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Monoclonal antibodies that could not bind native tetramers of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) but could bind to dimeric, monomeric, or denatured forms of GAPDH were used to investigate its intracellular localization. These antibodies distinctly stained the nucleus in growing HeLa cells. In the cytoplasm, non-native GAPDH was colocalized with actin filaments. Incubation of HeLa cells with tumor necrosis factor α (TNF-α) and the protein synthesis inhibitor emetine led to a drastic increase in the amount of the non-native GAPDH in the nuclei. Overproduction of Bcl-2 protein did not change the non-native GAPDH localization in the growing HeLa cells but prevented the development of apoptosis and the increase in the amount of non-native GAPDH in the nuclei upon incubation with TNF-α. [ABSTRACT FROM AUTHOR]