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Background:The current study was directed to determine the values of both GM3 ganglioside and specific anti-GM3 antibodies in in vitro-incubated normal cells, malignant cell and mixed cultures of co-cultivated cells from both types as well. So a better understanding of the molecular mechanisms, underlining differences between various cellular types and changes during the process of cell differentiation was necessary.Methods:Total lysates from cultivated normal cells from mouse embryos, mouse malignant myeloma line and mixed of both were prepared and passed through GSH-Agarose Columns. Molecules with affinity to the reduced form of Glutathione (GSH) were separated. The levels of ganglioside GM3 and of specific antibodies to it were assessed by enzyme-linked immuno-sorbent assay (ELISA) technique. Results:In the normal cells' lysate, supplemented with molecules, possessing affinity to GSH the lowest values were assessed. These differences could be due to contention of many non-possessing such affinity molecules in equal volume of biological material, as well as with the presence of various bonded forms of GM3. Conclusions:The data obtained confirm literature data about the increased levels of GM3 as a marker for malignancy. We propose derivation of lymphoid-like cells from the embryonic progenitors. Another hypothesis could be the production of immunoglobulins (IgG antibodies) from non-lymphoid cells in appropriate conditions.

There is the main agreement that proteins are key targets for heavy metals. Apart from the oxidative stress (OS) pathway, the harmful effects of heavy metal ions are also represented by different modes of interaction with protein molecules. For example, by changing the functions of proteins (such as displacement of the main metal ions in enzymes and metalloproteins/MT, or oxidation of amino acids in side residues of peptide molecules), including their attachment to free functional groups (thiol, carboxyl or other groups). In addition, heavy metals can interfere with the synthesis and spatial structuring of forming proteins (by inhibiting the processes of protein folding or refolding upon transfer through cell membranes, or denaturation), causing aggregation of nascent proteins in living cells. The current review aims to discuss some of the possible biochemical and physiological mechanisms related to the protein/enzyme structure and functional activity through which metals influence or contribute to the disruption of male reproductive processes.

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