Is on immunoglobulin and T cell receptor genes. We also thank Dr. Keiko Hiyama and Dr. Eiso Hiyama at Hiroshima University for technical advices to carry out gene expression analyses, Donna F. Kusewitt for consultation on histological diagnosis, and Dr. Lorenz Poellinger at Karolinska Institute for supplying HIF-1alpha expression plasmid and advices by means of this study.Author ContributionsConceived and created the experiments: ES NS-A KT. Performed the experiments: ES NS-A AS MI HN YK KT. Analyzed the information: TK KN SK. Contributed reagents/materials/analysis tools: YS CT HY. Wrote the paper: ES NS-A KT.
J Mol Med (2013) 91:599?11 DOI 10.1007/s00109-012-0976-yORIGINAL ARTICLEParkinson’s disease-associated mutations in DJ-1 modulate its dimerization in living cellsMariaelena Repici Kornelis R. Straatman Nadia Balduccio Francisco J. Enguita Tiago F. Outeiro Flaviano GiorginiReceived: 18 September 2012 / Revised: 17 October 2012 / Accepted: 25 October 2012 / Published on-line: 27 November 2012 # The Author(s) 2012. This article is published with open access at SpringerlinkAbstract Mutations within the protein DJ-1 lead to recessive forms of early onset familial Parkinson’s illness (PD).(R)-2-Chloro-2-fluoroacetic acid Chemscene To date, a lot of the causative mutations studied destabilize formation of DJ-1 homodimers, which appears to become closely linked to its typical function in oxidative anxiety as well as other cellular processes.2-Bromo-4-fluoro-5-methylpyridine Order Regardless of the significance of understanding the dimerization dynamics of this protein, this aspect of DJ1 biology has not previously been straight studied in living cells. Here, we use bimolecular fluorescence complementation to study DJ-1 dimerization and uncover not simply that DJ-1 forms homodimers in living cells but that most PD causativeElectronic supplementary material The on line version of this short article (doi:ten.1007/s00109-012-0976-y) includes supplementary material, that is readily available to authorized customers. M. Repici : N. Balduccio : F. Giorgini (*) Division of Genetics, University of Leicester, Leicester, UK e-mail: [email protected] K. R. Straatman Centre for Core Biotechnology Services, University of Leicester, Leicester, UK F. J. Enguita Unidade de Biologia Celular, Instituto de Medicina Molecular, Lisboa, Portugal T. F. Outeiro Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisbon, Portugal T. F. Outeiro Instituto de Fisiologia, Faculdade de Medicina de Lisboa, Lisboa, Portugal T.PMID:22943596 F. Outeiro (*) Department of Neurodegeneration and Restorative Study, University Medizin G tingen, G tingen, Germany e-mail: touteiro@gmailDJ-1 mutations disrupt this procedure, including the L166P, M26I, L10P, and P158 mutations. Interestingly, the E64D mutant form of DJ-1 retains the ability to type homodimers. On the other hand, even though wild-type DJ-1 dimers are stabilized under oxidative tension situations, we obtain that the E64D mutation blocks this stabilization. Additionally, our information show that the E64D mutation potentiates the formation of aggresomes containing DJ-1. We also observe that while the widely studied L166P mutation prevents DJ-1 from forming homodimers or heterodimers with wild-type protein, the mutant protein is in a position to partially disrupt formation of wild-type homodimers. In summary, by investigating DJ-1 dimerization in living cells, we’ve got uncovered many novel properties of PD causative mutations in DJ-1, which may possibly eventually give novel insight into PD pathogenesis and achievable therapeutic choices. Keyword phrases Parkinson’s illness . DJ-1 . Dimerization.
