Methyl mercury-induced nonselective blocking of phosphorylation processes as a possible cause of protein synthesis inhibition in vitro and in vivo.
Inhibition of protein synthesis by methyl mercury occurring in a reticulocyte lysate cell-free translation system can be substantially reduced by addition of excess ATP and inorganic phosphate to the incubation medium. It was established in in vivo experiments that intraperitoneal (i.p.) administration of sodium orthophosphate buffer to a considerable degree prevents the development of certain biochemical effects exerted by an i.p. injection of 1/3 LD50 methyl mercury. Inhibition of protein and ATP synthesis as well as protein phosphorylation in mouse brain and liver tissue was much less severe in phosphate-pretreated animals. Administration of orthophosphate in the absence of poison does not alter the rate of the biochemical processes studied. Orthophosphate proved to be less effective in correcting already induced metabolic disorders than in preventing the development of such disorders.
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D066298:In Vitro Techniques; D008297:Male; D008767:Methylmercury Compounds / Q000633:toxicity*; D051379:Mice; D010710:Phosphates / Q000494:pharmacology; D010766:Phosphorylation; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism
D008767:Methylmercury Compounds; D010710:Phosphates; D012346:RNA, Transfer, Amino Acyl; D000255:Adenosine Triphosphate