Gonzalo Izaguirre, PhD
Research Assistant Professor
Building & Room:
801 S. Paulina St., IL 60612
Dr. Gonzalo Izaguirre serves as Research Assistant Professor in the Department of Periodontics. Dr. Izaguirre earned his PhD from the University of Maryland and completed a postdoctoral fellowship at Rutgers University. His research interest include understanding the role of proteolytic enzymes in the maintenance of physiological homeostasis.
Izaguirre G, Swanson R, Roth R, Gettins PGW, and Olson ST. (2021) Paramount importance of core conformational changes for heparin allosteric activation of antithrombin. Biochemistry doi.org/10.1021/acs.biochem.1c00128
Izaguirre G. (2019) The proteolytic regulation of virus cell entry by furin and other proprotein convertases. Viruses 11(9) doi: 10.3390/v11090837
Izaguirre G, Arciniega M, and Quezada AG. (2019) Specific and selective inhibitors of proprotein convertases engineered by transferring serpin B8 reactive-site and exosite determinants of reactivity to the serpin α1PDX. Biochemistry 58:1679-1688
Aguila S, Izaguirre G, Martínez-Martínez I, Vicente V, Olson ST, and Corral J (2017) Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities. Journal of Biological Chemistry 292:16513-16520
Izaguirre G, Aguila S, Qi L, Swanson R, Roth R, Rezaie AR, Gettins PG, and Olson ST (2014) Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease. Journal of Biological Chemistry 289:34040-34064
Izaguirre G, Qi L, Lima M, and Olson ST (2013) Identification of serpin determinants of specificity and selectivity for furin inhibition through studies of α1-PDX (α1-proteinase inhibitor Portland)-serpin B8 and furin active-site loop chimeras. Journal of Biological Chemistry 288:21802-21814
- National Autonomous University of Mexico, B.Sc., Biology, 1988
- University of Maryland at College Park, PhD, Biochemistry, 1995
- Rutgers University, Postdoctoral Fellow, Protein Chemistry and Enzymology, 1998
- University of Medicine and Dentistry of New Jersey, Research Associate, 2001
Research Currently in Progress
Proteolytic enzymes play a central role in the maintenance of physiological homeostasis. Complex networks of serine proteases are controlled by serpins, which are a type of protease inhibitors. We conduct research on the inhibition of two networks of serine proteases by serpins:
One is the Proprotein Convertases (PCs), which are a family of intracellular and pericellular serine proteases that are key regulators of cell growth, proliferation and differentiation. PCs are important therapeutic targets and diagnostic markers in cancer and infectious diseases. We study the regulation of the mechanism of virus cell entry by PCs.
The other is the Clotting Factors, which are serum serine proteases that regulate blood coagulation. We study the mechanism of heparin-induced activation of the serpin antithrombin and the structural elements that determine specificity for the inhibition of clotting factors by antithrombin. We seek to engineer anticoagulant serpins for the heparin-independent inhibition of clotting factors.