Biologically Active Polypeptides of Anemonia sulcata—and of Other Sea Anemones—Tools in the Study of Exitable Membranes

During the past thirty years sea anemones turned out to be important producer of biologically highly active polypeptides acting on Na+ and K+ ion channels. They are compoused from 27 to 59 aminoacids having molecular weights from 3000 to 7000 Da. All contain six cystein molecules which are interconnected to three sisulfide bridges. Because of their specifique mode of action on nerve cell exitation and on the mammalian heart muscle they became very important tools in neurophysiology and pharmacology. In the present review the research on sea anemone polypeptid toxins is summarized from a historical point of view, focussed on the polypeptides of Anemonia sulcata, Condylactis gigantea and Anthopleura elegantissima.