Skip to Content
Merck
CN

Nuclear localization of aldolase A correlates with cell proliferation.

Biochimica et biophysica acta (2013-07-28)
Piotr Mamczur, Andrzej Gamian, Jerzy Kolodziej, Piotr Dziegiel, Dariusz Rakus
ABSTRACT

Muscle fructose 1,6-bisphosphate aldolase (ALDA) is a glycolytic enzyme which may localize both in nuclei and cytoplasm of cells, however its role in the nuclei is unclear. Here, we demonstrate the links between subcellular localization of ALDA and the cell cycle progression as well as the availability of energetic substrates. Results of our studies indicate that nuclear localization of ALDA correlates with the proliferative activity of the cells and with the expression of Ki-67, a marker of proliferation, both in the KLN-205 (mouse lung cancer cells) and human squamous cell lung cancer cells (hSCC). Chemically-induced block of cell cycle entry in S phase and the inhibition of transcription stimulate removal of ALDA from cells nuclei suggesting that nuclear ALDA is involved in cells proliferation. On the other hand, subcellular distribution of the enzyme also depends on the stress and pro-survival signals mediated by the Akt and the p38 pathways and, in non-proliferating cells, on the availability of glucose and lactate. The results presented here point to ALDA as a factor involved in the regulation of cells proliferation.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Concanavalin A from Canavalia ensiformis (Jack bean), Type IV-S, lyophilized powder, aseptically processed, BioReagent, suitable for cell culture
Sigma-Aldrich
Concanavalin A from Canavalia ensiformis (Jack bean), Type IV-S, lyophilized powder, γ-irradiated, BioReagent, suitable for cell culture
Sigma-Aldrich
Concanavalin A from Canavalia ensiformis (Jack bean), Type IV, lyophilized powder
Sigma-Aldrich
Concanavalin A from Canavalia ensiformis (Jack bean), Type VI, lyophilized powder
Sigma-Aldrich
Actinomycin D, from Streptomyces sp., ≥95% (HPLC)
Sigma-Aldrich
Aphidicolin, Ready Made Solution, from Nigrospora sphaerica
Sigma-Aldrich
Aldolase from rabbit muscle, ammonium sulfate suspension, 10-20 units/mg protein
Sigma-Aldrich
Aldolase from rabbit muscle, lyophilized powder, ≥8.0 units/mg protein