Chemical Research in Chinese Universities ›› 2009, Vol. 25 ›› Issue (6): 895-898.

• Articles • Previous Articles     Next Articles

Inhibition of Matrix Metalloproteinases Activities by Luteolin

JI Hai-tao1,2, SHI Xiu-juan1,2, HONG Yuan1,2, WANG Ye1,2, WANG Hui-ling1,2, WANG Zhi-yong1,2 and FANG Xue-xun2*   

  1. 1. College of Life Science,
    2. Key Laboratory of Molecular Enzymology and Enzyme Engineering of Ministry of Education, Jilin University, Changchun 130021, P. R. China
  • Received:2008-11-21 Revised:2009-03-09 Online:2009-11-25 Published:2010-01-25
  • Contact: FANG Xue-xun. E-mail: fangxx@jlu.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(No.30371656) and New Century Excellent Talent of Ministry of Education, China(No.NCET-08-0244).

Abstract:

Matrix metalloproteinases(MMPs) are a family of zinc dependent enzymes that can degrade the components of the extracellular matrix(ECM) and basement membranes. Because MMPs play roles in many important physiological and pathological processes, many MMP inhibitors(MMPIs) have been developed with the aim of interfe- ring in and treating diseases. The authors conclude via a fluorescence based assay in vitro that luteolin inhibits the enzymatic activities of MMP-2, MMP-7, MMP-9, MMP-14, and MMP-16. This compound most specifically inhibits MMP-7 of all the  MMPs tested. Finally, we used molecular modeling to dock luteolin with MMPs and revealed the binding mode of the luteolin-MMP interaction. Our results suggest that luteolin may exert its therapeutic effects via MMP inhibition.

Key words: Matrix metalloproteinase(MMP); MMP inhibitor(MMPI); Natural product; Luteolin