Craig Gatto

Prof. Craig Gatto
Illinois State University, USA



1989-1993 Ph.D., Physiology, University of Missouri-Columbia, USA

1987-1989 M.Sc., Zoology, Eastern Illinois University, USA
1983-1987 B.Sc., Zoology, Eastern Illinois University , USA

Publications (Selected)

  1. Black, T.H. and C. Gatto. An Inexpensive, Efficient Synthesis of 1-Methylxanthine. Synth. Comm. 19(5&6): 843-850, 1989.
  2. Gatto, C. and M.A. Milanick. Inhibition of the Human Red Calcium Pump by Eosin and other Fluorescein Analogs. Am. J. Physiol. Cell Physiology. 264, C1577-C1586, 1993.
  3. Gatto, C. and M.A. Milanick. Does Eosin Treat all P-type ATPases Equally?   In: Bamberg, E, Schoner, W. eds, The Sodium Pump: Structure Mechanism, Hormonal Control and its Role in Disease. Dietrich Steinkopff, Darmstadt, Germany, pp. 609-612, 1994.
  4. Gatto, C., C.C. Hale, Wanyan Xu, and M.A. Milanick. Eosin, a potent inhibitor of the plasma membrane Ca pump, does not inhibit the cardiac Na-Ca exchanger.   Biochemistry. 34, 965-972, 1995.
  5. Xu, W.-Y., C. Gatto, C.J. Allen, and M.A. Milanick. Use of cysteine replacements and chemical modification to alter XIP, the autoinhibitory region of the Na/Ca exchanger: Inhibition of the activated plasma membrane Ca pump.   Ann.N.Y. Acad. Sci.    779, 286-287, 1996.
  6. Gatto, C., W.-Y. Xu, H.A. Denison, C.C. Hale, and M.A. Milanick. Modifications of XIP, the autoinhibitory region of the Na/Ca exchanger, alter its ability to inhibit the Na/Ca exchanger in bovine sarcolemmal vesicles. Ann. N.Y. Acad. Sci.  779, 284-285, 1996.
  7. Xu, W.-Y., C. Gatto, M.A. Milanick. Positive charge modifications alter the ability of XIP to inhibit the plasma membrane calcium pump. Am. J. Physiol: Cell Physiol., 271, C736-C741, 1996.
  8. Gatto, C., S. Lutsenko, and Jack H. Kaplan. Chemical modification with H2DIDS reveals the distance between K480 and K501 in the ATP-binding domain of the Na,K-ATPase. Arch. Biochem. Biophys. 340, 90-100, 1997.
  9. Xu, W.-Y., C.C. Hale, H.D. Denison, C. Gatto, and M.A. Milanick. Identification of critical positive charges in XIP, the Na/Ca Exchange inhibitory peptide. Arch. Biochem. Biophys. 341, 273-279, 1997.
  10. Kaplan, J.H., C. Gatto, S. Lutsenko, and L.J. Kenney. Structural determinations of the cation and ATP binding domains of the Na/K-ATPase. Ann. N.Y. Acad. Sci. 834, 45-55, 1997.
  11. Gatto, C., A.X. Wang, and J.H. Kaplan. The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleotide triphosphates with the same selectivity as the native protein. J. Biol. Chem. 273(17), 10578-10585, 1998.
  12. Kaplan, J.H., C. Gatto, J.P. Holden, and S.J. Thornewell. Structural changes associated with the coupling of ATP Hydrolysis and Cation Transport by the Na pump. Acta Physiol. Scand. 163, 99-105, 1998.
  13. 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.
  14. 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 -subunit.aNa,K-ATPase   J. Biol. Chem. 274, 24995-25003, 1999.
  15. Gatto, C., S.J. Thornewell, and J.H. Kaplan. Cation-induced conformational changes in the ATP-binding domain of the Na,K-ATPase alter the reactivity of Lys501 and Cys577. In. Na/K-ATPase and Related ATPases. (K. Taniguchi and S. Kaya, eds.) pp. 429-432., 2000.
  16. 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. Physiol. - Cell Phys. 281, C982-C992, 2001.
  17. Kaplan, J.H., Hu, Y-K., Gatto, C. Conformational Coupling: The moving parts of an ion pump. J. Bioenerg. Biomemb. 33(5), 383-388, 2001.
  18. Gatto, C., Barkulis, C.T., Schneider, W.J., Arnett, K.H., and Milanick, M.A. Inhibition of Na pump by the antiarrthmic drug, Bretylium. Ann. NY Acad. Sci., 986, 620-622, 2003.
  19. Costa, C.J., Gatto, C, and Kaplan, J.H. Interaction between -subunit ATP-binding domains.aNa,K-ATPase J. Biol. Chem. 278, 9176-9184, 2003.
  20. Helms, J.B., Arnett, K.L., Gatto, C., and Milanick, M.A. Bretylium, an organic quaternary amine, inhibits the Na,K-ATPase by binding to the extracellular K-site. Blood cells, Mol., & Dis. 32(3), 394-400, 2004.
  21. 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. 289, C302-C311, 2005.
  22. Gatto, C., Helms, J.B., Prasse, M.C., Huang, SY, Zou, X., 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
  23. J.T. Ogan, M.S. Reifenberger, M.A. Milanick, and C. Gatto Kinetic characterization of Na,K-ATPase inhibition by Eosin. Blood cells, Mol., & Dis. 38, 229-237, 2007.
  24. M.S. Reifenberger, K.L. Arnett, C. Gatto, and M.A. Milanick. Extracellular terbium and divalent cation effects on the red blood cell Na pump and chrysoidine effects on the renal Na pump. Blood cells, Mol., and Dis. 39, 7-13, 2007.
  25. C. Gatto, K.L. Arnett, and M.A. Milanick. Divalent cation interactions with the cytoplasmic Na,K-ATPase sites: implications for pNPPase reaction mechanism. J. Memb. Biol. 216, 49-59, 2007.
  26. Reifenberger, M.S., Arnett, K.L., Gatto, C., Milanick, M.A. The reactive nitrogen species peroxynitrite is a potent inhibitor of renal Na,K-ATPase activity. Am. J. Physiol. – Renal Physiol. 295, 1191-1198, 2008.
  27. Johnson, N.A., Liu, F., Weeks, P.D., Hentzen, A.E., Kruse, H.P., Parker, J.J., Laursen, M., Nissen, P., Costa, C.J., and Gatto, C. A Tomato ER-type Ca2+-ATPase, LCA1, has a Low Thapsigargin-sensitivity and can Transport Manganese. Arch. Biochem. & Biophysics. 481, 157-168, 2009.
  28. Gatto, C. and Milanick, M.A. Red Blood Cell Na pump: Insights from Species Differences. Blood cells, Mol., and Dis. 2009, 42(3): 192-200, 2009 .
  29. Yaragatupalli, S., Olivera, J.F., Gatto, C., and Artigas, P. Altered Na+ transport after an -subunit deletion reveals strict external sequential release ofaintracellular Na+ from the Na/K pump. Proc. Natl. Acad. Sci. USA. 106, 15507-15512, 2009.
  30. AK Singh, Y-M Zhang, K Zhu, C Subramanian, Z Li, RK Jayaswal, C Gatto, CO Rock, and BJ Wilkinson. FabH selectivity for anteiso branched-chain fatty acid precursors in low temperature adaptation in Listeria monocytogenes. FEMS Microbiol. Lett. 301, 188-192, 2009.
  31. Julotok, M., Singh, A.K., Gatto, C., and Wilkinson, B.J. Influence of Fatty Acid Precursors, Including Food Preservatives, on the Growth and Fatty Acid Composition of Listeria monocytogenes at 37 and 10oC. App. Environ. Micro. 76, 1423-1432, 2010.
  32. Gatto, Craig. NO control: nitric oxide directly regulates substrate delivery to NOS. Am. J. Physiol. – Cell Physiol. 299, C213 – C215, 2010.
  33. Ratheal, I.M., Virgin, G.K., Yu, H., Roux, B., Gatto, C., and Artigas, P. Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations. Proc. Natl. Acad. Sci. USA. 107, 18718–18723, 2010.