Physiological adaptation of an Antarctic Na+/K +-ATPase to the cold

Gaddiel Galarza-Muñoz, Sonia I. Soto-Morales, Miguel Holmgren, Joshua J.C. Rosenthal

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


Because enzymatic activity is strongly suppressed by the cold, polar poikilotherms face significant adaptive challenges. For example, at 0°C the catalytic activity of a typical enzyme from a temperate organism is reduced by more than 90%. Enzymes embedded in the plasma membrane, such as the Na +/K+-ATPase, may be even more susceptible to the cold because of thermal effects on the lipid bilayer. Accordingly, adaptive changes in response to the cold may include adjustments to the enzyme or the surrounding lipid environment, or synergistic changes to both. To assess the contribution of the enzyme itself, we cloned orthologous Na+/K+-ATPase α-subunits from an Antarctic (Pareledone sp.;-1.8°C) and a temperate octopus (Octopus bimaculatus; ∼18°C), and compared their turnover rates and temperature sensitivities in a heterologous expression system. The primary sequences of the two pumps were found to be highly similar (97% identity), with most differences being conservative changes involving hydrophobic residues. The physiology of the pumps was studied using an electrophysiological approach in intact Xenopus oocytes. The voltage dependence of the pumps was equivalent. However, at room temperature the maximum turnover rate of the Antarctic pump was found to be 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibited a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures. Orthologous Na+/K+ pumps were then isolated from two tropical and two Arctic octopus. The temperature sensitivities of these pumps closely matched those of the temperate and Antarctic pumps, respectively. Thus, reduced thermal sensitivity appears to be a common mechanism driving cold adaptation in the Na+/K+-ATPase.

Original languageEnglish (US)
Pages (from-to)2164-2174
Number of pages11
JournalJournal of Experimental Biology
Issue number13
StatePublished - Jul 2011
Externally publishedYes


  • Antarctica
  • Ion channels
  • Ion transporters
  • Na/K -ATPase
  • Octopus
  • Temperature adaptation

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Physiology
  • Aquatic Science
  • Animal Science and Zoology
  • Molecular Biology
  • Insect Science


Dive into the research topics of 'Physiological adaptation of an Antarctic Na+/K +-ATPase to the cold'. Together they form a unique fingerprint.

Cite this