Widespread occurrence in frogs and toads of skin compounds interacting with the ouabain site of Na+, K+-ATPase.
Amphibians of the family Bufonidae contain high levels of skin compounds that both inhibit Na+- and K+-dependent adenosinetriphosphatase and antagonize the binding of ouabain to the enzyme. In species of Bufo and Atelopus, these compounds are relatively nonpolar bufodienolides, whereas Dendrophryniscus and Melanophryniscus contain more polar compounds of unknown structure. Skin extracts from 30 of 48 species of frogs representing an additional eight families contained relatively low levels of compounds that inhibit binding of ouabain to Na+,K+-adenosinetriphosphatase. The widespread occurrence of low levels of inhibitory compounds is consonant with the role for these compounds as physiological regulators of Na+,K+-adenosinetriphosphatase in amphibian skin; high levels in the Bufonidae probably also serve as a defense against some predators.[1]References
- Widespread occurrence in frogs and toads of skin compounds interacting with the ouabain site of Na+, K+-ATPase. Flier, J., Edwards, M.W., Daly, J.W., Myers, C.W. Science (1980) [Pubmed]
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