Internalized antibodies to the Aβ domain of APP reduce neuronal Aβ and protect against synaptic alterations
Tampellini, Davide LU ; Magrané, Jordi ; Takahashi, Reisuke H. ; Li, Feng ; Lin, Michael T. ; Almeida, Cláudia G. and Gouras, Gunnar K. LU
(2007)
In Journal of Biological Chemistry
282(26).
p.18895-18906
- Abstract
Immunotherapy against β-amyloid peptide (Aβ) is a leading therapeutic direction for Alzheimer disease (AD). Experimental studies in transgenic mouse models of AD have demonstrated that Aβ immunization reduces Aβ plaque pathology and improves cognitive function. However, the biological mechanisms by which Aβ antibodies reduce amyloid accumulation in the brain remain unclear. We provide evidence that treatment of AD mutant neuroblastoma cells or primary neurons with Aβ antibodies decreases levels of intracellular Aβ. Antibody-mediated reduction in cellular Aβ appears to require that the antibody binds to the extracellular Aβ domain of the amyloid precursor protein (APP) and be internalized. In addition, treatment with Aβ antibodies... (More)
Immunotherapy against β-amyloid peptide (Aβ) is a leading therapeutic direction for Alzheimer disease (AD). Experimental studies in transgenic mouse models of AD have demonstrated that Aβ immunization reduces Aβ plaque pathology and improves cognitive function. However, the biological mechanisms by which Aβ antibodies reduce amyloid accumulation in the brain remain unclear. We provide evidence that treatment of AD mutant neuroblastoma cells or primary neurons with Aβ antibodies decreases levels of intracellular Aβ. Antibody-mediated reduction in cellular Aβ appears to require that the antibody binds to the extracellular Aβ domain of the amyloid precursor protein (APP) and be internalized. In addition, treatment with Aβ antibodies protects against synaptic alterations that occur in APP mutant neurons.
(Less)
- author
- Tampellini, Davide
LU
; Magrané, Jordi
; Takahashi, Reisuke H.
; Li, Feng
; Lin, Michael T.
; Almeida, Cláudia G.
and Gouras, Gunnar K.
LU
- publishing date
- 2007-06-29
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 282
- issue
- 26
- pages
- 18895 - 18906
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:34547110577
- pmid:17468102
- ISSN
- 0021-9258
- DOI
- 10.1074/jbc.M700373200
- language
- English
- LU publication?
- no
- id
- 47966b80-03c2-48da-8af1-ca008e7764d4
- date added to LUP
- 2020-02-20 14:21:07
- date last changed
- 2024-05-15 15:47:59
@article{47966b80-03c2-48da-8af1-ca008e7764d4,
abstract = {{<p>Immunotherapy against β-amyloid peptide (Aβ) is a leading therapeutic direction for Alzheimer disease (AD). Experimental studies in transgenic mouse models of AD have demonstrated that Aβ immunization reduces Aβ plaque pathology and improves cognitive function. However, the biological mechanisms by which Aβ antibodies reduce amyloid accumulation in the brain remain unclear. We provide evidence that treatment of AD mutant neuroblastoma cells or primary neurons with Aβ antibodies decreases levels of intracellular Aβ. Antibody-mediated reduction in cellular Aβ appears to require that the antibody binds to the extracellular Aβ domain of the amyloid precursor protein (APP) and be internalized. In addition, treatment with Aβ antibodies protects against synaptic alterations that occur in APP mutant neurons.</p>}},
author = {{Tampellini, Davide and Magrané, Jordi and Takahashi, Reisuke H. and Li, Feng and Lin, Michael T. and Almeida, Cláudia G. and Gouras, Gunnar K.}},
issn = {{0021-9258}},
language = {{eng}},
month = {{06}},
number = {{26}},
pages = {{18895--18906}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Internalized antibodies to the Aβ domain of APP reduce neuronal Aβ and protect against synaptic alterations}},
url = {{http://dx.doi.org/10.1074/jbc.M700373200}},
doi = {{10.1074/jbc.M700373200}},
volume = {{282}},
year = {{2007}},
}