Background/aim: The aim of this study was to investigate the state of chromatin condensation in peripheral blood leukocytes of alcoholics, during the early detoxification period, in order to highlight structural modifications, indicating epigenetic mechanisms regulated by alcohol.
Materials And Methods: Blood samples were obtained from alcoholic patients, who were admitted for detoxification on an inpatient basis, and from healthy controls. The level of condensed heterochromatin and de-condensed euchromatin were detected through the ratio of lysine to arginine residues, by the application of the ammoniacal silver reaction (ASR) staining on leukocyte pellets, and through immunohistochemical localization of histone H1 on peripheral blood smears.
Our previous histochemical and ultrastructural studies have identified, in human catecholamine neurons, abundant spherical acidophilic protein bodies (pb), which originate from regular mitochondria, retaining their double membrane. In locus coeruleus (LC) neurons, pb have somatodendritic distribution and are unequivocal storage vesicles for noradrenaline, as demonstrated by immunolocalization of Dopamine-β-Hydroxylase. In the present study, in order to reinforce the identity of pb as monoamine storage sites in human LC, and to assess their potential of somatodendritic release, we studied the subcellular immunolocalization of chromogranin A (CgA) and vesicular monoamine transporter 2 (VMAT2), given the fact that their localization defines the vesicles capacity of filling with monoamine and hence exocytotic release.
View Article and Find Full Text PDFStudies of peripheral blood leukocytes of schizophrenic patients have shown in electron microscopy (EM) that decondensation of the chromatin constitutes a biological marker indicating increased genomic expression. Since this increase depends on chromatin relaxation by dissociation of lysine-rich histone H1 from nucleosomes, with exposure of arginine residues of core histones, the ratio of arginine to lysine residues in each nucleus represents a reliable measure of activation. Lysine- and arginine-rich proteins are demonstrable in light microscopy (LM), differentially, as yellow and black, respectively, with the ammoniacal silver reaction (ASR).
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