Comparison of bipyridyl, maltol and kojic acid action as organic vanadium ligands on activity of galactosyltransferase (EC 2.4.1.38), some physiological parameters and ultrastructure of Golgi complexes in rat hepatocytes.

Abstract

The biochemical activity and morphology of control and streptozotocin-diabetic rat liver Golgi complexes were previously investigated by us under influence of some vanadium [V(IV)] compounds. The effectiveness of these derivatives depends on the kind of complexing ligands. This paper presents the investigation of the effect of bipyridyl, the ligand of a new vanadium compound, tested by us with maltol and kojic acid (two ligands studied by the present and other authors). The three ligands alone action was tested under the same experimental conditions as in the case of whole compounds with vanadium and applied to liver Golgi complexes of control rats. A preliminary study for maltol and kojic acid had been previously carried out by us parallel with tests of whole vanadium complexes, but valuable differences in biological action found in our condition of experiments suggested the extension of studies to include the two above-mentioned ligands and to compare the effects of the three investigated ligands. The supplementary part of the experiment focused mainly on the ultrastructure of Golgi complexes in hepatocytes. Four groups of animals were used: C - control rats, C + M (maltol), C + (ka)2 (kojic acid) and C + (bpy)2 (bipyridyl). The control rats received 0.09M NaCl as drinking liquid; all the other animals were given 3.6 mmol/L of appropriate ligand solution in 0.09M NaCl during 7 days. All the animals survived the experiments. Only in group C + (bpy)2 did the authors observe statistically significant differences as compared with the controls (group C). The differences were detected in physiological studies and manifested as body weight decreased by approximately 20% during the experiment, lower liquid (p<0.001) and food (p<0.01) intake and increase of free blood sugar level (p<0.01). The yield of Golgi membrane isolation decreased in this group (p<0.01). The main investigated biochemical parameter, i.e. the activity of liver Golgi marker enzyme - galactosyltransferase - was not statistically significantly changed in comparison with the controls in all the investigated groups of rats; a similar dispersion of individual results were found in the four groups. In the three experimental groups, ultrastructural observations demonstrated a predominance of cylindrical Golgi structures, which were haphazardly twisted in the majority of cases. Typically shaped structures were encountered sporadically. The ligands alone evoked numerous subcellular changes in hepatocytes; these alterations most frequently involved the mitochondria and endoplasmic reticulum. No such changes had been seen, or else they had been less advanced when complex vanadium compounds were employed in our earlier experiments. As it follows, the ligands alone were demonstrated to be much more toxic to morphology of control liver Golgi apparatus as compared to complex compounds, which showed the ability of the former to normalize Golgi complexes of diabetic animals.