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The Role of Amyloid Precursor Protei...

Midthune, Brea June.

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The Role of Amyloid Precursor Protein in Amyloid-Beta-Mediated Synaptic Dysfunction.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	The Role of Amyloid Precursor Protein in Amyloid-Beta-Mediated Synaptic Dysfunction./
作者:	Midthune, Brea June.
面頁冊數:	117 p.
附註:	Source: Dissertation Abstracts International, Volume: 74-02(E), Section: B.
Contained By:	Dissertation Abstracts International74-02B(E).
標題:	Biology, Neurobiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3527670
ISBN:	9781267620897

The Role of Amyloid Precursor Protein in Amyloid-Beta-Mediated Synaptic Dysfunction.
Midthune, Brea June.

The Role of Amyloid Precursor Protein in Amyloid-Beta-Mediated Synaptic Dysfunction. - 117 p.

Source: Dissertation Abstracts International, Volume: 74-02(E), Section: B.

Thesis (Ph.D.)--University of California, San Diego, 2012.

Amyloid precursor protein (APP) is a type one transmembrane protein and has two mammalian homologues, amyloid precursor-like protein 1 (APLP1) and amyloid precursor-like protein 2 (APLP2). APP is the parent molecule to amyloid-beta (Abeta), the amyloidogenic species found in the plaques of people with Alzheimer's disease (AD). Several lines of evidence suggest Abeta to lie at the center of AD pathology, with converging evidence to indicate that synapses are the site of the initial damage.

ISBN: 9781267620897Subjects--Topical Terms:

1681328
Biology, Neurobiology.

The Role of Amyloid Precursor Protein in Amyloid-Beta-Mediated Synaptic Dysfunction.
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520 $a Amyloid precursor protein (APP) is a type one transmembrane protein and has two mammalian homologues, amyloid precursor-like protein 1 (APLP1) and amyloid precursor-like protein 2 (APLP2). APP is the parent molecule to amyloid-beta (Abeta), the amyloidogenic species found in the plaques of people with Alzheimer's disease (AD). Several lines of evidence suggest Abeta to lie at the center of AD pathology, with converging evidence to indicate that synapses are the site of the initial damage.
520 $a Recent studies have shown that APP may be necessary for the toxicity induced by Abeta, in part by cleavage of a caspase site on the intracellular domain of the APP protein and the subsequent release of the toxic molecule, C31. This caspase cleavage is shown to induce APP-mediated Abeta toxicity in cell culture models, however assays were based on contribution to cell death. Thus, the physiologic relevance of the cleavage event has never been tested and in particular, whether this pathway contributes to synaptic damage is unclear.
520 $a Here, we seek to test the role of caspase cleavage of APP in Abeta-induced synaptic damage and to test the specificity of this event by testing whether caspase cleavage of APLP2, the protein most homologous to APP, also contributes to these Abeta-driven synaptic changes. Additionally, because APP dimerization was shown to be necessary for the Abeta-induced caspase cleavage of APP and subsequent release of C31, we wanted to test the effects of dimerization on APP proteolysis and Abeta production.
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