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

Stephanie Grillo, N. A. Duggett, A. Ennaceur, P. L. Chazot

Research output: Contribution to journalArticle

27 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)13-22
Number of pages10
JournalJournal of Photochemistry and Photobiology B: Biology
Volume123
DOIs
StatePublished - Jun 5 2013

Fingerprint

Amyloidogenic Proteins
Brain Diseases
brain
mice
therapy
Alzheimer Disease
Heat-Shock Proteins
proteins
Crystallins
Amyloid beta-Protein Precursor
Therapeutics
shock
heat
Western World
Proteins
Immunoblotting
Neurodegenerative Diseases
Cerebral Cortex
cerebral cortex
Dementia

All Science Journal Classification (ASJC) codes

  • Radiation
  • Radiological and Ultrasound Technology
  • Biophysics
  • Radiology Nuclear Medicine and imaging

Cite this

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title = "Non-invasive infra-red therapy (1072 nm) reduces β-amyloid protein levels in the brain of an Alzheimer's disease mouse model, TASTPM",
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.",
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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. / Grillo, Stephanie; Duggett, N. A.; Ennaceur, A.; Chazot, P. L.

In: Journal of Photochemistry and Photobiology B: Biology, Vol. 123, 05.06.2013, p. 13-22.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Non-invasive infra-red therapy (1072 nm) reduces β-amyloid protein levels in the brain of an Alzheimer's disease mouse model, TASTPM

AU - Grillo, Stephanie

AU - Duggett, N. A.

AU - Ennaceur, A.

AU - Chazot, P. L.

PY - 2013/6/5

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N2 - 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.

AB - 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.

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