Antioxidant effects of curcumin in models of neurodegeneration, aging, oxidative and nitrosative stress: A review. (15th May 2019)

• Record Type: Journal Article
• Authors: Abrahams, Shameemah; Haylett, William L.; Johnson, Glynis; Carr, Jonathan A.; Bardien, Soraya
• Is Part Of: Neuroscience. Volume 406(2019)
• Page Start: 1
• Page End: 21
• Publication Date: 2019-05-15
• Subjects: 3-NP 3-nitropropionic acid -- 6-OHDA 6-hydroxydopamine -- Aβ40 or Aβ42 40- or 42-amino acid amyloid-β peptide -- A172 human glioma cells -- A53T point-mutation resulting in alanine to threonine change at amino acid 53 of α-synuclein -- AD Alzheimer's disease -- Akt serine/threonine protein kinase B -- AKR1B4 aldo-keto reductase family 1, member B4 -- AKR1B8 aldo-keto reductase family 1, member B8 -- ALAS1 5′-aminolevulinate synthase 1 -- AlCl3 aluminum chloride -- AP-1 activated protein 1 -- APE1 apurinic/apyrimidinic endonuclease -- AOX1 aldehyde oxidase 1 -- APP amyloid precursor protein -- ARE antioxidant responsive element -- b.w. body weight -- C6 rat glioma cells -- Ca2+ calcium -- CAT catalase -- curcumin D1 di-piperoyl -- CoCl2 cobalt chloride -- Cu(II) copper(II) -- curcumin D2 di-valinoyl -- curcumin D3 di-glutamoyl -- DAF-FM DA 4-Amino-5-methylamino-2′, 7′-difluorofluorescein diacetate -- DCHF-DA dichlorodihydrofluorescein diacetate -- DHR123 dihydrorhodamine 123 -- DMC demethoxycurcumin -- DMSO dimethyl sulfoxide -- DNPH 2, 4-dinitrophenylhydrazine -- DPPH 2, 2-diphenyl-1-picryl-hydrazyl-hydrate -- DTNB 5, 5-dithio-bis-(2-nitrobenzoic acid) or Ellman's reagent -- ELISA enzyme-linked immunosorbent assay -- FRAP ferric reducing antioxidant power -- G6PD glucose-6-phosphate dehydrogenase -- GAPDH glyceraldehyde 3-phosphate dehydrogenase -- GFAP glial fibrillary acidic protein -- GFP green fluorescent protein -- GGT1 gamma-glutamyltransferase 1 -- GPx glutathione peroxidase -- GR glutathione reductase -- GSH glutathione -- GST glutathione S-transferase -- GSTA5 glutathione S-transferase alpha 5 -- GSTD1 glutathione S-transferase D1 -- GSTP1 glutathione S-transferase pi 1 -- h hours -- H2O2 hydrogen peroxide -- HA-sp human spinal cord-derived astrocytes -- HD Huntington's disease -- HEK293 human kidney cells -- HFP hydroxyl radical and peroxynitrite sensor -- HMOX1 heme oxygenase 1 -- HNE 4-hydroxy-2-nonenal -- HT22 mouse hippocampal cells -- ICV-STZ intracerebroventricular–streptozotocin -- IκBα inhibitors-of-kappaB -- IL-6 interleukin-6 -- IMR-32 human brain neuroblastoma cells -- iNOS inducible nitrogen oxide synthase -- i.p. intraperitoneally -- LC liquid chromatography -- LPO malondialdehyde-thiobarbituric assay -- LPS lipopolysaccharide -- LRRK2 leucine-rich repeat kinase 2 -- MAPK mitogen-activated protein kinases -- MDA malondialdehyde -- MGST1 microsomal glutathione S-transferase 1 -- min minutes -- MnCl2 manganese chloride -- MPP+ 1-methyl-4-phenylpyridinium -- MPTP 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine -- MS multiple sclerosis -- MS/MS tandem mass spectrometry -- mth methuselah -- N27 rat dopaminergic neurons -- N9 mouse microglia -- NDD neurodegenerative disorder -- Neuro-2a mouse neuroblastoma cells -- NF-κB nuclear-factor κB -- NGF nerve growth factor -- NMDA N-methyl-D-aspartate -- NQO1 NAD(P)H quinone dehydrogenase 1 -- NO nitric oxide -- NO2 nitrogen dioxide -- N2O3 dinitrogen trioxide -- NR8383 gerbil macrophages -- Nrf1/2 nuclear factor-E2-related factor 1/2 -- O2− superoxide anion -- O2−2 peroxide -- OH hydroxyl radical -- OLN-93 rat oligodendrocytes -- PC12 rat pheochromocytoma cells -- PD Parkinson's disease -- Plp1 proteolipid protein 1 -- PN peroxynitrate -- p.o. per os/orally ingested -- ppm parts per million -- Rh-123 rhodamine 123 -- RNS reactive nitrogen species -- ROS reactive oxygen species -- RT-PCR real time polymerase chain reaction -- SAMP8 senescence accelerated mouse-prone 8 -- SAMR1 senescence-resistant 1 mice -- s.c. subcutaneous injection -- SH-SY5Y and SK-N-SH human bone marrow neuroblastoma cells -- SMA spinal muscular atrophy -- SMN survival of motor neuron -- SOD superoxide dismutase -- SOD1/2 superoxide dismutase 1/2 -- TAC total antioxidant capacity -- TBA thiobarbituric acid -- TBARS thiobarbituric acid-reactive substances -- t-BHP tert-Butyl hydroperoxide -- TEAC trolox equivalent antioxidant capacity assay -- TNF-α tumor necrosis factor α -- TRPM2 transient receptor potential cation subfamily M, member 2, channel -- TTCA trichloroacetic acid assay -- WST cell proliferation assay -- w/v percent weight/volume -- w/w percent mass; curcumin -- neurodegenerative disorders -- antioxidant -- oxidative stress -- nitrosative stress -- curcumin derivatives; Neurochemistry -- Periodicals; Neurophysiology -- Periodicals; Neurology -- Periodicals; Neurochimie -- Périodiques; Neurophysiologie -- Périodiques; Neurochemistry; Neurophysiology; Electronic journals; Periodicals; Electronic journals; 612.8
• DOI: 10.1016/j.neuroscience.2019.02.020
• Languages: English
• ISSNs: 0306-4522

Abstract

Abstract: The global burden of neurodegenerative disorders has increased substantially over the past 2 decades due to rising rates of population aging. Although neurodegenerative disorders differ in their clinical presentation, the underlying pathobiological processes are largely shared. Oxidative stress, among other mechanisms, is strongly implicated in neurodegenerative disorders and aging, and can potentially be targeted by antioxidative agents. Curcumin, a component of turmeric, is a compound that has received considerable attention for its therapeutic properties, and it is considered to be a powerful antioxidant. In this review, we analyzed the evidence for curcumin as an antioxidant in models of neurodegenerative disorders as well as oxido-nitrosative stress. A total of 1451 articles were found from 3 scientific literature databases (PubMed, Scopus, and Web of Science). After all exclusions, a final total of 64 articles were included in this review. The majority of the studies showed that curcumin, or derivatives thereof, were protective against oxidative and/or nitrosative stress in various cellular and animal models. Overall, curcumin protected against lipid and protein oxidation with a reduction in levels of malondialdehyde, and protein carbonyls, thiols and nitrotyrosines. Furthermore, it stimulated the activities of antioxidant enzymes such as superoxide dismutase and glutathione peroxidase. In conclusion, curcumin appears to be a promising compound for phytomedicine. However, due to some concerns about its efficacy, further targeted experiments are needed to identify its exact molecular targets and pathways responsible for its antioxidant effects. Highlights: 64 relevant articles were found in animal and cellular models of neurodegeneration, aging and oxido-nitrosative stress. The majority of studies showed curcumin alleviated oxidative stress under a wide range of experimental conditions. Curcumin inhibited lipid and protein oxidation by suppressing malondialdehyde and protein carbonyls. Curcumin stimulated the activities of various antioxidant enzymes, including superoxide dismutase and catalase.