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S-nitrosylated glyceraldehyde-3-phos...

Hara, Makoto.

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S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding./
作者:	Hara, Makoto.
面頁冊數:	78 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5836.
Contained By:	Dissertation Abstracts International66-11B.
標題:	Biology, Neuroscience. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197160
ISBN:	9780542429729

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.
Hara, Makoto.

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding. - 78 p.

Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5836.

Thesis (Ph.D.)--The Johns Hopkins University, 2006.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a classical glycolytic protein known for its pivotal role in energy production. Recent evidence demonstrates that mammalian GAPDH displays a number of diverse activities unrelated to its glycolytic function, including its possible role in apoptosis. Our laboratory has found that GAPDH translocates to the nucleus following a wide range of apoptotic stimuli1. Antisense oligonucleotides targeted to GAPDH decrease nuclear GAPDH and prevent cell death. This thesis attempts to study a mechanism underlying this nuclear translocation and cytotoxicity. GAPDH, which lacks a nuclear localization signal (NLS), bind to the NLS-containing protein Siahl (an E3-ubiquitin-ligase), which mediates GAPDH's nuclear translocation. Nitric oxide (NO) generation following apoptotic stimulation elicits S-nitrosylation of GAPDH, which augments its binding to Siahl. GAPDH stabilizes Siahl facilitating its degradation of nuclear proteins. Activation of macrophages by endotoxin and of neurons by glutamate elicits GAPDH-Siahl binding, nuclear translocation and apoptosis, which are prevented by NO deletion. The NO-S-nitrosylation-GAPDH-Siahl cascade may represent a major molecular mechanism of cytotoxicity.

ISBN: 9780542429729Subjects--Topical Terms:

1017680
Biology, Neuroscience.

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.
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