Giuseppe Inesi, M.D. Ph.D. Professor and Chair      108 N. Greene Street, Room 103      Baltimore, MD 21201      Phone: 410-706-3220      Fax: 410-706-8297      email: ginesi@umaryland.edu EDUCATION 1954 - 1960 M.D./Ph.D.   University of Modena and Bologna, Italy   1960 - 1963  Postdoctoral     University of Pennsylvania   1963 - 1965  Postdoctoral     University of California, San Francisco

PROFESSIONAL EXPERIENCE
1965-69           Established Investigator of the American Heart Association
1965-69           Assistant Pro­fessor,  Pharmacology University of California San Francisco, California                
1969-72           Associate Professor, Carnegie-Mellon University. Pittsburgh, (Biochemistry)
1972-81           Professor, University of the Pacific, San Francisco, California (Physiology)
1981-present    Professor and Chairman, University of Maryland Baltimore, Biochemistry                  
1989-90           Visiting Professor, Stanford University, Stanford, California
1996-97           Visiting Professor, University of California, San Francisco, California  

RESEARCH DESCRIPTION
Our laboratory is interested in the molecular characterization of the mechanism of Ca2+ transport by a group of ATPases associated with intracellular membranes, and the effects of these ATPases in cellular functions. These ATPases play an important role in control of the cytosolic Ca2+ concentration and, thereby, in regulation of cellular functions by Ca2+. Our experimental approach includes isolation of intracellular membranes; purification of proteins; kinetic measurements of ion fluxes and coupled enzyme reactions; studies of protein structure and function by chemical derivatization and site directed mutagenesis; gene transfer to express recombinant protein and to influence cellular functions.

                                                       Click Figure Below to Enlarge:

SELECTED PUBLICATIONS:
Inesi, G., Mechanism of calcium transport. Ann. Rev. Physiol., 47:573-601, (1985).

Inesi, G. Kurzmack, M. and Lewis, D., Kinetic and equilibrium charac­ter­ization of an energy dependent enzyme and its partial reactions.  In: "Methods in   Enzymology" (S. Fleischer and B. Fleischer, eds.), New York: Academic Press, Inc., Vol. 157, 154-190, (1988).

Inesi, G., Sumbilla, C., and Kirtley, M.E. Relationships of molecular structure and function in the Ca²⁺ transport. ATPase.  Physiol. Rev. 7(3):749-760 (1990).

Inesi, G., Lewis, D., Nikic, D., and Kirtley, M.E. Long range intramolecular linked functions in the calcium transport ATPase. In: “Advances in Enzymology” (Alton Meister, Ed.) New York: John Wiley & Sons, 185-215  (1992)

Seth M, Sumbilla C, Mullen SP, Lewis D, Klein MG, Hussain A, Soboloff J, Gill DL, Inesi,G. Sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) gene silencing and remodeling of the Ca2+ signaling mechanism in cardiac myocytes. Proc Natl Acad Sci   U S A. 101:16683-8 (2004) 

Teucher N, Prestle J, Seidler T, Currie S, Elliott EB, Reynolds DF, Schott P, Wagner S, Kogler H, Inesi G, Bers DM, Hasenfuss G, Smith GL.Excessive sarcoplasmic / endoplasmic reticulum Ca2+-ATPase expression causes increased sarcoplasmic reticulum Ca2+ uptake but decreases myocyte shortening.Circulation. 110:3553-9 (2004)

Ma H, Sumbilla CM, Farrance IK, Klein MG, Inesi G.Cell-specific expression of SERCA, the exogenous Ca2+ transport ATPase,in cardiac myocytes. Am J Physiol Cell Physiol. 2004;286(3):C556-64  (2004)

Inesi G, Ma H, Lewis D, Xu C.: Ca2+ occlusion and gating function of Glu309 in the ADP-fluoroaluminate analog of the Ca2+-ATPase phosphoenzyme intermediate.J Biol Chem. 279:316 (2004)