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Gonzalo Emiliano Aranda Abreu

Universidad VeracruzanaMexico

Professor Dr. Gonzalo Emiliano Aranda Abreu (Centro de Investigaciones Cerebrales, Universidad Veracruzana, Xalapa, Veracruz, Mexico) was born in 1968 in Ciudad del Carmen, Campeche, Mexico. He received his BSc (Experimental Biology) degree from the Universidad Autónoma Metropolitana, Iztapalapa, Mexico, in 1992; MSc (Molecular Biology and Genetics) degree from the Centro de Investigación y Estudios Avanzados, IPN, Mexico, in 1996; and PhD (Neurobiology) degree from Weizmann Institute of Science, Rehovot, Israel, in 2001. He has more than 20 years of experience in Alzheimer’s disease research. He has written articles on tau mRNA transport in the neuronal axon and Alzheimer’s disease, as well as book chapters where the main theme is brain rehabilitation. He is the president and member of the Southeastern Mexican Chapter of the Society for Neuroscience, USA. He is involved in the training of doctoral students. He teaches molecular and cellular neurobiology, and bioinformatics to PhD degree students. Dr. Gonzalo Aranda\'s research is focused on Alzheimer\'s disease. He has extensive experience in mechanisms for locating mRNAs in the axon. He is also interested in the relationship that exists between neuroinflammation mechanisms and neurodegenerative diseases such as Alzheimer\'s disease. He is trying to find a therapy that can help Alzheimer\'s patients have a better quality of life.

2books edited

2chapters authored

Latest work with IntechOpen by Gonzalo Emiliano Aranda Abreu

"Mechanisms of Neuroinflammation" book explains how the neuronal cells become swollen at the moment of the blood-brain barrier disruption and how they lose their immunological isolation. A cascade of cytokines and immune cells from the bloodstream enters the nervous system, inflaming neurons and activating the glia. This produces a neuroinflammatory process that can generate different neurodegenerative diseases. Better understanding of mechanisms that are activated at the time when the damage to the brain occurs could lead to the development of suitable therapies that revert the neuronal inflammation and thus prevent further damage to the nervous system.

Mechanisms of NeuroinflammationEdited by Gonzalo Emiliano Aranda Abreu

Mechanisms of Neuroinflammation

Edited by Gonzalo Emiliano Aranda Abreu

Books edited

NeuronsDendrites and AxonsEdited by Gonzalo Emiliano Aranda Abreu

Neurons

Edited by Gonzalo Emiliano Aranda Abreu

Chapters authored

Therapeutics of Alzheimer’s Disease

By Marisol Herrera-Rivero and Gonzalo Emiliano Aranda-Abreu

Part of the book: Advanced Understanding of Neurodegenerative Diseases

Alternative Splicing and Alzheimer’s Disease

By Gonzalo Emiliano Aranda Abreu, Sonia Lilia Mestizo Gutiérrez, María Elena Hernández Aguilar and Fausto Rojas Durán

Alzheimer’s disease is a neurodegenerative process whose origin is unknown. It has been associated with this process at least two important proteins: the first is the β-amyloid forming amyloid plaques and the second protein is Tau, which has been determined to precipitates inside the neuron because hyperphosphorylation, causing instability in the axon. Tau microtubule-associated protein (MAP) is essential for the development of neuronal cell polarity. Tau protein is preferentially localized in the axons, whereas MAP2, another neuronal specific microtubule-associated protein, is localized in the somatodendritic domain. Previous studies have demonstrated that the localization of these proteins depends, at least in part, on messenger RNA (mRNA) subcellular localization, that is, Tau mRNA into the axon and MAP2 mRNA into the dendrite. Tau protein has an essential role in the pathology of Alzheimer’s disease, and hyperphosphorylated Tau promotes destabilization of microtubules. Tau alternative splicing generates six isoforms in the adult human brain due to the inclusion or exclusion of exons 2, 3, and 10. The failure in the splicing process of exon 10 generates a tauopathy, which can be carried out by the amyloid peptide; however, the splicing of other exons is less studied. The impact of amyloid peptide on the alternative splicing of exons 2, 3, and 6 caused formed cell processes to retract in differentiated cells and altered the expression of exons 2/3 in cell culture. Expression of exon 6 was repressed under β-amyloid treatment. The molecular mechanism for this amyloid-Tau interaction remains to be determined, but may have potential implications for the understanding of the underlying neuropathological processes in Alzheimer’s disease.

Part of the book: Update on Dementia

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