title: Peptide toxins in sea anemones: structural and functional aspects.
abstract: Sea anemones are a rich source of two classes of peptide toxins, sodium channel toxins and potassium channel toxins, which have been or will be useful tools for studying the structure and function of specific ion channels. Most of the known sodium channel toxins delay channel inactivation by binding to the receptor site 3 and most of the known potassium channel toxins selectively inhibit Kv1 channels. The following peptide toxins are functionally unique among the known sodium or potassium channel toxins: APETx2, which inhibits acid-sensing ion channels in sensory neurons; BDS-I and II, which show selectivity for Kv3.4 channels and APETx1, which inhibits human ether-a-go-go-related gene potassium channels. In addition, structurally novel peptide toxins, such as an epidermal growth factor (EGF)-like toxin (gigantoxin I), have also been isolated from some sea anemones although their functions remain to be clarified.
authors.affiliation: Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Konan-4, Minato-ku, Tokyo, 108-8477, Japan.
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Honma
authors.forename: Kazuo
authors.initials: K
authors.lastname: Shiomi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004815:Epidermal Growth Factor / Q000737:chemistry; D007473:Ion Channels / Q000187:drug effects*; D008322:Mammals; D008387:Marine Toxins / Q000737:chemistry* / Q000145:classification / Q000494:pharmacology*; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000187:drug effects; D012615:Sea Anemones / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment / Q000662:veterinary; D017386:Sequence Homology, Amino Acid; D015222:Sodium Channels / Q000187:drug effects; D013329:Structure-Activity Relationship
chemical_list: D007473:Ion Channels; D008387:Marine Toxins; D015221:Potassium Channels; D015222:Sodium Channels; D004815:Epidermal Growth Factor