Na,K-ATPase isoforms

Lingrel, J.B. (1992). Na,K-ATPase Isoform structure, function, and expression. J. Bioenerg. Biomem. 24,263-270. 

Nishi A, Fisone G, Snyder GL, Dulubova I, Aperia A, Nairn AC, Greengard P (1999) Regulation of Na+, K+-ATPase isoforms in rat neostriatum by dopamine and protein kinase C. J Neurochem 73 1492-1501. 

DEVELOPMENTAL AND THYROID HORMONE REGULATION OF Na,K-ATPase ISOFORMS IN THE BRAIN... 

The expansion of our knowledge of the structure and function of Na,K-ATPase is reflected in a rapid succession of reviews on Na,K-ATPase genes and regulation of expression [17], subunit assembly and functional maturation [20], the isozymes of Na,K-ATPase [18], and the stability of a subunit isoforms during evolution [21], physiological aspects and regulation of Na,K-ATPase [22], reconstitution and cation exchange [23], chemical modification [24], and occlusion of cations [25]. Other valuable sources are the review articles [26] and recent developments [27] reported at the International Na,K-pump Conference in September 1990. 

In the family of cation pumps, only the Na,K-ATPase and H,K-ATPase possess a p subunit glycoprotein (Table II), while the Ca-ATPase and H-ATPase only consist of an a subunit with close to 1 000 amino acid residues. It is tempting to propose that the p subunit should be involved in binding and transport of potassium, but the functional domains related to catalysis in Na,K-ATPase seem to be contributed exclusively by the a subunit. The functional role of the P subunit is related to biosynthesis, intracellular transport and cell-cell contacts. The P subunit is required for assembly of the aj8 unit in the endoplasmic reticulum [20]. Association with a j8 subunit is required for maturation of the a subunit and for intracellular transport of the xP unit to the plasma membrane. In the jSl-subunit isoform, three disulphide... 

Na,K-ATPase is a heterodimer consisting of a catalytic a-subunit and an accessory p-subunit. Four isoforms of the a-subunit and three of the P-subunit are expressed in mammals. Three of the a-subunit isoforms are expressed in brain and will be discussed in a later section. 

Besirli, C. G., Gong, T. W. and Lomax, M. I. Novel beta 3 isoform of the Na,K-ATPase beta subunit from mouse retina. Biochim. Biophys. Acta 1350 21-26,1997. 

Banerjee, B. and Chaudhurym, S. Thyroidal regulation of different isoforms of Na,K-ATPase in glial cells of developing rat brain. Life Sci. 69 2409-2417, 2001. 

Grillo, C., Piroli, G., Lima, A., McEwen, B. S. and DeNicola, A. F. Aldosterone up-regulates mRNA for the alpha3 and betal isoforms of (Na,K)-ATPase in several brain regions from adrenalectomized rats. Brain Res. 767 120-127,1997. 

James PF, Grupp IL, Grupp G et al 1999 Identification of a specific role for the Na,K-ATPase a2 isoform as a regulator of calcium in the heart. Mol Cell 3 555—563 Janiak R, Wilson, SM, Montague S, Hume JR 2001 Heterogeneity of calcium stores and elementary release events in canine pulmonary arterial smooth muscle cells. Am J Physiol 280 C22-C33... 

Skelly, P.J., Dougan, P.M., Maule, A.G., Day, T.A. and Shoemaker, C.B. (2001) Cloning and characterization of a muscle isoform of a Na-, K-ATPase alpha subunit (SNaK1) from Schistosoma mansoni. Parasitology 123, 277-284. 

Jewell, E.A. Lingrel, J.B. (1991). Comparison of the substrate dependence properties of the rat Na,K-ATPase al, a2, and a3 isoforms expressed in HeLa cells. J. Biol. Chem. 266,16925-16930. 

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