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Na + /K + -ATPase maintains electrochemical gradients of Na +  and K +  essential for a variety of cellular functions including neuronal activity. The α-subunit of the Na + /K + -ATPase exists in four different isoforms (α1–α4) encoded by different genes. With a view to future use of pig as an animal model in studies of human diseases caused by Na + /K + -ATPase mutations, we have determined the porcine coding sequences of the α1–α3 genes,  ATP1A1 ,  ATP1A2 , and  ATP1A3 , their chromosomal localization, and expression patterns. Our  ATP1A1  sequence accords with the sequences from several species at five positions where the amino acid residue of the previously published porcine  ATP1A1  sequence differs. These corrections include replacement of glutamine 841 with arginine. Analysis of the functional consequences of substitution of the arginine revealed its importance for Na +  binding, which can be explained by interaction of the arginine with the C-terminus, stabilizing one of the Na +  sites. Quantitative real-time PCR expression analyses of porcine  ATP1A1 ,  ATP1A2 , and  ATP1A3  mRNA showed that all three transcripts are expressed in the embryonic brain as early as 60 days of gestation. Expression of α3 is confined to neuronal tissue. Generally, the expression patterns of  ATP1A1 ,  ATP1A2 , and  ATP1A3  transcripts were found similar to their human counterparts, except for lack of α3 expression in porcine heart. These expression patterns were confirmed at the protein level. We also report the sequence of the porcine  ATP1A3  promoter, which was found to be closely homologous to its human counterpart. The function and specificity of the porcine  ATP1A3  promoter was analyzed in transgenic zebrafish, demonstrating that it is active and drives expression in embryonic brain and spinal cord. The results of the present study provide a sound basis for employing the  ATP1A3  promoter in attempts to generate transgenic porcine models of neurological diseases caused by  ATP1A3  mutations.

Molecular Cloning and Characterization of Porcine Na+/K+-ATPase Isoforms α1, α2, α3 and the ATP1A3 Promoter