Thionins: Plant Peptides that Modify Membrane Permeability in Cultured Mammalian Cells
Open Access
- 1 May 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 116 (1), 185-189
- https://doi.org/10.1111/j.1432-1033.1981.tb05317.x
Abstract
Thionins, which are toxic high-S polypeptides present in the endosperm of wheat [Triticum aestivum] and related species, prevent growth and inhibit macromolecular synthesis in cultured mammalian cells. Baby hamster kidney BHK-21 (BHK) cells were markedly more sensitive to thionins than the other cell lines tested (monkey kidney CV1, mouse fibroblast L, human cervical carcinoma HeLa). A thionin concentration of 5 .mu.g/ml (1 .mu.M) completely blocked translation in BHK cells. Omission of both Ca and Mg ions fromthe medium strongly enhanced the inhibitory effects of thionins (BHK cells, 80% inhibition, 0.5 .mu.g/ml). Thionins may act at the membrane level. Both the 86Rb+ content and the nucleotide pool of BHK cells were drastically decreased at thionin concentrations that inhibited translation. Thionin concentrations that did not affect macromolecular synthesis in these cells, allowed inhibition of translation by antibiotics, such as hygromycin B, that are not able to cross the cell plasma membrane by themselves. The inhibition of protein, RNA and DNA synthesis in BHK cells may be a consequence of membrane leakiness induced by thionin treatment. Parallelism was found between 86Rb+ leakage and inhibition of protein synthesis by treatment with different genetic variants of thionins (.alpha.1 purothionin, .alpha.2 purothionin, .beta. purothionin from wheat; hordothionin from barley), as well as with the viscotoxins, which are homologous polypeptides from the European mistletoe [Viscum album].This publication has 19 references indexed in Scilit:
- Action of Membrane-Active Compounds on Mammalian Cells. Permeabilization of Human Cells by Ionophores to Inhibitors of Translation and TranscriptionEuropean Journal of Biochemistry, 1980
- Toxicity of purothionin and its homologues to the tobacco hornworm, Manduca sexta (L.) (lepidoptera: sphingidae)Toxicology and Applied Pharmacology, 1979
- Physico‐chemical Basis of Ion Transport through Biological Membranes: Ionophores and Ion ChannelsEuropean Journal of Biochemistry, 1979
- Identification and purification of a purothionin homolog from rye (Secale cereale L.)Journal of Agricultural and Food Chemistry, 1978
- Reconstitution of petroleum ether soluble wheat lipopurothionin by binding of digalactosyl diglyceride to the chloroform-soluble formJournal of Agricultural and Food Chemistry, 1977
- Antibiotics and Membrane BiologyAnnual Review of Biophysics and Bioengineering, 1975
- The amino acid sequence of purothionin A, a lethal toxic protein for brewer's yeasts from wheat.Agricultural and Biological Chemistry, 1975
- The Mode of Action of Toxic Protein in Wheat and Barley on Brewing YeastAgricultural and Biological Chemistry, 1973
- Purothionins inAegilops-Triticum spp.Cellular and Molecular Life Sciences, 1969
- Purothionin analogues from barley flourJournal of the Science of Food and Agriculture, 1969