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Irreversible protein binding of acrylonitrile
Xenobiotica; the Fate of Foreign Compounds in Biological Systems
|January 1, 1981
Summary
Acrylonitrile irreversibly binds to rat proteins, particularly in the liver. This non-enzymatic binding in microsomes is inhibited by thiols like cysteine and glutathione.
Area of Science:
- Toxicology
- Biochemistry
- Chemical carcinogenesis
Background:
- Acrylonitrile is an industrial chemical with potential toxicological effects.
- Understanding the metabolic fate and protein binding of acrylonitrile is crucial for risk assessment.
Purpose of the Study:
- To investigate the in vivo and in vitro irreversible binding of acrylonitrile to proteins.
- To elucidate the mechanism of acrylonitrile-protein adduct formation.
Main Methods:
- Rats were injected with radiolabeled acrylonitrile ([2,3-14C]acrylonitrile).
- Rat liver microsomes were incubated with [2,3-14C]acrylonitrile in vitro.
- Binding inhibition studies were performed using various thiol compounds.
Main Results:
- Significant radioactivity from acrylonitrile was found bound to proteins in multiple rat tissues.
- Acrylonitrile demonstrated time-dependent, non-enzymatic irreversible binding to rat liver microsomal proteins.
- Thiol compounds, notably dithiocarbamate, significantly inhibited acrylonitrile binding.
Conclusions:
- Acrylonitrile can form irreversible adducts with proteins in vivo and in vitro.
- The binding process is not dependent on enzymatic metabolism.
- Thiols play a role in mitigating acrylonitrile-protein binding.