title: Biology of lysenin, a protein in the coelomic fluid of the earthworm Eisenia foetida.
abstract: 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 terms of both its biochemical and its biological characteristics. The large coelomocytes and free chloragocytes in the typhlosole of Eisenia foetida appear to be the cells that produce lysenin since the mRNA for lysenin and immunoreactive lysenin have been found in these cells. Lysenin binds specifically to sphingomyelin (SM) but not to other phospholipids in cell membranes. After binding to the cell membranes of target cells, lysenin forms oligomers in an SM-dependent manner, with subsequent formation of pores with a hydrodynamic diameter of approximately 3?nm. The biochemical interactions between lysenin and SM in cell membranes are responsible for the pharmacological activities of lysenin and of CF that contains lysenin in vertebrates, such as hemolysis, cytotoxicity, and contraction of smooth muscle in vitro and vasodepressor activity and lethality in vivo. When incubated with SM-liposomes, CF and lysenin lost some or all of their activity, an observation that suggests that SM might be involved in the induction of the various activities of lysenin and CF. However, in general, lysenin is neither cytotoxic nor lethal to invertebrates. An attempt has been made to explain the differences in the responses to lysenin and CF between vertebrates and invertebrates in terms of the presence or absence of SM in the various animals. Among Protostomia, SM is absent in Lophotrochozoa, with the exception of some molluscan species, but it is present in Ecdysozoa, with the exception of Nematomorpha and flies. Among Deuterostomia, Echinodermata and Hemichordata lack SM but SM is found in Chordata. Thus, the difference in terms of the response to lysenin between invertebrates and vertebrates cannot be fully explained by reference to the presence or absence of SM in the organism. Lysenin and its antiserum have made it possible to localize SM in the cell membranes. They should be a useful tool for studies of membrane physiology and the role of SM.
authors.affiliation: Research Laboratory, Zenyaku Kogyo Co., Ltd., Nerima-ku, Tokyo 178-0062, Japan.
authors.forename: Hideshi
authors.initials: H
authors.lastname: Kobayashi
authors.forename: Naoshi
authors.initials: N
authors.lastname: Ohta
authors.forename: Masato
authors.initials: M
authors.lastname: Umeda
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D009835:Oligochaeta / Q000033:anatomy & histology / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D016415:Sequence Alignment; D013109:Sphingomyelins / Q000737:chemistry / Q000378:metabolism; D014118:Toxins, Biological
chemical_list: D000900:Anti-Bacterial Agents; D008081:Liposomes; D011506:Proteins; D013109:Sphingomyelins; D014118:Toxins, Biological; C107040:lysenin