Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
J Exp Biol. July 1, 2011; 214 (Pt 13): 2164-74.

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

Galarza-Muñoz G , Soto-Morales SI , Holmgren M , Rosenthal JJ .

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.

PubMed ID: 21653810
PMC ID: PMC3110501
Article link: J Exp Biol.
Grant support: 1R01NS64259 NINDS NIH HHS , 2 U54 NS039405-06 NINDS NIH HHS , G12 RR 03051 NCRR NIH HHS , P20 RR16470 NCRR NIH HHS , S06GM08102 NIGMS NIH HHS , ZIA NS002993-10 NINDS NIH HHS , ZIA NS002993-10 Intramural NIH HHS, G12 MD007600 NIMHD NIH HHS, R01 NS064259 NINDS NIH HHS , P20 RR016470 NCRR NIH HHS , G12 RR003051 NCRR NIH HHS , U54 NS039405 NINDS NIH HHS , S06 GM008102 NIGMS NIH HHS

External Resources:

Albers, 2008, Pubmed[+]

Xenbase: The Xenopus laevis and X. tropicalis resource.
Version: 4.9.0
Major funding for Xenbase is provided by the National Institute of Child Health and Human Development, grant P41 HD064556