title: Low energy laser light (632.8 nm) suppresses amyloid-β peptide-induced oxidative and inflammatory responses in astrocytes.
abstract: Oxidative stress and inflammation are important processes in the progression of Alzheimer's disease (AD). Recent studies have implicated the role of amyloid β-peptides (Aβ) in mediating these processes. In astrocytes, oligomeric Aβ induces the assembly of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase complexes resulting in its activation to produce anionic superoxide. Aβ also promotes production of pro-inflammatory factors in astrocytes. Since low energy laser has previously been reported to attenuate oxidative stress and inflammation in biological systems, the objective of this study was to examine whether this type of laser light was able to abrogate the oxidative and inflammatory responses induced by Aβ. Primary rat astrocytes were exposed to Helium-Neon laser (λ=632.8 nm), followed by the treatment with oligomeric Aβ. Primary rat astrocytes were used to measure Aβ-induced production of superoxide anions using fluorescence microscopy of dihydroethidium (DHE), assembly of NADPH oxidase subunits by the colocalization between the cytosolic p47(phox) subunit and the membrane gp91(phox) subunit using fluorescent confocal microscopy, phosphorylation of cytosolic phospholipase A(2) cPLA(2) and expressions of pro-inflammatory factors including interleukin-1β (IL-1β) and inducible nitric-oxide synthase (iNOS) using Western blot Analysis. Our data showed that laser light at 632.8 nm suppressed Aβ-induced superoxide production, colocalization between NADPH oxidase gp91(phox) and p47(phox) subunits, phosphorylation of cPLA(2,) and the expressions of IL-1β and iNOS in primary astrocytes. We demonstrated for the first time that 632.8 nm laser was capable of suppressing cellular pathways of oxidative stress and inflammatory responses critical in the pathogenesis in AD. This study should prove to provide the groundwork for further investigations for the potential use of laser therapy as a treatment for AD.
authors.affiliation: Department of Biological Engineering, University of Missouri, Columbia, MO 65211, USA.
authors.forename: X
authors.initials: X
authors.lastname: Yang
authors.forename: S
authors.initials: S
authors.lastname: Askarova
authors.forename: W
authors.initials: W
authors.lastname: Sheng
authors.forename: J K
authors.initials: JK
authors.lastname: Chen
authors.forename: A Y
authors.initials: AY
authors.lastname: Sun
authors.forename: G Y
authors.initials: GY
authors.lastname: Sun
authors.forename: G
authors.initials: G
authors.lastname: Yao
authors.forename: J C-M
authors.initials: JC
authors.lastname: Lee
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology / Q000517:prevention & control; D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors* / Q000528:radiation effects* / Q000633:toxicity; D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000473:pathology* / Q000528:radiation effects*; D002478:Cells, Cultured; D002540:Cerebral Cortex / Q000378:metabolism / Q000473:pathology / Q000528:radiation effects; D004307:Dose-Response Relationship, Radiation; D018836:Inflammation Mediators / Q000037:antagonists & inhibitors* / Q000528:radiation effects / Q000633:toxicity*; D028022:Low-Level Light Therapy / Q000379:methods*; D018384:Oxidative Stress / Q000502:physiology / Q000528:radiation effects*; D010446:Peptide Fragments / Q000037:antagonists & inhibitors* / Q000528:radiation effects* / Q000633:toxicity; D051381:Rats; D013481:Superoxides / Q000037:antagonists & inhibitors / Q000378:metabolism
chemical_list: D016229:Amyloid beta-Peptides; D018836:Inflammation Mediators; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42); D013481:Superoxides