The glycation of liver histones was studied in rats with streptozotocin-ind
uced diabetes, in ethanol (EtOH)-treated rats, and in EtOH-treated diabetic
rats. In diabetes, the conditions of glucose-protein addition are more fav
ourable extracellularly in serum and in erythrocytes than in the nucleus. T
his is indicated by the increased level of serum fructosamine and by the hi
gh level of glycated haemoglobin, while the glycation of intracellular hist
one is decreased. In the serum of diabetic rats, we found a relatively high
acetaldehyde level, which resulted in elevated histone fluorescence. Fluor
escence is an accepted marker of advanced glycation end-product (AGE), the
intensity of which, according to our experiments is related not to the leve
l of serum glucose, but to the level of acetaldehyde. The data obtained wit
h histone proteins in diabetic rats treated with EtOH are in good agreement
with the results of our earlier in vitro experimental results obtained wit
h H1 histone: the reaction of the two aldehydes (glucose and acetaldehyde)
in combination gives a lower glycohistone value than they do separately.