β-amyloid peptide fragment 31–35 induces apoptosis in cultured cortical neurons

Yan, X.-Z; Qiao, Jian‐Tian; Dou, Yi; Qiao, Zhiguang

doi:10.1016/s0306-4522(98)00727-1

Cited by 77 publications

(107 citation statements)

References 31 publications

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“…Many researchers have demonstrated that Aβ triggers apoptotic degeneration in in vitro neuronal experiments (Ekinci et al, 1999;Yan et al, 1999). In the present work, cultured cortical neurons exposed to Aβ (25-35) for 36 h showed increased chromatin condensation, a typical feature of apoptotic cell death, which was reduced by CSF.…”

Section: +supporting

confidence: 50%

Inhibitory Effect of Chaenomeles sinensis Fruit on Amyloid β Protein (25-35)-Induced Neurotoxicity in Cultured Neurons and Memory Impairment in Mice

Jung¹,

Song²,

Seong³

2012

Korean Journal of Medicinal Crop Science

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Section: +supporting

confidence: 50%

Inhibitory Effect of Chaenomeles sinensis Fruit on Amyloid β Protein (25-35)-Induced Neurotoxicity in Cultured Neurons and Memory Impairment in Mice

Jung¹,

Song²,

Seong³

2012

Korean Journal of Medicinal Crop Science

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“…They demonstrated that A␤ and A␤ [25][26][27][28][29][30][31][32][33][34][35] induce apoptosis through caspase-dependent pathways. [41][42][43][44][45][46][47] In vivo, 1 week after A␤ [25][26][27][28][29][30][31][32][33][34][35] , an increase in caspase-3 activity in the hippocampus of rats 9 and increases in levels of pro-caspases 9, 12, and 3 in the hippocampus of mice 11 were observed. In the present study, we observed increases in pro-and cleaved forms for caspase-9 (mitochondrial stress marker) and caspase-12 (endoplasmic reticulum stress marker) in all structures except the hypothalamus.…”

Section: Discussionmentioning

confidence: 99%

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Zussy

Brureau

Delair

et al. 2011

The American Journal of Pathology

121

129

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Alzheimer's disease (AD) is a neurodegenerative pathology characterized by the presence of senile plaques and neurofibrillary tangles, accompanied by synaptic and neuronal loss. The major component of senile plaques is an amyloid ␤ protein (A␤) formed by pathological processing of the A␤ precursor protein. We assessed the time-course and regional effects of a single intracerebroventricular injection of aggregated A␤ fragment 25-35 (A␤ 25-35 ) in rats. Using a combined biochemical, behavioral, and morphological approach, we analyzed the peptide effects after 1, 2, and 3 weeks in the hippocampus, cortex, amygdala, and hypothalamus. The scrambled A␤ 25-35 peptide was used as negative control. The aggregated forms of A␤ peptides were first characterized using electron microscopy, infrared spectroscopy, and Congo Red staining. Intracerebroventricular injection of A␤ 25-35 decreased body weight, induced short-and long-term memory impairments, increased endocrine stress, cerebral oxidative and cellular stress, neuroinflammation, and neuroprotective reactions, and modified endogenous amyloid processing, with specific time-course and regional responses. Moreover, A␤ 25-35 , the presence of which was shown in the different brain structures and over 3 weeks, provoked a rapid glial activation, acetylcholine homeostasis perturbation, and hippocampal morphological alterations. Alzheimer's disease (AD) is a chronic neurodegenerative pathology characterized by the presence of senile plaques and neurofibrillary tangles, accompanied by synaptic and neuronal loss in brain areas responsible for learning and memory impairments. 1 The major component of senile plaques is an amyloid ␤ protein (A␤) derived from amyloid precursor protein (APP). Genetic, cell biological, and postmortem studies on AD brain, together with A␤ neurotoxicity findings, gave rise to the amyloid cascade hypothesis to explain A␤-associated neurodegenerative processes. 2 In normal healthy individuals, A␤ peptides are present only in small quantities, as soluble monomers that circulate in cerebrospinal fluid and blood. In AD patients, A␤ peptides, which vary in length from 40 to 43 amino acids, accumulate as insoluble fibrillar deposits. 3 When cultured rat hippocampal neurons are exposed to aggregated A␤ peptides, their neurites adopt a dystrophic appearance and become comparable to those observed surrounding and infiltrating senile plaques. This observation suggested that A␤ is responsible for the neuritic abnormalities in AD pathology. 4 Structure-activity studies revealed that peptides containing the highly hydrophobic 25-35 region formed stable aggregates and mediated neuronal death by necrosis or apoptosis. 5,6,7 The truncated A␤ 25-35 fragment includes extracellular and intramembrane residues that have been reported to represent an active region of A␤. 8

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“…Vitis amurensis, Aralia cordata, and Glycyrrhizae radix, the constituents of SSB, have been reported to possess antioxidant principles, resveratrol, oleanolic acid, and isoliquirtigenin (Du and Ko, 2006;Ha et al, 2009a, b;Kumar et al, 2007), respectively, suggesting that inhibition of Aβ (25-35)-induced neuronal death by SSB might be due to their ROS scavenging activity. Further Many studies have demonstrated that Aβ is accompanied by multiple events culminating in apoptosis in in vitro neuronal experiments (Ekinci et al, 2000;Yan et al, 1999). In the present work, cultured cortical neurons exposed to ] i , ROS generation and neural apoptotic death (Ban et al, 2006;Lee et al, 2005).…”

Section: Ssb Inhibited Aβ (25-35)-induced Memory Impairmentmentioning

confidence: 55%

Inhibitory Effect of an Ethanol Extract Mixture of Vitis amurensis, Aralia cordata, and Glycyrrhizae radix on Amyloid β Protein (25-35)-Induced Neurotoxicity

Jang

Seong²

2014

Korean Journal of Medicinal Crop Science

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: The present study investigated an ethanol extract (SSB) of a mixture of three medicinal plants of Vitis amurensis, Aralia cordata, and Glycyrrhizae radix for possible neuroprotective effects on neurotoxicity induced by Amyloid β protein (Aβ) (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) . From these results, it is suggested that antidementia effect of SSB is due to its neuroprotective effect against Aβ (25-35)-induced neurotoxicity and that SSB may have a therapeutic role in preventing the progression of Alzheimer's disease.

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β-amyloid peptide fragment 31–35 induces apoptosis in cultured cortical neurons

Cited by 77 publications

References 31 publications

Inhibitory Effect of Chaenomeles sinensis Fruit on Amyloid β Protein (25-35)-Induced Neurotoxicity in Cultured Neurons and Memory Impairment in Mice

Inhibitory Effect of Chaenomeles sinensis Fruit on Amyloid β Protein (25-35)-Induced Neurotoxicity in Cultured Neurons and Memory Impairment in Mice

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Inhibitory Effect of an Ethanol Extract Mixture of Vitis amurensis, Aralia cordata, and Glycyrrhizae radix on Amyloid β Protein (25-35)-Induced Neurotoxicity

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