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Phosphorylation and sequence depende...

Liu, Quan.

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Phosphorylation and sequence dependency of neurofilament protein oxidative modification in Alzheimer disease.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Phosphorylation and sequence dependency of neurofilament protein oxidative modification in Alzheimer disease./
作者:	Liu, Quan.
面頁冊數:	243 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0111.
Contained By:	Dissertation Abstracts International66-01B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3159437
ISBN:	0496932519

Phosphorylation and sequence dependency of neurofilament protein oxidative modification in Alzheimer disease.
Liu, Quan.

Phosphorylation and sequence dependency of neurofilament protein oxidative modification in Alzheimer disease. - 243 p.

Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0111.

Thesis (Ph.D.)--Case Western Reserve University, 2005.

Protein adducts of the lipid peroxidation product 4-hydroxy-2-nonenal (HNE) are prominent features of oxidative damage in neuronal cell bodies in Alzheimer disease (AD). Such adducts are also seen in axons of normal as well as diseased individuals. These HNE adducts are constant throughout the axons and the aging process of humans, mice, and rats, indicating that HNE adduction is physiological and regulated from birth to senility. In axons, HNE is primarily adducted to the neurofilament heavy subunit (NFH) and the neurofilament medium subunit (NFM), and limited to lysine residues. Interestingly, we found that phosphorylation is essential since formation and removal of HNE adducts are controlled by the NFH/M phosphorylation state. Studies using immunochemistry, synthetic peptides, mass spectrometry and chemical stabilization of HNE adducts, demonstrated that XKSPX, the most repeated sequences in NFH/M, are the major component in neurons highly susceptible to phosphorylation regulated aldehyde adduction. To our knowledge, this is the first study to directly show phosphorylation can regulate NFH-HNE levels in axons and the multiple KSP repeats are the critical motifs which preserve the phosphorylation-dependent regulation. This study provides the new evidence that indicates signal transduction could modulate oxidative modification in brain through activation of kinases and phosphatases.

ISBN: 0496932519Subjects--Topical Terms:

1017719
Biology, Molecular.

Phosphorylation and sequence dependency of neurofilament protein oxidative modification in Alzheimer disease.
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520 $a Protein adducts of the lipid peroxidation product 4-hydroxy-2-nonenal (HNE) are prominent features of oxidative damage in neuronal cell bodies in Alzheimer disease (AD). Such adducts are also seen in axons of normal as well as diseased individuals. These HNE adducts are constant throughout the axons and the aging process of humans, mice, and rats, indicating that HNE adduction is physiological and regulated from birth to senility. In axons, HNE is primarily adducted to the neurofilament heavy subunit (NFH) and the neurofilament medium subunit (NFM), and limited to lysine residues. Interestingly, we found that phosphorylation is essential since formation and removal of HNE adducts are controlled by the NFH/M phosphorylation state. Studies using immunochemistry, synthetic peptides, mass spectrometry and chemical stabilization of HNE adducts, demonstrated that XKSPX, the most repeated sequences in NFH/M, are the major component in neurons highly susceptible to phosphorylation regulated aldehyde adduction. To our knowledge, this is the first study to directly show phosphorylation can regulate NFH-HNE levels in axons and the multiple KSP repeats are the critical motifs which preserve the phosphorylation-dependent regulation. This study provides the new evidence that indicates signal transduction could modulate oxidative modification in brain through activation of kinases and phosphatases.
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