Prevention of toxic effects of ochratoxin A, a natural contaminant of mouldy food and feed: effects of A 19 (structural analogue of phenylalanine), on the nephrotoxicity in rats and on the inhibition of protein synthesis in Vero cells

Toxicon ◽  
1995 ◽  
Vol 33 (9) ◽  
pp. 1119
Author(s):  
I. Baudrimont ◽  
A.M. Betbeder ◽  
E.E. Creppy
Keyword(s):  
Protein Synthesis ◽  
Ochratoxin A ◽  
Vero Cells ◽  
Toxic Effects ◽  
Structural Analogue ◽  
Inhibition Of Protein Synthesis ◽  
Food And Feed

Inhibition of protein synthesis in Streptococcus faecalis by ochratoxin A

1978 ◽  
Vol 24 (4) ◽  
pp. 466-472 ◽  
Author(s):  
K. Heller ◽  
R. Röschenthaler
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Ochratoxin A ◽  
Rna Synthesis ◽  
Competitive Inhibition ◽  
Preliminary Evidence ◽  
Streptococcus Faecalis ◽  
Rna And Protein Synthesis ◽  
Inhibition Of Protein Synthesis ◽  
Camp Stimulation

A non-competitive inhibition of binding of cAMP to bovine protein kinase by ochratoxin A (OTA) is shown. Preliminary evidence of a protein kinase in Streptococcus faecalis is presented. The cAMP stimulation of this kinase is also inhibited by OTA. At the lowest OTA concentrations, RNA and protein synthesis are inhibited in S. faecalis. The inhibition of RNA synthesis is secondary, as in the presence of chloramphenicol no inhibition occurs for 10 min after the addition of OTA. The synthesis but not the induction of β-P-galactosidase is inhibited by OTA. The polysomes of S. faecalis are stablized after addition of OTA, showing an inhibition of peptide elongation. The mode of action of OTA in bacteria is discussed and it is concluded that inhibition of protein synthesis is the process which might be closest to the primary target of OTA.

Sign in / Sign up

Export Citation Format

Share Document