Lysenin, a Novel Bioactive Protein Isolated from Coelomic Fluid of the Earthworm Eisenia foetida - Structure, Secretion and Biological Activity

Kobayashi, Hideshi; Sekizawa, Yoshiyuki; Shioda, Seiji; Natori, Shunji; Nakajima, Terumi; Umeda, Masato

doi:10.1007/978-3-642-60915-2_19

Cited by 5 publications

(4 citation statements)

References 26 publications

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“…Previously it was shown that lysenin causes lysis of erythrocytes from various animal species (12,25). The sensitivity to lysenin that differed among species and sheep erythrocytes were the most sensitive.…”

Section: Lysenin Forms 3-nm Diameter Pores In Target Membranes-mentioning

confidence: 99%

Oligomerization and Pore Formation of a Sphingomyelin-specific Toxin, Lysenin

Yamaji‐Hasegawa

Makino

Baba

et al. 2003

Journal of Biological Chemistry

121

146

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Lysenin is a novel protein derived from coelomic fluid of the earthworm Eisenia foetida, which specifically recognizes sphingomyelin and induces cytolysis. The mechanism underlying lysenin-induced cell lysis has not been clarified. In this report we studied the interaction of lysenin with red blood cells as well as artificial liposomes. Our results showed that lysenin bound membranes and assembled to SDS-resistant oligomers in a sphingomyelin-dependent manner, leading to the formation of pores with a hydrodynamic diameter of ϳ3 nm. Antibody scanning analysis suggested that the Cterminal region of lysenin was exposed, whereas the N-terminal was hidden in the isolated oligomer complex. Differential scanning calorimetry revealed that lysenin interacted with both hydrophilic head group and hydrophobic hydrocarbon tails of sphingomyelin. Oligomerization but not binding was affected by the amide-linked fatty acid composition of sphingomyelin, suggesting the role of membrane fluidity in the oligomerization step.

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Section: Lysenin Forms 3-nm Diameter Pores In Target Membranes-mentioning

confidence: 99%

Oligomerization and Pore Formation of a Sphingomyelin-specific Toxin, Lysenin

Yamaji‐Hasegawa

Makino

Baba

et al. 2003

Journal of Biological Chemistry

121

146

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“…This period starts around the end of the exfoliation period (stage 34), suggesting that the exfoliation and the defecation induced by CF and lysenin might be independent phenomena. During the food-intake period, CF and lysenin might reach and stimulate the larval intestine, with resultant defecation, since it is known that CF and lysenin induce contraction of smooth muscles in some other tissues (13).…”

Section: Comparison Of the Exfoliative Activities Of Cf And Lyseninmentioning

confidence: 99%

“…Lysenin is a novel bioactive 33-kDa protein which we isolated from the coelomic fluid (CF) of the earthworm Eisenia foetida and it does not contain any amino acid sequences homologous to those of proteins in standard databases (13,23,24). This protein binds specifically to sphingomyelin (SM) among the various phospholipids found in the cell membrane (29).…”

mentioning

confidence: 99%

Exfoliation of the Epidermal cells and Defecation by Amphibian Larvae in Response to Coelomic Fluid and Lysenin from the Earthworm Eisenia foetida

2006

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Coelomic fluid (CF) and lysenin from the earthworm Eisenia foetida induced heavy epidermal exfoliation in the larvae of Bufo japonicus formosus at developmental stages from hatching (stage 22) to operculum completion (stage 34). In experiments with Xenopus laevis, we observed that exfoliated cells were not stained by trypan blue. Thus, it appeared that these cells were still alive. It is likely, therefore, that both CF and lysenin might disrupt the adhesion between epidermal cells of larvae prior to stage 34. Since it is known that lysenin exerts its toxic effects through its specific binding to sphingomyelin (SM), SM might be involved in such adhesion. This hypothesis was supported by the observations that CF and lysenin which had been incubated with SM-liposomes lost their exfoliative activity. In larvae after stage 34, the mechanism of adhesion between epidermal cells seemed to change and the adhesion was no longer disrupted by CF and lysenin. In larvae at around stage 34, a collagen layer started to form beneath the basement membrane of the epidermis. Furthermore, larvae at around this stage started to eat solid food. The developing collagen layer and food intake might be related indirectly to the chemical change in epidermal adhesion. The induction of exfoliation by CF and lysenin was also observed in other amphibian species. In Bufo larvae, defecation was induced both by CF and by lysenin but this effect was independent of exfoliation.

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“…We isolated a novel protein of 297 amino acids with a molecular mass of 33 kDa from the CF of the same species. This protein induced the contraction of smooth muscle and was named lysenin (Sekizawa et al 1996aKobayashi et al 1997). Lysenin differs from the other proteins mentioned above in terms of both amino acid sequence and biological activity.…”

Section: Introductionmentioning

confidence: 97%

Sites of expression of mRNA for lysenin, a protein isolated from the coelomic fluid of the earthworm Eisenia foetida

Ohta

Shioda

Sekizawa

et al. 2000

Cell and Tissue Research

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Lysenin is a 33-kDa protein of 297 amino acids that was originally purified from the coelomic fluid of the earthworm Eisenia foetida. It binds specifically to sphingomyelin. In this study, we attempted to identify the site of synthesis of lysenin in the earthworm. We detected the expression of mRNA for lysenin and the presence of immunoreactive lysenin in the large coelomocytes and in the free large chloragocytes present in the lumen of the typhlosole, a depression in the dorsal wall of the intestine. These coelomocytes and chloragocytes seemed to be mature and separate from the chloragogen tissue that lined the typhlosole. The free large chloragocytes in the typhlosole contained numerous vacuoles. The nuclei were small and irregular in shape, and glycogen granules and mitochondria were occasionally found between vacuoles. The chloragocytes of the chloragogen tissue that surrounded the coelomic side of the intestine and the dorsal blood vessel did not react with the lysenin antiserum and no expression of lysenin mRNA was detected in these cells. Furthermore, no evidence of the protein or of the mRNA was found in the cells of the pharyngeal gland. Our findings suggest that lysenin is produced in the free large chloragocytes in the lumen of the typhlosole.

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Lysenin, a Novel Bioactive Protein Isolated from Coelomic Fluid of the Earthworm Eisenia foetida - Structure, Secretion and Biological Activity

Cited by 5 publications

References 26 publications

Oligomerization and Pore Formation of a Sphingomyelin-specific Toxin, Lysenin

Oligomerization and Pore Formation of a Sphingomyelin-specific Toxin, Lysenin

Exfoliation of the Epidermal cells and Defecation by Amphibian Larvae in Response to Coelomic Fluid and Lysenin from the Earthworm Eisenia foetida

Sites of expression of mRNA for lysenin, a protein isolated from the coelomic fluid of the earthworm Eisenia foetida

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