Left to right: Tatiana Burrinha, Cláudia Almeida, Catarina Perdigão
As part of World Alzheimer's Day we also share with you a news article regarding the publishing of two papers from Cláudia Almeida's lab, Neuronal Trafficking in Aging, that showcase the contribuition of fundamental science to the deeper knowledge we now have of this disease.
The contribution of fundamental science is essential for the application of clinical research in a vast number of human diseases, such as Alzheimer's disease. The neurons, cells that establish synapses responsible for signalling in the brain, are the same age of the body itself and, as they age, they lose the plasticity. That is due in part to the accumulation of the peptide β-amyloid, first inside neurons and, subsequently abroad taking the form and accumulation in amyloid plaques in the brains of patients with Alzheimer's.
In Cláudia Almeida's laboratory at CEDOC-NMS, Neuronal Trafficking in Aging, the focus is to determine the causal mechanisms of neuronal synapse dysfunction in the most common form of Alzheimer's disease. This form of the disease is closely related to aging, usually beginning after age 65: late-onset Alzheimer's disease (LOAD). Despite aging being the main risk factor for Alzheimer's disease, the contribution of cellular aging of neurons to LOAD is still unknown.
Tatiana Burrinha, PhD student , found that the aging of neurons increases the internalization (endocytosis) of a precursor protein of toxic peptide β - amyloid (APP) . "We found that β-amyloid accumulation within aged neurons is due to an increased internalization of its precursor, amyloid precursor protein (APP). Notably, we also proved that the accumulation of β-amyloid in aged neurons causes synaptic decline. These alterations might contribute to the development of Alzheimer's disease. " said Tatiana in the first person feature of Journal of Cell Science where the results were published.
Catarina Perdigão, also PhD student at Cláudia’s lab, is studying the mechanism involved in the association of the BIN1 gene to LOAD . Catarina found that mutations identified in patients cause alterations in the traffic of BACE1, the enzyme which initiates the processing of APP, leading to its accumulation in the endosomes, thereby increasing the amount of β - amyloid. These results were published in the Journal of Biological Chemistry.