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1

Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Kanagawa 223-8522, Japan

2

Department of Molecular Target Screening, School of Medicine, Aichi Medical University Nagakute, Aichi 481-1195, Japan





*

Author to whom correspondence should be addressed.



Abstract Lysenin is a pore-forming toxin from the coelomic fluid of earthworm Eisenia foetida. This protein specifically binds to sphingomyelin and induces erythrocyte lysis. Lysenin consists of 297 amino acids with a molecular weight of 41 kDa. We screened for cellular signal transduction inhibitors of low molecular weight from microorganisms and plants. The purpose of the screening was to study the mechanism of diseases using the obtained inhibitors and to develop new chemotherapeutic agents acting in the new mechanism. Therefore, our aim was to screen for inhibitors of Lysenin-induced hemolysis from plant extracts and microbial culture filtrates. As a result, we isolated all-E-lutein from an extract of Dalbergia latifolia leaves. All-E-lutein is likely to inhibit the process of Lysenin-membrane binding and-or oligomer formation rather than pore formation. Additionally, we isolated tyrosylproline anhydride from the culture filtrate of Streptomyces as an inhibitor of Lysenin-induced hemolysis. View Full-Text

Keywords: Lysenin; Eisenia foetida; hemolysis; pore formation; sphingomyelin binding; Dalbergia latifolia; all-E-lutein; tyrosylproline anhydride Lysenin; Eisenia foetida; hemolysis; pore formation; sphingomyelin binding; Dalbergia latifolia; all-E-lutein; tyrosylproline anhydride





Autor: Neelanun Sukumwang 1 and Kazuo Umezawa 2,*

Fuente: http://mdpi.com/



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