Articles by Javier Gualix in JoVE
Live Imaging Followed by Single Cell Tracking to Monitor Cell Biology and the Lineage Progression of Multiple Neural Populations Rosa Gómez-Villafuertes*1,2,3, Lucía Paniagua-Herranz*1,2,3, Sergio Gascon*4,5, David de Agustín-Durán1,2,3, María de la O Ferreras1,2,3, Juan Carlos Gil-Redondo1,2,3, María José Queipo1,2,3, Aida Menendez-Mendez1,2,3, Ráquel Pérez-Sen1,2,3, Esmerilda G. Delicado1,2,3, Javier Gualix1,2,3, Marcos R. Costa6, Timm Schroeder7, María Teresa Miras-Portugal1,2,3, Felipe Ortega1,2,3 1Biochemistry and Molecular Biology Department, Faculty of Veterinary medicine, Complutense University, 2University Institute for Neurochemistry Research (IUIN), 3Instituto de Investigación Sanitaria del Hospital Clínico San Carlos (IdISSC), 4Institute of Stem Cell Research, Helmholtz Center Munich, Neuherberg/Munich, Germany Physiological Genomics, Biomedical Center, Ludwig-Maximilians University Munich, 5Toxicology and Pharmacology Department, Faculty of Veterinary medicine, Complutense University, 6Brain Institute, Federal University of Rio Grande do Norte, 7Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich A robust protocol to monitor neural populations by time-lapse video-microscopy followed by software-based post-processing is described. This method represents a powerful tool to identify biological events in a selected population during live imaging experiments.
Other articles by Javier Gualix on PubMed
Role of P2X7 and P2Y2 Receptors on α-secretase-dependent APP Processing: Control of Amyloid Plaques Formation "in Vivo" by P2X7 Receptor Computational and Structural Biotechnology Journal. | Pubmed ID: 25848496 Amyloid precursor protein (APP) is expressed in a large variety of neural and non-neural cells. The balance between non-pathogenic and pathologic forms of APP processing, mediated by α-secretase and β-secretase respectively, remains a crucial step to understand β-amyloid, Aβ42 peptide, formation and aggregation that are at the origin of the senile plaques in the brain, a characteristic hallmark of Alzheimer's disease (AD). In Neuro-2a, a neuroblastoma cell line that constitutively expresses APP, activation of the P2X7 receptor leads to reduction of α-secretase activity, the opposite effect being obtained by P2Y2 receptor activation. The in vivo approach was made possible by the use of J20 mice, a transgenic mouse model of familial Alzheimer's disease (FAD) expressing human APP mutant protein. This animal exhibits prominent amyloid plaques by six months of age. In vivo inhibition of the P2X7 receptor induced a significant decrease in the number and size of hippocampal amyloid plaques. This reduction is mediated by an increase in the proteolytic processing of APP through α-secretase activity, which correlates with an increase in the phosphorylated form of GSK-3, a less active form of this enzyme. The in vivo findings corroborate the therapeutic potential of P2X7 antagonists in the treatment of FAD.