Molecular interaction of acrylonitrile and potassium cyanide with rat blood.
The interaction of acrylonitrile (VCN) with rat blood has been investigated at the molecular level in an attempt to understand the possible mechanism of its toxicity. The results obtained were compared to those with potassium cyanide (KCN), a compound known to liberate cyanide (CN-) in biologic conditions. The radioactivity derived from K14CN was eliminated faster than that from [1-14C]VCN. Up to a maximum of 94% of 14C from VCN in erythrocytes was detected covalently bound to cytoplasmic and membrane proteins, whereas 90% of the radioactivity from KCN in erythrocytes was found in the heme fraction of hemoglobin. Determination of specific activity showed that binding occurred more in vivo than in vitro which indicated that the VCN molecule was bioactivated inside erythrocytes. These results indicate that KCN interacts mainly through CN- liberation and binding to heme, whereas VCN, which binds to cytoplasmic and membrane proteins, may cause damage to red cells by mechanisms other than release of CN-.
D000181:Acrylonitrile / Q000008:administration & dosage / Q000097:blood / Q000494:pharmacology*; D000284:Administration, Oral; D000818:Animals; D003486:Cyanides / Q000494:pharmacology*; D004912:Erythrocytes / Q000187:drug effects*; D006418:Heme / Q000032:analysis; D006454:Hemoglobins / Q000032:analysis; D008297:Male; D008565:Membrane Proteins / Q000097:blood; D009570:Nitriles / Q000494:pharmacology*; D011190:Potassium Cyanide / Q000097:blood / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013997:Time Factors
D003486:Cyanides; D006454:Hemoglobins; D008565:Membrane Proteins; D009570:Nitriles; D006418:Heme; D000181:Acrylonitrile; D011190:Potassium Cyanide