L3038
Lysenin from Eisenia foetida
solid
Sinónimos:
Eisenia Lysenin, Lysenin Protein
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About This Item
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General description
Lysenin is a superfamily of certain proteins including lysenin-related protein 1 (LRP-1, lysenin 2) and LRP-2 (lysenin 3).
Application
Lysenin from Eisenia foetida has been used to treat B cells and study lysenin′s effect on membrane diacylglycerol (DAG) and surface sphingomyelin (SM).
Biochem/physiol Actions
Lysenin is a 33kDa protein present in the coelomic fluid of the earthworm Eisenia foetida. It interacts with sphingomyelin in cell membranes. In vertebrates, this binding results in cytotoxicity and contraction of smooth muscle in vitro as well as vasodepressor activity and lethality under in vivo conditions.
Lysenin serves as a tool to explore membrane lipid organization. It is known to induce hemolysis in vertebrates and mammalian cells.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Reiko Ishitsuka et al.
Anatomical science international, 79(4), 184-190 (2005-01-07)
Sphingomyelin is a major sphingolipid species in animal cells and is a major lipid constituent of plasma membranes. Recent reports have established important roles for sphingomyelin and its metabolites as second messengers in signal transduction events during development and differentiation.
Hideshi Kobayashi et al.
International review of cytology, 236, 45-99 (2004-07-21)
Lysenin is a protein of 33?kDa in the coelomic fluid (CF) of the earthworm Eisenia foetida. It differs from other biologically active proteins, such as fetidins, eiseniapore, and coelomic cytolytic factor (CCF-1), that have been found in Eisenia foetida, in
Peiqi Ou et al.
Cell reports, 36(9), 109624-109624 (2021-09-02)
B cell tolerance prevents autoimmunity by deleting or deactivating autoreactive B cells that otherwise may cause autoantibody-driven disorders, including systemic lupus erythematosus (lupus). Lupus is characterized by immunoglobulin Gs carrying a double-stranded (ds)-DNA autospecificity derived mainly from somatic hypermutation in
A Yamaji et al.
The Journal of biological chemistry, 273(9), 5300-5306 (1998-03-28)
Lysenin, a novel 41-kDa protein purified from coelomic fluid of the earthworm Eisenia foetida, induced erythrocyte lysis. Preincubation of lysenin with vesicles containing sphingomyelin inhibited lysenin-induced hemolysis completely, whereas vesicles containing phospholipids other than sphingomyelin showed no inhibitory activity, suggesting
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