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The somatic isoform of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC1.2.1.12)  is involved in such crucial for cancer cells development pathways as induction of apoptosis and glycolytic regulation.  At the same time, sperm-specific isoform (GAPDHS) does not exhibit all the same functions as somatic enzyme.  The expression of sperm-specific GAPDH without N-terminal domain in some melanoma cells along with somatic  isoenzyme, shown in our previous work, has led to the proposal of this unusual enzyme's possible role in regulation  of cancer cells glycolysis. In the presented work we have tested production of GAPDHS in 13 additional melanoma  cell lines by immunoblotting. We have also gathered data on energy metabolism in 5 selected cell lines by evaluation  of glucose uptake and lactate production in differing conditions. We have demonstrated that in standard cultivation  media glucose uptake by MelP cells, producing substantial amounts of GAPDHS protein was higher than  in MelKor cells, producing lesser amounts of GAPDHS. All other analyzed cell lines that do not produce GAPDHS  (MelMS, MelSi and Malme3M) had even a lower glucose uptake rate.

Expression of sperm-specific glyceraldehyde-3-phosphate dehydrogenase in melanoma cells changes their energy metabolism