Stress-induced nucleocytoplasmic shuttling of TDP-43 is controlled by eIF-5A hypusination
Poster Feb 13, 2017
Carlos Osorno, Shayna Smeltzer, Frank Zamudio, Zain Quadri, Maj-Linda Selenica
Aggregation and phosphorylation of TAR DNA-binding protein-43, TDP-43, has been found to be associated with the neuropathology of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTLD). It has been proposed that TDP-43 accumulation in stress granules (SG) may contribute to the aggregation of TDP43. Eukaryotic translational initiation factor 5A (eIF5A) is hypusinated by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). It is involved at the level of mRNA turnover, cell proliferation, and protein translational elongation. In this experiment we sought to determine the function of hypusinated eIF5a in relation to TDP-43 pathology in nuclear and cytoplasmic compartments under cellular stress.
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A femoral nerve defect model was adapted for the evaluation of proregenerative effects of extracorporeal shockwave therapy (ESWT). Functional evaluation, histology and qRT-PCR data show differences between sensory and motor-derived nerve transplants and a pro-regenerative effect of ESWT. These data provide evidence for the clinical application of ESWT after autologous nerve transplantation as a novel non-invasive method.READ MORE
Electrophysiological Changes Underlying Lapses in Memory ConsolidationPoster
In this study we explore the electrophysiological changes associated with lapses in memory consolidation.READ MORE