Luis Eduardo Soares Netto

Luis Eduardo Soares Netto

I attended the University of Sao Paulo (Bacharel Degree in Biology, 1987; Ph.D. in 1992, under the guidance of Dr. Ohara Augusto). During my PhD program, I performed an interchange program (from October 1990 to March 1991) in the Eppley Institute for Research in Cancer and Allied Diseases, Omaha-Nebraska. Later (from December 1992 to May 1996), I was a NIH Postdoctoral Fellow in the Laboratory of Biochemistry – National Heart, Lung and Blood Institute in collaboration with Dr. Stadtman, E.R. In September 1996, I returned to Brazil, where I got a position as Professor of Biochemistry and Molecular Biology at Universidade Estadual de Campinas (UNICAMP – Brazil) until November 1997. I am currently Professor of Genetics at Instituto de Biociências –Universidade de São Paulo (Brazil), where I became a full professor in 2007. My interest is in antioxidant mechanisms and we utilize yeast as a model organism. I participated in the Xylella fastidiosa Genome Project (2000), receiving a prize from the Governor of Sao Paulo State (2000), which resulted in the characterization of a novel class of antioxidant proteins that may represent a novel target for drug development.


Research Profile
The main research interest of Dr. Netto´s group is the investigation of the mechanisms of cell protection against toxic effects of free radicals and related species. In 2005, we joined the Center for Human Genome Research Center as a collaborative group and our activities can be divided into three aspects. (1) Production of recombinant proteins expressed in Escherichia coli. We already provided support for recombinant protein production, allowing the production of antibodies against proteins involved in different kinds of muscular dystrophies (such as teletonin and fukutin-related protein) and for Ube2A (product of the gene associated with a X-linked mental retardation); (2) Investigation of biological effects in yeast of mutations in human genes. In collaboration with Dr. Vianna–Morgante, wild type and mutant alleles of UBE2A gene (related to novel X-linked mental retardation syndrome) were expressed in the yeast Saccharomyces cerevisiae. Insights on the toxic effects of UBE2A gene mutations were obtained. More recently, wild type and mutant alleles associated with Familial Amyotrophic Sclerosis 1 (SOD1) Familial Amyotrophic Sclerosis 8 (VAPB) were also expressed in yeast. The effects of various combinations of double expression of two of these human genes are currently being investigated. (3) Investigation of oxidative stress as a modulator of genetic diseases. In several genetic diseases, their clinical expression is highly variable suggesting the involvement of genetic and environmental factors. We intend to investigate if oxidative stress can represent a modifier component involved in these clinical heterogeneities. Preliminary studies are being conducted with patients with FascioScapuloHumeral Dystrophy (FSHD), whose clinical expression is highly variable even within a single family, ranging from nearly asymptomatic to wheelchair-dependent patients. Initially, we are conducting experiments to establish appropriated oxidative stress markers. Levels of reduced to oxidized glutathione (GSH/GSSG ratios) and protein carbonyls are determined in the serum of control and FSHD patients. Currently, my group is composed of two post-doctoral fellows and six graduate students (five in the PhD program and one in the masters program). Also my laboratory is a member of the National Institute for Science and Technology (INCT): Redox Processes in Biomedicine (“Redoxome”)..


Diagnostic and counseling activities


Total number: 53


Full description in the Google scholar:
10 favourite publications

  1. Cussiol JR, Alegria TG, Szweda LI, Netto LE. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J Biol Chem. 2010; 285(29):21943-50.
  2. Cussiol JR, Alves SV, de Oliveira MA, Netto LE. Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase. J Biol Chem. 2003 Mar 28;278(13):11570-8.
  3. Demasi AP, Pereira GA, Netto LE. Yeast oxidative stress response. Influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state. FEBS J. 2006 Feb;273(4):805-16.
  4. Demasi M, Silva GM, Netto LE. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem. 2003; 278(1):679-85.
  5. Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Bárcena JA, Porras P, Padilla CA, Guimarães BG, Netto LE. Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae. J Mol Biol. 2009 Jan 23;385(3):889-901.
  6. Monteiro G, Horta BB, Pimenta DC, Augusto O, Netto LE. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Proc Natl Acad Sci U S A. 2007;104(12):4886-91.
  7. Netto LE, Chae HZ, Kang SW, Rhee SG, Stadtman ER. Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity. J Biol Chem. 1996; 271(26):15315-21.
  8. Oliveira MA, Guimarães BG, Cussiol JR, Medrano FJ, Gozzo FC, Netto LE. Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa. J Mol Biol. 2006 Jun 2;359(2):433-45.
  9. Simpson AJ et al. The genome sequence of the plant pathogen Xylella fastidiosa. The Xylella fastidiosa Consortium of the Organization for Nucleotide Sequencing and Analysis. Nature. 2000; 406(6792):151-9.
  10. Tairum CA Jr, de Oliveira MA, Horta BB, Zara FJ, Netto LE. Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin. J Mol Biol. 2012 Nov 23;424(1-2):28-41.