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Keywords = tyrosylproline anhydride

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10 pages, 917 KiB  
Review
Earthworm-Derived Pore-Forming Toxin Lysenin and Screening of Its Inhibitors
by Neelanun Sukumwang and Kazuo Umezawa
Toxins 2013, 5(8), 1392-1401; https://doi.org/10.3390/toxins5081392 - 8 Aug 2013
Cited by 17 | Viewed by 9846
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Pore-Forming Toxins)
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