Planta Med 2012; 78(10): 957-961
DOI: 10.1055/s-0031-1298538
Biological and Pharmacological Activity
Original Papers
Georg Thieme Verlag KG Stuttgart · New York

Inhibition of Lysenin-induced Hemolysis by All-E-Lutein Derived from the Plant Dalbergia latifolia

Authors

  • Yuki Niwa

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
  • Chino Matsui

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
  • Neelanun Sukumwang

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
  • Hironobu Iinuma

    2   Bioscience Associates, Tokyo, Japan
  • Yoko Ikeda

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
  • Takashi Koyano

    3   Temko Corporation, Tokyo, Japan
  • Taworn Kovitayakorn

    4   Faculty of Agriculture, Khon Kaen University, Khon Kaen, Thailand
  • Siro Simizu

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
  • Kazuo Umezawa

    1   Faculty of Science and Technology, Keio University, Kanagawa, Japan
Further Information

Publication History

received 15 November 2011
revised 08 April 2012

accepted 11 April 2012

Publication Date:
15 May 2012 (online)

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Abstract

Lysenin is a pore-forming toxin derived from coelomic fluid of the earthworm Eisenia foetida. The model of lysenin-induced hemolysis includes the specific binding of lysenin to sphingomyelin, oligomerization of the pore proteins, and pore formation. Although the mechanism of lysenin-induced hemolysis is unique, its precise mechanism of action and its inhibitors are poorly understood. In the present study, we screened for inhibitors of lysenin-induced hemolysis by using an optimized screening system and found a methanolic extract of Dalbergia latifolia leaves to be a potential candidate. After isolation and identification, all-E-lutein was identified as the hemolysis inhibitor with an effective dose of 0.025–2.5 ng/mL without any toxicity. The inhibition by all-E-lutein is likely to occur during the receptor binding and/or pore-forming protein oligomerization.

Supporting Information