Peter Vitiello, PhD
The Vitiello laboratory works to identify and define the molecular interface between environmental toxins and biological systems, influencing tissue development, homeostasis, and disease pathogenesis. Research is targeted at understanding how toxins alter redox signaling and molecular networks via cysteine oxidation. The laboratory uses a variety of genetic, molecular, proteomic, and cellular approaches to determine the role of redox signaling during development and disease in response to oxidative perturbations.
Dr. Vitiello graduated from Lafayette College with a BS in Biology and obtained a PhD in Toxicology in the Department of Environmental Medicine at the University of Rochester School of Medicine and Dentistry. Peter continued as a postdoctoral fellow in the Department of Pediatrics at the University of Rochester School of Medicine and Dentistry. Currently, he is an Assistant Scientist in the Environmental Influences on Health & Disease Group at Sanford Research and Assistant Professor of Pediatrics at the University of South Dakota Sanford School of Medicine.
Areas of expertise:
Redox biology, molecular toxicology, lung development and disease
Forred BJ, Daugaard DR, Titus BK, Wood RR, Floen MJ, Booze ML, and Vitiello PF. Detoxification of mitochondrial oxidants and apoptotic signaling are facilitated by thioredoxin-2 and peroxiredoxin-3 during hyperoxic injury. PLOS One v12:e0168777, 2017. PMID: 28045936. PMC5207683.
Booze ML, Hansen J, and Vitiello PF. A novel mouse model for the identification of thioredoxin-1 protein interactions. Free Rad Biol Med v99:533-43, 2016. PMID: 27639450. PMC5107173.
Baack ML, Forred BJ, Jensen DN, Khan M, Larsen T, Wachal AL, and Vitiello PF. Consequences of a maternal high fat diet and late gestation diabetes on the developing rat lung. PLOS One v11:e0160818, 2016. PMID 27518105. PMC4982689.
Floen MJ, Forred BJ, Bloom EJ, Vitiello PF. Thioredoxin-1 redox signaling regulates cell survival in response to hyperoxia. Free Rad. Biol. Med. v75:167-77, 2014. PMID 25106706. PMC4174305.
Staversky RJ, Vitiello PF, O’Reilly MA. Epithelial-specific ablation of Bcl-XL increases susceptibility to oxygen without disrupting lung development. Am J Physiol Lung Cell Mol Physiol v43:376-85, 2009. PMID 19880821. PMC2933553.
Vitiello PF, Wu YM, Staversky RJ, O’Reilly MA. P21Cip1 protects against oxidative stress by suppressing ER dependent activation of mitochondrial death pathways. Free Rad Biol Med v46:33-41, 2009. PMID 18948188. PMC2631574.
Vitiello PF, Staversky RJ, Keng PC, O’Reilly MA. PUMA inactivation protects against oxidative stress through p21/Bcl-XL inhibition of Bax death. Free Rad Biol Med v44:367-74, 2008. PMID 18215742. PMC2276618.
Yee M, Vitiello PF, Roper JM, Staversky RJ, Wright TW, McGrath-Morrow SA, Maniscalco WM, Finkelstein JN, O’Reilly MA. Type II epithelial cells are a critical target for hyperoxia-mediated impairment of postnatal lung development. Am J Physiol Lung Cell Mol Physiol v291:L1101-11, 2006. PMID 16861382.
Staversky RJ, Vitiello PF, Gehen SC, Helt CE, Rahman A, Keng PC, O’Reilly MA. P21Cip1/Waf1/Sdi1 protects against hyperoxia by maintaining expression of Bcl-XL. Free Rad Biol Med v41:601-9, 2006. PMID: 16863993.
Vitiello PF, Staversky RS, Gehen SC, Johnston CJ, Finkelstein JN, Wright TW, O’Reilly MA. P21Cip1 protection against hyperoxia requires Bcl-XL and is uncoupled from its ability to suppress growth. Am J Pathol v168:1838-47, 2006. PMID: 16723699.
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