Event Title
Effect of sulforaphane on hyperphosphorylation of tau
Location
Suwanee, GA
Start Date
3-5-2022 1:00 PM
End Date
3-5-2022 4:00 PM
Description
Introduction: Various biomarkers have been used to assess astrocyte toxicity. Tau aggregates are insoluble and associated with the pathological symptoms seen in neurodegenerative diseases. Substantial research on pathogenesis of Alzheimer's disease is focused on the buildup of beta-amyloid plaques and phosphorylated tau protein tangles, in which astrocytes are involved in the clearance of these plaques and tangles. It is possible that sulforaphane may positively alter Nuclear factor erythroid 2-related factor 2 (Nrf2), a transcription factor that is a key regulator of oxidative stress and neuroinflammation. Currently, sulforaphane is being examined for an ability to reduce hyperphosphorylation of tau in astrocytes under hypoglycemic conditions. Methods: To induce hyperphosphorylation of tau, an experimental model was developed to deprive rat hippocampal astrocytes of glucose in growth media. Embryonic hippocampal rat astrocytes were cultured in T75 Poly-D-Lysine flasks for 13 days before trypsinizing. The cells were then transitioned to a media containing 100% complete media (high-glucose DMEM and 10% fetal bovine serum). Visualizing tau microtubules in vitro was accomplished via utilization of antibodies specific to the tau protein and a Confocal Microscope. The phosphate groups that bind to the tau protein have been shown to attach to several amino acid residues (Friedhoff, et al. 2012). Serine and threonine are two amino acids that are associated with phosphorylation of tau. Experiments were performed to determine the possible role altered phosphorylated tau at threonine 181 and Ser199/Ser202 distribution within the astrocytes.
Results: Confocal microscopy revealed increased fluorescence due to hyperphosphorylated tau in DNA regions of cells exposed to less glucose. However, the distribution of phosphorylated tau at threonine 181 and Ser199/Ser202 is varied within the astrocytes.
Discussion: Cellular signaling between autophagy and apoptosis is complex. Therefore, a dysfunction of mitochondria in these cells may be associated with the pathophysiology of neurological diseases.
Embargo Period
5-31-2022
Effect of sulforaphane on hyperphosphorylation of tau
Suwanee, GA
Introduction: Various biomarkers have been used to assess astrocyte toxicity. Tau aggregates are insoluble and associated with the pathological symptoms seen in neurodegenerative diseases. Substantial research on pathogenesis of Alzheimer's disease is focused on the buildup of beta-amyloid plaques and phosphorylated tau protein tangles, in which astrocytes are involved in the clearance of these plaques and tangles. It is possible that sulforaphane may positively alter Nuclear factor erythroid 2-related factor 2 (Nrf2), a transcription factor that is a key regulator of oxidative stress and neuroinflammation. Currently, sulforaphane is being examined for an ability to reduce hyperphosphorylation of tau in astrocytes under hypoglycemic conditions. Methods: To induce hyperphosphorylation of tau, an experimental model was developed to deprive rat hippocampal astrocytes of glucose in growth media. Embryonic hippocampal rat astrocytes were cultured in T75 Poly-D-Lysine flasks for 13 days before trypsinizing. The cells were then transitioned to a media containing 100% complete media (high-glucose DMEM and 10% fetal bovine serum). Visualizing tau microtubules in vitro was accomplished via utilization of antibodies specific to the tau protein and a Confocal Microscope. The phosphate groups that bind to the tau protein have been shown to attach to several amino acid residues (Friedhoff, et al. 2012). Serine and threonine are two amino acids that are associated with phosphorylation of tau. Experiments were performed to determine the possible role altered phosphorylated tau at threonine 181 and Ser199/Ser202 distribution within the astrocytes.
Results: Confocal microscopy revealed increased fluorescence due to hyperphosphorylated tau in DNA regions of cells exposed to less glucose. However, the distribution of phosphorylated tau at threonine 181 and Ser199/Ser202 is varied within the astrocytes.
Discussion: Cellular signaling between autophagy and apoptosis is complex. Therefore, a dysfunction of mitochondria in these cells may be associated with the pathophysiology of neurological diseases.