Page 81 - CIBERER-2015-eng

Most relevant scientific articles
Research Groups
launaY n*, aguado c*, Fourcade s, ruiZ m, grau l, ri- era J, guilera c, giròs m, Ferrer i, Knecht e, PuJol a (2015). Autophagy induction halts axonal degeneration in a mouse model of X-adrenoleukodystrophy. Acta Neuro- pathol, 29(3): 399-415. *equal contribution.
macías-Vidal J, guerrero m, estanYol Jm, aguado c, Knecht e, coll mJ, Bachs o (2015). Identification of lyso- somal Npc1-Binding Proteins: Cathepsin D activity is reg- ulated by NPC1. Proteomics, oct 28.
martíneZ-Zamora a, meseguer s, esteVe Jm, Villar- roYa m, aguado c, enríqueZ Ja, Knecht e, armengod ma (2015). Defective expression of the mitochondrial-tR- NA modifying enzyme GTPBP3 triggers AMPK-mediated
Highlights
Our CiberER group is funded by MINECO (projects SAF2014-54604-C3-2-R y BFU2014-58673-P). The most outstanding results obtained this year have been:
• Lafora disease. The fibroblasts from patients present a decrease in autophagic mitochondrial degradation that would explain the previously ob- served accumulation of damaged mitochondria and the consequent increase in the production of ROS. In collaboration with: U733 and U742.
• X-adrenoleukodystrophy. In all models analyzed of this pathology there is an impairment of auto- phagy that is restored by an inhibitor of mTOR. This treatment improves the neurological pheno- type in mouse models of the disease. We are also analyzing in spinal cords from these mice the ef- fect on autophagy of other treatments. In collabo- ration with: U759.
• Retinitis pigmentosa. The CERKL protein, in- volved in retinitis pigmentosa, but not its patho- logical mutants, interacts with mRNAs from hu- manin-like peptides and with non-coding RNA RN7SL2. CERKL would bind to the mRNAs from
adaptive responses involving complex I assembly factors, uncoupling protein 2, and the mitochondrial pyruvate car- rier. PLoS One. 2015 Dec 7;10(12): e0144273.
romá-mateo c*, aguado c*, garcía-giméneZ Jl*, iBáñeZ-caBellos Js, seco-cerVera m, Pallardó FV, Kne- cht e, sanZ P (2015). Increased Oxidative Stress and Im- paired Antioxidant Response in Lafora Disease. Mol Neu- robiol, 51(3):932-946. *equal contribution.
romá-mateo c*, aguado c*, garcía-giméneZ Jl*, Knecht e, sanZ P, Pallardó FV (2015). Oxidative stress, a new hallmark in the pathophysiology of Lafora progressive my- oclonus epilepsy. Free Rad Biol & Med, 88:30-41. *equal contribution.
humanin-like peptides in the nucleus and, once in the cytoplasm, other proteins of the translation- al machinery and the non-coding RNA RN7SL2 would join them to form compact ribonucleop- rotein particles. They move, via microtubules, to the plasma membrane where co-translational synthesis and secretion of the humanin-like pep- tides probably occurs. These peptides play an an- tiapoptotic role. In collaboration with: U718.
• Mitochondrial diseases. We study here GTPBP3, an evolutionarily conserved protein involved in mitochondrial tRNA modification. In a GTPBP3 stable silenced cell model we found a decrease in mitochondrial size and in their fractional volume, which would be related to an increase in auto- phagy due to activation of AMPK.
• Finally, we collaborate with Dr. Coll. (Hospital Clin- ic, Barcelona) in the study of a lysosomal storage disease, Niemann Pick type C, caused by muta- tions in the NPC1 gene. The work has allowed the identification of several proteins that interact with NPC1.
Institution: Fundación Centro de Investigación Príncipe Felipe. Contact: C/ Eduardo Primo Yúfera, 3 46013 Valencia · Tel.: 96 328 96 81- Ext: 2007 / 2008 (Carmen Aguado) · E.mail: [email protected]
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