The difference in gliosis induced by β-amyloid and Tau treatments in astrocyte cultures derived from senescence accelerated and normal mouse strains.
Astrocytes react to various neurodegenerative insults rapidly and undergo changes known as gliosis or astrogliosis. In Alzheimer's disease (AD), a wall of reactive astrocytes surrounds senile plaques of β-amyloid (Aβ) and might play an important role in clearing of Aβ. AD is neuropathologically characterized by the co-existence of two pathological structures, senile plaques and neurofibrillary tangles composed of Aβ and Tau protein respectively. However, the molecular mechanisms underlie astrogliosis and increased expressions of GFAP and other astrogliosis markers are poorly understood. Since AD is age related, the aim of this study is to compare the gliosis of aging prone astrocytes cultured from senescence-accelerated mice and astrocytes from normal mice in response to Aβ and Tau treatment. Our results demonstrated that the aging prone astrocytes have showed larger degree of gliosis than normal astrocytes. Since reactive astrocytes had less ability to support co-cultured neurons as compared with control astrocytes. Therefore, it is likely that aging prone astrocytes might contribute to cell loss or dysfunction associated with insults in AD. In other words, aging prone astrocytes might have decreased ability than normal astrocytes to protect or prevent neuronal dysfunction in AD pathology. In addition, further AD related studies should use aging prone astrocytes instead of normal astrocytes.
Lü
Lanhai
L
Department of Anatomy, School of Medicine, Sun Yat-sen University, Guangzhou, People's Republic of China.
Mak
Ying T
YT
Fang
Marong
M
Yew
David T
DT
D019588:Aging, Premature / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000818:Animals; D001253:Astrocytes / Q000378:metabolism* / Q000473:pathology; D015415:Biomarkers / Q000378:metabolism; D015153:Blotting, Western; D053148:Caspase 3 / Q000378:metabolism; D002478:Cells, Cultured; D016922:Cellular Senescence / Q000187:drug effects; D004195:Disease Models, Animal; D005904:Glial Fibrillary Acidic Protein; D005911:Gliosis / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D006593:Hexokinase / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D051379:Mice; D008817:Mice, Mutant Strains; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009414:Nerve Growth Factors / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins / Q000378:metabolism; D016875:tau Proteins / Q000378:metabolism*
D016229:Amyloid beta-Peptides; D015415:Biomarkers; D005904:Glial Fibrillary Acidic Protein; D008869:Microtubule-Associated Proteins; C079240:Mtap2 protein, mouse; D009414:Nerve Growth Factors; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins; C075222:amyloid beta-protein (1-42); C528900:glial fibrillary astrocytic protein, mouse; D016875:tau Proteins; D007770:L-Lactate Dehydrogenase; C515658:HK1 protein, mouse; D006593:Hexokinase; D011493:Protein Kinase C; C505409:Casp3 protein, mouse; D053148:Caspase 3