We are studying the relationships between structure and function in Calcium ATPase and other ion transport enzymes. The properties of the ATPase isoforms found in cardiac or skeletal muscle are being compared. In these studies we are using different methods of expression of wild type and mutant Ca2+ATPases, as well as, chimeric combinations between Ca2+ATPase and other ATPases in mammalian cell systems, including COS-1 cells and cardiac myocytes. We then determine the functional consequences of these site-specific mutations and chimerizations.
Garnett, C., Sumbilla, C., Fernandez-Belda, F. and Inesi, G. Energy Transduction and Kinetic Regulation by the Peptide Segment Connecting Phosphorylation and Cation Binding Domains in transport ATPases, Biochemistry,35, 11019-11025,1996.
Inesi,G.,Lewis,D.,Sumbilla,C.,Nandi,A.,Strock,C.,Huff,K., Rogers,T.,Johns,D.,Kessler,P.,and Ordahl,C. Cell-specific promoter in adenovirus vector for transgenic expression of SERCA1 ATPase in cardiac myocytes.Am. J. Physiol. 274 (Cell Physiol.43) March,1998.