<p>Mammalian cells have been previously shown to utilize maltose as an energy source for long-term cell growth. To characterize maltose uptake and consumption in CHO-K1, we measured its intracellular concentrations over time and tracked the incorporation of C13-labelled disaccharides into TCA cycle intermediates. Lysosomal acid α-glucosidase (GAA) was identified to potentially be involved in the initial reaction of breaking the α(1 → 4)-glycosidic bond in maltose, releasing two glucose residues for energy metabolism. Using a GAA-KO CHO-K1 cell line, we showed that GAA is involved in CHO-K1 maltose metabolism. Transport of maltose in wild-type and GAA-KO CHO-K1 is concentration-dependent. The rate of maltose uptake for GAA-KO cells was also linear when extracellular maltose is between 0 to 40&#xa0;g/L, and saturation in uptake kinetics was not observed over that concentration range.</p>

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Maltose metabolism in serum free CHO culture involves lysosomal acid α-glucosidase

  • Tessa Rui Min Tan,
  • Lian Yee Yip,
  • Janice Gek Ling Tan,
  • Dawn Sow Zong Leong,
  • Yan Ni Annie Soh,
  • Shi Ya Mak,
  • Ying Swan Ho,
  • Say Kong Ng

摘要

Mammalian cells have been previously shown to utilize maltose as an energy source for long-term cell growth. To characterize maltose uptake and consumption in CHO-K1, we measured its intracellular concentrations over time and tracked the incorporation of C13-labelled disaccharides into TCA cycle intermediates. Lysosomal acid α-glucosidase (GAA) was identified to potentially be involved in the initial reaction of breaking the α(1 → 4)-glycosidic bond in maltose, releasing two glucose residues for energy metabolism. Using a GAA-KO CHO-K1 cell line, we showed that GAA is involved in CHO-K1 maltose metabolism. Transport of maltose in wild-type and GAA-KO CHO-K1 is concentration-dependent. The rate of maltose uptake for GAA-KO cells was also linear when extracellular maltose is between 0 to 40 g/L, and saturation in uptake kinetics was not observed over that concentration range.