For many years, astrocytes were primarily thought to function as supportive and structural elements in the brain. However, recent studies have revealed that they play much more complex and significant roles in the central nervous system (CNS) including the clearance of cellular debris, unwanted synapses and protein aggregates. Aggregated proteins are a common feature in many neurodegenerative diseases (NDs), including Alzheimer’s disease (AD). The pathology of AD is characterized by the formation of amyloid-beta plaques and the accumulation of Tau protein in neuronal cells. These protein aggregates are toxic to neurons and are released into the extracellular space, where they can be taken up by glial cells, such as astrocytes. The discovery of aggregated neuronal proteins within astrocytes has raised new questions about the mechanisms through which astrocytes operate this clearance. A novel mediator of this process, Annexin A2 (AnxA2), has been identified. AnxA2 is an actin-binding protein involved in processes such as endocytosis, exocytosis, and actin remodeling, which can interact directly with the N-terminal region of Tau. The aim of this study is to evaluate the role of AnxA2 in Tau clearance in astrocytes, shedding light on the mechanisms involved in this process and the degradation capacity of astrocytes.
For many years, astrocytes were primarily thought to function as supportive and structural elements in the brain. However, recent studies have revealed that they play much more complex and significant roles in the central nervous system (CNS) including the clearance of cellular debris, unwanted synapses and protein aggregates. Aggregated proteins are a common feature in many neurodegenerative diseases (NDs), including Alzheimer’s disease (AD). The pathology of AD is characterized by the formation of amyloid-beta plaques and the accumulation of Tau protein in neuronal cells. These protein aggregates are toxic to neurons and are released into the extracellular space, where they can be taken up by glial cells, such as astrocytes. The discovery of aggregated neuronal proteins within astrocytes has raised new questions about the mechanisms through which astrocytes operate this clearance. A novel mediator of this process, Annexin A2 (AnxA2), has been identified. AnxA2 is an actin-binding protein involved in processes such as endocytosis, exocytosis, and actin remodeling, which can interact directly with the N-terminal region of Tau. The aim of this study is to evaluate the role of AnxA2 in Tau clearance in astrocytes, shedding light on the mechanisms involved in this process and the degradation capacity of astrocytes.
Investigating the Role of Annexin A2 in Astrocyte-Mediated Clearance of Tau Aggregates
ZANON, ILARIA
2023/2024
Abstract
For many years, astrocytes were primarily thought to function as supportive and structural elements in the brain. However, recent studies have revealed that they play much more complex and significant roles in the central nervous system (CNS) including the clearance of cellular debris, unwanted synapses and protein aggregates. Aggregated proteins are a common feature in many neurodegenerative diseases (NDs), including Alzheimer’s disease (AD). The pathology of AD is characterized by the formation of amyloid-beta plaques and the accumulation of Tau protein in neuronal cells. These protein aggregates are toxic to neurons and are released into the extracellular space, where they can be taken up by glial cells, such as astrocytes. The discovery of aggregated neuronal proteins within astrocytes has raised new questions about the mechanisms through which astrocytes operate this clearance. A novel mediator of this process, Annexin A2 (AnxA2), has been identified. AnxA2 is an actin-binding protein involved in processes such as endocytosis, exocytosis, and actin remodeling, which can interact directly with the N-terminal region of Tau. The aim of this study is to evaluate the role of AnxA2 in Tau clearance in astrocytes, shedding light on the mechanisms involved in this process and the degradation capacity of astrocytes.File | Dimensione | Formato | |
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https://hdl.handle.net/20.500.12608/81083