Abstract
Alzheimer’s disease (AD) is characterized clinically by progressive cognitive decline and pathologically by the accumulation of amyloid-β (Aβ) in the brain. Royal jelly (RJ), a secretion of honeybee hypopharyngeal and mandibular glands, has previously been shown to have anti-aging and neuromodulatory activities. In this study, we discovered that 3 months of RJ treatment substantially ameliorated behavioral deficits of APP/PS1 mice in the Morris Water Maze (MWM) test and step-down passive avoidance test. Our data also showed that RJ significantly diminished amyloid plaque pathology in APP/PS1 mice. Furthermore, RJ alleviated c-Jun N-terminal kinase (JNK) phosphorylation-induced neuronal apoptosis by suppressing oxidative stress. Importantly, hippocampal cyclic adenosine monophosphate (cAMP), p-PKA, p-CREB and BDNF levels were significantly increased in the APP/PS1 mice after RJ treatment, indicating that the cAMP/PKA/CREB/BDNF pathway might be related to the ameliorative effect of RJ on cognitive decline. Collectively, these results provide a scientific basis for using RJ as a functional food for targeting AD pathology.
Highlights
Alzheimer’s disease (AD) is an age-related neurodegenerative disease characterized by progressive loss of cognitive and memory function (Citron, 2010)
The content of trans-10-hydroxy-2-decenoic acid (10-HDA), 10-hydroxydecanoic acid (10-HDAA) and sebacic acid (SEA) in Royal jelly (RJ) samples were measured using Gas Chromatography (GC). 0.25 g lyophilized RJ powder was extracted with 20 mL ethanol for 15 min and 5 mL methyl 4-hydroxybenzoate was added as internal standard
amyloid precursor protein (APP)/PS1 mice were structured based on Aβ pathology, learningmemory deficits accompanied by detectable cerebral Aβ at 4 months, significant amyloidosis at 6–7 months, and further aggravates pathology at 10 months (Blanchard et al, 2003; Jankowsky et al, 2004)
Summary
Alzheimer’s disease (AD) is an age-related neurodegenerative disease characterized by progressive loss of cognitive and memory function (Citron, 2010). It has been reported that Aβ induced the progression of other pathological abnormalities, including intraneuronal neurofibrillary tangles (NFTs), which are caused by hyperphosphorylated tau, neuroinflammation, and neuronal loss. These pathological events aggravated the deposition of Aβ and further promoted AD progression (Tanzi and Bertram, 2005; Bettens et al, 2013). Aβ-degrading enzymes, including insulin-degrading enzyme (IDE) and neprilysin (NEP), are responsible for the clearance of Aβ in the brain They are capable of cleaving and converting Aβ polypeptide to benign forms (Mukherjee et al, 2000; Shirotani et al, 2001). It is widely accepted that excessive deposition of Aβ can be explained by the imbalance between formation and degradation (Hardy and Selkoe, 2002)
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