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Prevention of beta-amyloid neurotoxi...

Seyb, Kathleen I.

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Prevention of beta-amyloid neurotoxicity by microtubule-stabilizing drugs: The calcium(2+) connection.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Prevention of beta-amyloid neurotoxicity by microtubule-stabilizing drugs: The calcium(2+) connection./
作者:	Seyb, Kathleen I.
面頁冊數:	130 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-09, Section: B, page: 4744.
Contained By:	Dissertation Abstracts International66-09B.
標題:	Health Sciences, Pharmacology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3190148
ISBN:	0542323788

Prevention of beta-amyloid neurotoxicity by microtubule-stabilizing drugs: The calcium(2+) connection.
Seyb, Kathleen I.

Prevention of beta-amyloid neurotoxicity by microtubule-stabilizing drugs: The calcium(2+) connection. - 130 p.

Source: Dissertation Abstracts International, Volume: 66-09, Section: B, page: 4744.

Thesis (Ph.D.)--The University of Kansas, 2005.

The complex pathology of Alzheimer's disease involves formation of two lesions in the brain: extracellular plaques of Abeta peptides and intracellular tangles of hyperphosphorylated tau protein. Application of Abeta to neurons in culture results increased cytosolic Ca2+, phosphorylation of tau, microtubule (MTs) disruption, and cell death. Treatment of neurons with MT-stabilizing drugs prevented both the increased tau phosphorylation and cell death induced by Abeta; however the mechanism by which this protection occurs remains unclear. There is some evidence that MT stability may be involved in Ca2+ regulation; therefore the current studies were performed to explore the role of MTs in pathways related to Ca2+ regulation and cell death. In particular the studies focused on ER dysfunction and calpain activation. Abeta treatment of neurons resulted in depletion of ER Ca 2+ stores and induction of the Unfolded Protein Response (UPR). Pretreatment of the neurons with MT-stabilizing drugs prevented induction of the UPR as well as toxicity by both Abeta and thapsigargin. This suggests that MT stability may be involved in regulation of ER Ca2+ stores.

ISBN: 0542323788Subjects--Topical Terms:

1017717
Health Sciences, Pharmacology.

Prevention of beta-amyloid neurotoxicity by microtubule-stabilizing drugs: The calcium(2+) connection.
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500 $a Adviser: Mary L. Michaelis.
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520 $a The complex pathology of Alzheimer's disease involves formation of two lesions in the brain: extracellular plaques of Abeta peptides and intracellular tangles of hyperphosphorylated tau protein. Application of Abeta to neurons in culture results increased cytosolic Ca2+, phosphorylation of tau, microtubule (MTs) disruption, and cell death. Treatment of neurons with MT-stabilizing drugs prevented both the increased tau phosphorylation and cell death induced by Abeta; however the mechanism by which this protection occurs remains unclear. There is some evidence that MT stability may be involved in Ca2+ regulation; therefore the current studies were performed to explore the role of MTs in pathways related to Ca2+ regulation and cell death. In particular the studies focused on ER dysfunction and calpain activation. Abeta treatment of neurons resulted in depletion of ER Ca 2+ stores and induction of the Unfolded Protein Response (UPR). Pretreatment of the neurons with MT-stabilizing drugs prevented induction of the UPR as well as toxicity by both Abeta and thapsigargin. This suggests that MT stability may be involved in regulation of ER Ca2+ stores.
520 $a The involvement of calpain in Abeta-induced tau phosphorylation and cell death was investigated using neurons lacking p35, a substrate for calpain and regulator of cdk5 activity.{09}In wild type neurons, the MT-stabilizing drug Taxol and low concentrations of exogenous ceramide prevented calpain activation, tau phosphorylation, and toxicity induced by Abeta. We expected that ablation of p35 would prevent activation of this pathway in neurons. However the results showed that Abeta still induced tau phosphorylation and toxicity. Pretreatment with Taxol prevented tau phosphorylation but did not protect against toxicity in p35-/- cells. These findings suggest that calpain-mediated cleavage of p35 is not required for prevention of tau phosphorylation but is essential for neuroprotection by Taxol. Interestingly, these data also suggest a divergence in the pathways resulting in tau phosphorylation and toxicity in the absence of p35. However, the protection afforded by Taxol against Abeta-induced calpain activation, tau phosphorylation, and cell death in the wild type neurons, as well as the prevention of activation of the UPR, indicates that MT stabilization may prevent Ca2+ dysregulation in Abeta-treated neurons.
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