"We focus on molecules called phosphatases, which are genes involved in juvenile
diabetes and rheumatoid arthritis, Graves disease, Lupus and others, and try to understand how they work in the immune cells in order to determine if they are good drug targets for these diseases" - Nunzio Bottini, M.D., Ph.D.
Nunzio Bottini, M.D., Ph.D., is a scientist in the The La Jolla Institute Type 1 Diabetes Research Center. Bottini joined the La Jolla Institute from the USC School of Medicine. Bottini is interested in the genetics of autoimmune diseases, particularly type I (juvenile) diabetes, and the role of molecules called phosphatases in signal transduction.
Bottini received his M.D. in 1996 from the University of Rome, where he also obtained his Ph.D. and completed a residency in allergy and clinical immunology. Between 2000 and 2005, he received postdoctoral training at the Burnham Institute for Medical Research.
Bottini currently serves on grant review panels for the NIH, JDRF and several other groups and also is a reviewer for various scientific journals. At the USC School of Medicine he was an Assistant Professor in the Institute for Genetic Medicine. Previously, he served as an Assistant Professor of Medicine at the University of Rome in Italy.
Research in the Bottini lab is focused on a protein called PTPN22, which is a critical negative regulator of T lymphocyte activation. Dr. Bottini discovered that a mutation in the PTPN22 gene is a predisposing factor to T1D in humans. This finding was then confirmed by many groups and currently PTPN22 is ranked as a major T1D gene. Dr. Bottini's laboratory at the LIAI T1D Center is entirely focused on understanding the regulation of PTPN22 and how the T1D-predisposing PTPN22 variant alters immune cell responses in a manner that predisposes to the autoimmune destruction of insulin-producing beta-cells. The laboratory recently discovered that the T1D-predisposing PTPN22 variant shows higher function than normal. This result suggests that pharmacological inhibition of PTPN22 might be beneficial for prevention or treatment of T1D. In collaboration with other groups at the Center, the laboratory has an active translational program focused on identification of inhibitors of PTPN22 and on testing of these early drugs in animal models of T1D.
The PTPN22 R263Q polymorphism is a risk factor for rheumatoid arthritis in Caucasian case-control samples. Arthritis Rheum. 2011
Autoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residue. J Biol Chem. 2010
Carbon nanotube-based nanocarriers: the importance of keeping it clean.
J Nanosci Nanotechnol. 2010
A study of Adenosine-Deaminase genetic polymorphism in rheumatoid arthritis.
Int J Immunopathol Pharmacol. 2010
Lymphoid tyrosine phosphatase and autoimmunity: human genetics rediscovers tyrosine phosphatases. Semin Immunopathol. 2010
A study of three polymorphic sites of the ADA gene in children with type 1 diabetes mellitus.
J Pediatr Endocrinol Metab. 2010
Gold(I) phosphine mediated selective inhibition of lymphoid tyrosine phosphatase.
J Inorg Biochem. 2010
Type I Diabetes Genetics Consortium. rs2476601 T allele (R620W) defines high-risk PTPN22 type I diabetes-associated haplotypes with preliminary evidence for an additional protective haplotype. Genes Immun. 2009
Identifying potent, selective protein tyrosine phosphatase inhibitors from a library of Au(I) complexes. J Med Chem. 2009
Association of PTPN22 gene functional variants with development of pulmonary tuberculosis in Moroccan population. Tissue Antigens. 2009
Evidence for sex-specific associations between variation in acid phosphatase locus 1 (ACP1) and insulin sensitivity in Mexican-Americans. J Clin Endocrinol Metab. 2009
Regulation of lymphoid tyrosine phosphatase activity: inhibition of the catalytic domain by the proximal interdomain. Biochemistry. 2009
Crystal structure Of The Human Lymphoid Tyrosine Phosphatase Catalytic Domain: Insights Into Redox Regulation. Biochemistry. 2009
Conjugation of Antisense Oligonucleotides to PEGylated Carbon Nanotubes Enables Efficient Knockdown of PTPN22 in T Lymphocytes. Bioconjug Chem. 2009
A loss of function variant of PTPN22 is associated with reduced risk of systemic lupus erythematosus. Hum Mol Genet. 2009
Gold(I)-mediated inhibition of protein tyrosine phosphatases: a detailed in vitro and cellular study. J Med Chem. 2008
Association between PTPN22 C1858T and type 1 diabetes: a replication in continental Italy. Tissue Antigens. 2008
Further evidence of a primary, causal association of the PTPN22 620W variant with type 1 diabetes. Diabetes. 2008
Protein tyrosine phosphatase PTPN22 in human autoimmunity. Autoimmunity. 2007
Lipid raft targeting of hematopoietic protein tyrosine phosphatase by protein kinase C theta-mediated phosphorylation. Mol Cell Biol. 2006
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