Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

Hideko Kokubo; Rakez Kayed; Charles G. Glabe; Takaomi C. Saido; Nobuhisa Iwata; J. Bernd Helms; Haruyasu Yamaguchi

doi:10.1016/j.brainres.2005.03.017

Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

Hideko Kokubo
, Rakez Kayed
, Charles G. Glabe
, Takaomi C. Saido
, Nobuhisa Iwata
, J. Bernd Helms
, Haruyasu Yamaguchi

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

19 Scopus citations

Abstract

We examined the ultrastructural localization of oligomeric proteins, Aβ42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1- immunoreactive rafts than Aβ42, suggesting that rafts are one of the sites of polymeric Aβ deposition, but not of oligomeric proteins including Aβ.

Original language	English (US)
Pages (from-to)	224-228
Number of pages	5
Journal	Brain Research
Volume	1045
Issue number	1-2
DOIs	https://doi.org/10.1016/j.brainres.2005.03.017
State	Published - May 31 2005
Externally published	Yes

Keywords

Alzheimer's disease
Amyloid-β
Flotillin-1
Oligomer
Raft
Tg2576 mouse

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
Clinical Neurology
Developmental Biology

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10.1016/j.brainres.2005.03.017

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title = "Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain",

abstract = "We examined the ultrastructural localization of oligomeric proteins, Aβ42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1- immunoreactive rafts than Aβ42, suggesting that rafts are one of the sites of polymeric Aβ deposition, but not of oligomeric proteins including Aβ.",

keywords = "Alzheimer's disease, Amyloid-β, Flotillin-1, Oligomer, Raft, Tg2576 mouse",

author = "Hideko Kokubo and Rakez Kayed and Glabe, \{Charles G.\} and Saido, \{Takaomi C.\} and Nobuhisa Iwata and Helms, \{J. Bernd\} and Haruyasu Yamaguchi",

note = "Funding Information: The authors thank Dr. Karen Hsiao-Ashe (Department of Neurology, University of Minnesota) for kindly providing Tg2576 mice. The authors also thank R. Shinohara for technical assistance. HK also thanks Dr. M. Takatama and senior physical therapists in Geriatrics Research Institute Hospital for generous support. H. Yamaguchi was supported by a Grant-in-Aid for Scientific Research and that for Priority Areas from the Ministry of Education, Science, Sports, Culture and Technology, Japan, and Life Science Research Foundation of Japan.",

year = "2005",

month = may,

day = "31",

doi = "10.1016/j.brainres.2005.03.017",

language = "English (US)",

volume = "1045",

pages = "224--228",

journal = "Brain Research",

issn = "0006-8993",

publisher = "Elsevier B.V.",

number = "1-2",

}

TY - JOUR

T1 - Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

AU - Kokubo, Hideko

AU - Kayed, Rakez

AU - Glabe, Charles G.

AU - Saido, Takaomi C.

AU - Iwata, Nobuhisa

AU - Helms, J. Bernd

AU - Yamaguchi, Haruyasu

N1 - Funding Information: The authors thank Dr. Karen Hsiao-Ashe (Department of Neurology, University of Minnesota) for kindly providing Tg2576 mice. The authors also thank R. Shinohara for technical assistance. HK also thanks Dr. M. Takatama and senior physical therapists in Geriatrics Research Institute Hospital for generous support. H. Yamaguchi was supported by a Grant-in-Aid for Scientific Research and that for Priority Areas from the Ministry of Education, Science, Sports, Culture and Technology, Japan, and Life Science Research Foundation of Japan.

PY - 2005/5/31

Y1 - 2005/5/31

N2 - We examined the ultrastructural localization of oligomeric proteins, Aβ42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1- immunoreactive rafts than Aβ42, suggesting that rafts are one of the sites of polymeric Aβ deposition, but not of oligomeric proteins including Aβ.

AB - We examined the ultrastructural localization of oligomeric proteins, Aβ42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1- immunoreactive rafts than Aβ42, suggesting that rafts are one of the sites of polymeric Aβ deposition, but not of oligomeric proteins including Aβ.

KW - Alzheimer's disease

KW - Amyloid-β

KW - Flotillin-1

KW - Oligomer

KW - Raft

KW - Tg2576 mouse

UR - https://www.scopus.com/pages/publications/19444371852

UR - https://www.scopus.com/pages/publications/19444371852#tab=citedBy

U2 - 10.1016/j.brainres.2005.03.017

DO - 10.1016/j.brainres.2005.03.017

M3 - Article

C2 - 15910781

AN - SCOPUS:19444371852

SN - 0006-8993

VL - 1045

SP - 224

EP - 228

JO - Brain Research

JF - Brain Research

IS - 1-2

ER -

Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain

Abstract

Keywords

ASJC Scopus subject areas

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