkat cells, and that it causes non-competitive inhibition of phosphatase activity. Unlike CsA and FK506, QC does not require a matchmaker protein for CN inhibition. It acts directly on the catalytic domain and its inhibitory effect was increased by the presence of CNB. Using semi quantitative and real-time RT-PCR, we show that QC inhibits IL-2 gene expression in activated Jurkat cells. The physiological inhibitory activity of QC together with its hypotoxicity suggest that it may be an effective immunosuppressant.

Key Words: Quercetin, Calcineurin, inhibitor, Jurkat cell, RT-PCR


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