Inhibition of protein synthesis in liver and kidney of mice by bolesatine: mechanistic approaches to the mode of action at the molecular level.
Protein synthesis was assayed in liver and kidney of mice treated with bolesatine, a toxic glycoprotein from the mushroom Boletus satanas (Lenz) which was previously shown to be an inhibitor of protein synthesis by cell-free systems in vitro and by cultured cell-lines. Protein synthesis in vivo (Swiss mice) is inhibited in a dose-dependent manner in liver and kidney. The mechanism of action does not appear to be due to RNA-N-glycosidase activity of bolesatine or a RNAase activity of this toxin on the ribosomal RNAs. Ribosomes do not appear to be damaged by pretreatment with bolesatine as judged by a poly(U) translation system. Thus bolesatine cannot be included in the group of protein synthesis inhibitors of plant origin known as ribosome-inactivating proteins (RIPs).
Kretz
O
O
Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Strasbourg, France.
Barbieri
L
L
Creppy
E E
EE
Dirheimer
G
G
D000818:Animals; D005656:Fungal Proteins / Q000633:toxicity*; D006026:Glycoside Hydrolases / Q000378:metabolism; D007668:Kidney / Q000187:drug effects* / Q000378:metabolism; D007930:Leucine / Q000378:metabolism; D008099:Liver / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D008297:Male; D051379:Mice; D009183:Mycotoxins; D010649:Phenylalanine / Q000378:metabolism; D014176:Protein Biosynthesis
D005656:Fungal Proteins; D009183:Mycotoxins; C060924:Bolesatine protein, Boletus satanas; D010649:Phenylalanine; D006026:Glycoside Hydrolases; D007930:Leucine