![]() ![]() In Schizosaccharomyces pombe the Na +/H+ exchanger (sod2) moves Na + out of the cell in exchange for H +. We also have a great interest in pH regulation and ion movements in yeast. Both p90rsk and MAP kinase are key protein kinases involved in regulation of activity of the protein. We have shown that MAP kinase dependent pathways are key to the regulation of activity of the Na +/H + exchanger. In the heart we have examined regulation of expression and activity of the protein. We have a special interest in the Na +/H + exchanger in the mammalian heart, because the protein is important in heart disease. My laboratory has also studied phosphorylation of the antiporter and factors affecting localization and targeting of the protein. In collaboration with others we have elucidated the structure of parts of the membrane domain of the protein. We have used site-specific mutagenesis to discover which amino acids are important in transport and have examined the structure of parts of the cytosolic and membrane domains. We have examined the structure and characterized activity of the protein. My laboratory has studied many aspects of the NHE1 protein. NHE1 is the most widespread and exists in all mammalian cells. ![]() Several isoforms of the protein exist (NHE1 to NHE10). It is involved in pH regulation and is stimulated by growth factors. The Na +/H +exchanger is a mammalian plasma membrane protein that exchanges one intracellular proton for an extracellular sodium. In mammalian tissues the main protein responsible for this is the Na +/H + exchanger. Our laboratory studies the regulation of intracellular pH and the removal of excess intracellular acid. In the heart, too much acid inhibits contractile activity and damages the myocardium. Too much acid has a deleterious effect on the activity of various enzymes and results in abnormalities in metabolism and cell cycle. As a result of metabolism, excess intracellular acid is produced in all cells. Handling acid is a problem in all organisms. Fax: 780.492.0886 Lab Website Research Description ![]()
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