Non-invasive infra-red therapy (1072 nm) reduces β-amyloid protein levels in the brain of an Alzheimer’s disease mouse model, TASTPM

Grillo, S.L., Duggett, N.A., Ennaceur, A. and Chazot, P.L. (2013) Non-invasive infra-red therapy (1072 nm) reduces β-amyloid protein levels in the brain of an Alzheimer’s disease mouse model, TASTPM. Journal of Photochemistry and Photobiology B: Biology, 123. pp. 13-22. ISSN 1011-1344

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Non-invasive_infra-red_therapy_(1072_nm)_reduces_β-amyloid_protein_levels_in_the_brain_of_an_Alzheimer’s_disease_mouse_model,_TASTPM.pdf - Published Version
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Abstract

Background
Alzheimer’s disease (AD) is the most prevalent neurodegenerative disease and common cause of dementias in the Western world. This study investigated the expression profile of heat-shock proteins (HSPs) involved in maintaining healthy neurons in the TASTPM AD mouse model, and whether chronic treatment with 1072 nm infra-red (IR1072) modified the expression profiles of HSPs and amyloidopathy in female TASTPM mice.

Methodology/principal findings
Quantitative immunoblotting and immunohistochemistry were used to examine the expression of proteins such as HSPs, phosphorylated tau (tau-P), amyloid precursor protein (APP), β-amyloid1–40 (Aβ), and Aβ1–42. TASTPM mice at 3, 7 and 12 months were investigated as well as female TASTPM mice which had undergone a chronic, 5 month, IR1072 treatment. During the first 12 months of age, a critical period of AD progression, reduced HSP40 and HSP105 were observed. αB-crystallin, Aβ1–42 and tau-P increased over this period, particularly between 3 and 7 months. Chronic IR1072 treatment of female TASTPM mice elicited significant increases in HSP60, 70 and 105 and phosphorylated-HSP27 (P-HSP27) (50–139%), together with a concomitant profound decrease in αB-crystallin, APP, tau-P, Aβ1–40 and Aβ1–42 (43–81%) protein levels at 7 months of age. Furthermore, IR1072 treatment elicited a modest, but significant, reduction in Aβ1–42 plaques in the cerebral cortex.

Conclusions/significant findings
IR1072 treatment provides a novel non-invasive and safe way to upregulate a panel of stress response proteins in the brain, known to both reduce protein aggregation and neuronal apoptosis. This approach recently entered clinical trials for AD in the USA, and may provide a novel disease modifying therapy for a range of neuropathologies.

Item Type: Article
Subjects: Sciences > Biomedical Sciences
Sciences > Health Sciences
Psychology > Neuropsychology
Sciences > Pharmacy and Pharmacology
Divisions: Faculty of Applied Sciences > Department of Pharmacy Health and Wellbeing
Related URLs:
Depositing User: Abdelkader Ennaceur
Date Deposited: 09 May 2013 10:28
Last Modified: 09 Mar 2017 15:40
URI: http://sure.sunderland.ac.uk/id/eprint/3907

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