My laboratory studies the role of ion-transport proteins of the plasma membrane in cell function. Research is focused on the Na,K-ATPase, a plasma membrane enzyme system that uses theenergy from ATP to establish and maintain the high internal K+ and low internal Na+ concentrations characteristic of most animal cells. The transporter comprises a group of isozymes, each characterized by unique enzymatic properties and a cell-dependent and developmentall regulated pattern of expression. Experiments are designed to understand the function and regulation of the different molecular forms of the transporter. A variety of molecular and cellular biology methods are used to study these important enzymes, both in their native environment and after expression in cells in culture. These studies are important to understand how cells are able to control water and ion balance in physiological and pathological conditions.
Blanco, G, RJ Melton, G Sánchez and RW Mercer. (2000). Alpha 4 is a functional isoform of the Na,K-ATPase and displays similar kinetics when associated with the beta-1 or beta-3 subunits. Excerpta Medica. 305-308.
Blanco, G, G Sánchez, RJ Melton, WG Tourtellotte and RW Mercer. (2000) The alpha 4 isoform of the Na,K-ATPase is expressed in the germ cells of the testes. J. Histochem. Cytochem. 48: 1023-1032.
Blanco, G. (2003). Functional expression of the alpha 4 isoform of the Na,K-ATPase in both diploid and haploid germ cells of male rats. In: Na,K-ATPase and related cation pumps: Structure, function, and regulatory mechanisms. Annals N. Y. Acad. Sci. 986: 536-538.
Huang B, G Blanco, RW Mercer, T Fleming and JS Pepose. (2003) Human corneal endothelial cell expression of Na,K-adenosine triphosphatase isoforms. Arch. Ophtalmol. 121: 840-845.
Sanchez, G and G Blanco. (2004) Residues within transmembrane domains 4 and 6 of the Na,K-ATPase alpha subunit are important for Na+ selectivity. Biochem. 43: 9061-9074.
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