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© 1993 Medical Council on Alcohol

research-article

EVIDENCE FOR THE COVALENT BINDING OF HYDROXYETHYL RADICALS TO RAT LIVER MICROSOMAL PROTEINS

EMANUELE ALBANO, MAURIZIO PAROLA, ADRIANA COMOGLIO and MARIO U. DIANZANI

Department of Experimental Medicine and Oncology, University of Turin Corso Raffaello 30, 10125 Torino, Italy

Received 25 October 1992; first review notified 5 January 1993; accepted 29 January 1993

It is well known that acetaldehyde is capable of covalent binding to liver proteins. However, in experiments using liver rnicrosomes prepared from chronically ethanol-fed rats we have observed that the addition of EDTA-iron complex to the microsomes increases by about 4–5 fold both the spin trapping of hydroxyethyl radicals and the covalent binding of 14C-ethanol to proteins, while it only doubles acetaldehyde formation. Conversely, the presence of GSH strongly decreases the trapping of hydroxyethyl radicals and completely inhibits the covalent binding, without affecting acetaldehyde production. Furthermore, the spin trapping agent 4-pyridyl-N-oxide-t-butyl nitrone (4-POBN), previously employed for the detection of hydroxy-ethyl radicals, decreases by about 70% the covalent binding of 14C-ethanol to microsomal proteins. 4-POBN does not affect acetaldehyde production by liver microsomes, nor does it interefere with the covalent binding of acetaldehyde produced by ADH-mediated oxidation of ethanol. The results obtained indicate that hydroxyethyl radicals generated during ethanol oxidation by cytochrome P-450 play an important role in the alkylation of microsomal proteins consequent to ethanol metabolism.


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