Education:

Current Research Support:   (we also thank our previous supporters - click)

    - National Institutes of Health - General Medical Sciences Division

    - National Institutes of Health - Allergy and Infectious Disease

    - National Science Foundation - CAREER Award

    - National Science Foundation - Major Research Instrumentation

Research Interests:

Determining the mechanism of energy transduction by ion pumps (e.g. how is the chemical energy stored in ATP converted to mechanical work required to move substances in and out of cells?).  The answer to this and similar questions will help us understand the underlying mechanisms of several pathophysiological states which stem from improperly functioning transport proteins (e.g. Cystic Fibrosis, Menkes disease, Wilson's disease).  Currently, we use modern molecular biology and protein biochemistry techniques to study the structure and function of the Sodium Pump (i.e. Na,K-ATPase).  The Na,K-ATPase is the pharmacological target for cardiac glycoside treatment of congestive heart failure.  A goal of the lab is to determine the amino acids that coordinate cardiac glycoside binding and deciphering the functional mode of pump inhibition.  In addition, we are interested P-type ATPases in general and are currently comparing structural and functional differences between Ca pumps between plants and animals. 

Recent Publications (click on citations to get a pdf file of the article):
  * In addition you can click on some of my co-authors if you want to learn more about their research programs.

Gatto, C., Helms, J.B., Prasse, M., Arnett, K.L., and Milanick, M.A.   Testing Homology Models of P-type ATPases via Kinetics: similarities and differences between cytoplasmic cation access in Na,K-ATPase and PMCA.  Biochemistry.  45, 13331-13345, 2006

Gatto, C., Helms, J.B., Prasse, M., Arnett, K.L., and Milanick, M.A.  Tetrapropylammonium, an exclusive extracellular cation site probe in Na,K-ATPase, reveals how ATP and Pi alter access to the transport site Am. J. Physiol. – Cell Physiol. 2005.

Helms, J.B., Arnett, K.L., Gatto, C., Milanick, M.A.  Bretylium, an organic quaternary amine, inhibits the Na,K-ATPase by binding to the extracellular K-site.  Blood cells, Mol., and Dis. 32, 394-400, 2004.

Costa, C.J., Gatto, C, and Kaplan, J.H.  Interaction between Na,K-ATPase a-subunit ATP-binding domains.  J. Biol. Chem.  278(11): 9176-9184, 2003.

Gatto, C., Barkulis, C.T., Schneider, W.J., Holden, J.P., Arnett, K.H., and Milanick, M.A.  Inhibition of Na pump by the antiarrthmic drug, Bretylium.  Ann. NY Acad. Sci.,   986: 620-622, 2003. 

Gatto, C., McLoud, S.M., and Kaplan, J.H. Heterologous Expression of Na,K-ATPase in Insect Cells:  Intracellular Distribution of Pump Subunits, Am. J. Phys.-Cell Phys. 281(3): C982-C992, 2001.

Kaplan, J.H., Hu, Y-K., and Gatto, C.  Conformational Coupling:  The moving parts of an ion pump. J. Bioeng. Biomemb.  33(5): 383-388, 2001.

Gatto, C., Thornewell, S.J., Holden, J.P., and Kaplan, J.H. Cys⁵⁷⁷ is a conformationally mobile residue in the ATP-binding domain of the Na,K-ATPase a-subunit. J. Biol. Chem. 274: 24995-25003, 1999.

Gatto, C., S. Lutsenko, J.M. Shin, G. Sachs, and J.H. Kaplan. Stabilization of the H,K-ATPase M5M6 membrane hairpin by K⁺ ions: Mechanistic significance for P₂-type ATPases. J. Biol. Chem. 274: 13737-13740, 1999.  

OTHER PUBLICATIONS

People, places, and things (of interest to me)

A great tasting wine:     Lexington Valley Vineyards

For those that prefer hops over grapes check out my friends at: Yukon Cornelius Brewers

This page was last updated on 02/07/08.