Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease

Jae Kwang Jin; Bong Hyun Ahn; Yeo Jung Na; Jae Il Kim; Yong Sun Kim; Eun Kyoung Choi; Young Gyu Ko; Kwang Chul Chung; Piotr B. Kozlowski; Do Sik Min

doi:10.1016/j.neurobiolaging.2006.05.022

Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease

Jae Kwang Jin, Bong Hyun Ahn, Yeo Jung Na, Jae Il Kim, Yong Sun Kim, Eun Kyoung Choi, Young Gyu Ko, Kwang Chul Chung, Piotr B. Kozlowski, Do Sik Min

Research output: Contribution to journal › Article › peer-review

38 Citations (Scopus)

Abstract

Amyloid precursor protein (APP) is a widely expressed transmembrane protein of unknown function that is involved in the pathogenesis of Alzheimer's disease (AD). We investigated the involvement of phospholipase D (PLD) in the pathophysiology of AD. We showed dramatic upregulation of PLD1 immunoreactivity in reactive astroglial cells in brain tissue sections from authentic AD patients. Expression and activity of PLD1 were up-regulated in brain tissues from AD patients, especially caveolae membrane fraction, compared with those of control brains. Interestingly, PLD1 physically interacts and colocalizes with APP and caveolin-3. We found that APP was associated with the pleckstrin homology domain of PLD1, and the amyloid region of APP interacted with PLD. Elevated expression of APP stimulated PLD activity in human astroglioma cells. These results suggest that up-regulation of PLD might have a role in the neuronal pathology associated with AD.

Original language	English
Pages (from-to)	1015-1027
Number of pages	13
Journal	Neurobiology of Aging
Volume	28
Issue number	7
DOIs	https://doi.org/10.1016/j.neurobiolaging.2006.05.022
Publication status	Published - 2007 Jul

Bibliographical note

Funding Information:
This study was supported by grant No. R01-2006-000-10521-0 (2006) from the Basic Research Program of the Korea Science & Engineering Foundation and by the Biotechnology Development Program (grant number 2005-00115) from Ministry of Science and Technology (MOST), Korea and grant of the Korea Health 21 R&D project, Ministry of Health and Welfare, Republic of Korea (A020007). A total of six post-mortem brain specimens of Alzheimer's disease patients and age-matched controls were obtained from the IBR Brain Bank (Dr. Piotr B. Kozlowski, who is head of New York IBR brain bank and co-author of this manuscript). So, we used post-mortem brain specimens of Alzheimer's disease patients according to appropriate approval and procedure.

Keywords

Alzheimer's disease
Amyloid precursor protein
Caveolin
Phospholipase D
Reactive astrocytes
β-Amyloid

ASJC Scopus subject areas

General Neuroscience
Ageing
Clinical Neurology
Developmental Biology
Geriatrics and Gerontology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.neurobiolaging.2006.05.022

Cite this

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title = "Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease",

abstract = "Amyloid precursor protein (APP) is a widely expressed transmembrane protein of unknown function that is involved in the pathogenesis of Alzheimer's disease (AD). We investigated the involvement of phospholipase D (PLD) in the pathophysiology of AD. We showed dramatic upregulation of PLD1 immunoreactivity in reactive astroglial cells in brain tissue sections from authentic AD patients. Expression and activity of PLD1 were up-regulated in brain tissues from AD patients, especially caveolae membrane fraction, compared with those of control brains. Interestingly, PLD1 physically interacts and colocalizes with APP and caveolin-3. We found that APP was associated with the pleckstrin homology domain of PLD1, and the amyloid region of APP interacted with PLD. Elevated expression of APP stimulated PLD activity in human astroglioma cells. These results suggest that up-regulation of PLD might have a role in the neuronal pathology associated with AD.",

keywords = "Alzheimer's disease, Amyloid precursor protein, Caveolin, Phospholipase D, Reactive astrocytes, β-Amyloid",

author = "Jin, {Jae Kwang} and Ahn, {Bong Hyun} and Na, {Yeo Jung} and Kim, {Jae Il} and Kim, {Yong Sun} and Choi, {Eun Kyoung} and Ko, {Young Gyu} and Chung, {Kwang Chul} and Kozlowski, {Piotr B.} and Min, {Do Sik}",

note = "Funding Information: This study was supported by grant No. R01-2006-000-10521-0 (2006) from the Basic Research Program of the Korea Science & Engineering Foundation and by the Biotechnology Development Program (grant number 2005-00115) from Ministry of Science and Technology (MOST), Korea and grant of the Korea Health 21 R&D project, Ministry of Health and Welfare, Republic of Korea (A020007). A total of six post-mortem brain specimens of Alzheimer's disease patients and age-matched controls were obtained from the IBR Brain Bank (Dr. Piotr B. Kozlowski, who is head of New York IBR brain bank and co-author of this manuscript). So, we used post-mortem brain specimens of Alzheimer's disease patients according to appropriate approval and procedure.",

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language = "English",

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AU - Jin, Jae Kwang

AU - Ahn, Bong Hyun

AU - Na, Yeo Jung

AU - Kim, Jae Il

AU - Kim, Yong Sun

AU - Choi, Eun Kyoung

AU - Ko, Young Gyu

AU - Chung, Kwang Chul

AU - Kozlowski, Piotr B.

AU - Min, Do Sik

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PY - 2007/7

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N2 - Amyloid precursor protein (APP) is a widely expressed transmembrane protein of unknown function that is involved in the pathogenesis of Alzheimer's disease (AD). We investigated the involvement of phospholipase D (PLD) in the pathophysiology of AD. We showed dramatic upregulation of PLD1 immunoreactivity in reactive astroglial cells in brain tissue sections from authentic AD patients. Expression and activity of PLD1 were up-regulated in brain tissues from AD patients, especially caveolae membrane fraction, compared with those of control brains. Interestingly, PLD1 physically interacts and colocalizes with APP and caveolin-3. We found that APP was associated with the pleckstrin homology domain of PLD1, and the amyloid region of APP interacted with PLD. Elevated expression of APP stimulated PLD activity in human astroglioma cells. These results suggest that up-regulation of PLD might have a role in the neuronal pathology associated with AD.

AB - Amyloid precursor protein (APP) is a widely expressed transmembrane protein of unknown function that is involved in the pathogenesis of Alzheimer's disease (AD). We investigated the involvement of phospholipase D (PLD) in the pathophysiology of AD. We showed dramatic upregulation of PLD1 immunoreactivity in reactive astroglial cells in brain tissue sections from authentic AD patients. Expression and activity of PLD1 were up-regulated in brain tissues from AD patients, especially caveolae membrane fraction, compared with those of control brains. Interestingly, PLD1 physically interacts and colocalizes with APP and caveolin-3. We found that APP was associated with the pleckstrin homology domain of PLD1, and the amyloid region of APP interacted with PLD. Elevated expression of APP stimulated PLD activity in human astroglioma cells. These results suggest that up-regulation of PLD might have a role in the neuronal pathology associated with AD.

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Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

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