The increase in different precursor proteins that have been shown to form amyloid fibrils and the identification of common properties have not yet led to any unifying theory or mechanism for the pathogenesis of amyloidogenesis. Papua New Guinea holds a unique place in the story of amyloidosis and in this article we review the current status of amyloidosis research indicating how this relates to those forms relevant to Papua New Guinea. This review concentrates on secondary reactive amyloid (AA), which is found in the highest frequency in the world in parts of Papua New Guinea, and kuru, in which the amyloid protein itself is infectious. The history, pathogenesis and future prospects for these diseases are discussed in the light of what is known about other forms of amyloidosis
Amyloid beta-Peptides ; Amyloid - genetics ; Global Health ; Humans ; Mutation ; Papua New Guinea - epidemiology ; Serum Amyloid A Protein

Traumatic brain injury (TBI) is the leading cause of mortality and disability among young individuals in our society, and globally the incidence of TBI is rising sharply. Mounting evidence has indicated that apolipoprotein E (apoE: protein; APOE: gene) genotype influences the outcome after TBI. The proposed mechanism by which APOE affects the clinicopathological consequences of TBI is multifactorial and includes amyloid deposition, disruption of lipid distribution, dysfunction of mitochondrial energy production, oxidative stress and increases intracellular calcium in response to injury. This paper reviews the current state of knowledge regarding the influence of apoE and its receptors on cerebral amyloid beta-protein precursor metabolism following TBI.
Amyloid beta-Peptides ; Apolipoproteins E ; Brain Injuries ; metabolism ; Humans

Alzheimer's disease(AD) is a neurodegenerative disease that has no effective drug to cure it. Studies in several AD models have shown that Erigeron breviscapus and its active ingredients(scutellarin and caffeoylquinic acid) could improve/enhance the learning and memory ability, and the mechanisms are associated with inhibiting amyloid β(Aβ) production, aggregation, fibrosis and Aβ neurotoxicity toxicity, regulating cholinergic nervous system, inhibiting oxidative stress and inflammation, inhibiting tau hyperphosphorylation, improving mitochondrial function, and resisting neuronal apoptosis. This article systematically reviewed the research progress of E. breviscapus and its active ingredients for treatment of AD in AD models, in the expectation of providing references for further development of E. breviscapus's medicinal potential.
Alzheimer Disease ; Amyloid beta-Peptides ; Erigeron ; Humans ; Neurodegenerative Diseases

Alzheimer's disease (AD) is a chronic central neurodegenerative disease. The pathological features of AD are the extracellular deposition of senile plaques formed by amyloid-β oligomers (AβOs) and the intracellular accumulation of neurofibrillary tangles formed by hyperphosphorylated tau protein. In this paper, an in vitro pathological model of AD based on neuronal network chip and its real-time dynamic analysis were presented. The hippocampal neuronal network was cultured on the microelectrode array (MEA) chip and induced by AβOs as an AD model to simultaneously record two firing patterns from the interneurons and pyramidal neurons. The spatial firing patterns mapping and cross-correlation between channels were performed to validate the degeneration of neuronal network connectivity. This biosensor enabled the detection of the AβOs toxicity responses, and the identification of connectivity and interactions between neuronal networks, which can be a novel technique in the research of AD pathological model .
Alzheimer Disease ; Amyloid beta-Peptides ; Humans ; Neurofibrillary Tangles ; tau Proteins

Humans ; Alzheimer Disease/genetics* ; Apolipoprotein E4/genetics* ; Amyloid beta-Peptides

Alzheimer's disease (AD) is a chronic central neurodegenerative disease. The pathological features of AD are the extracellular deposition of senile plaques formed by amyloid-β oligomers (AβOs) and the intracellular accumulation of neurofibrillary tangles formed by hyperphosphorylated tau protein. In this paper, an in vitro pathological model of AD based on neuronal network chip and its real-time dynamic analysis were presented. The hippocampal neuronal network was cultured on the microelectrode array (MEA) chip and induced by AβOs as an AD model in vitro to simultaneously record two firing patterns from the interneurons and pyramidal neurons. The spatial firing patterns mapping and cross-correlation between channels were performed to validate the degeneration of neuronal network connectivity. This biosensor enabled the detection of the AβOs toxicity responses, and the identification of connectivity and interactions between neuronal networks, which can be a novel technique in the research of AD pathological model in vitro.
Alzheimer Disease ; Amyloid beta-Peptides ; Humans ; Neurofibrillary Tangles ; tau Proteins

BACKGROUND: Considerable evidences suggest that the beta-amyloid acts as a neurotoxin, and the epigallocatechin-3- gallate (EGCG) has the anti-inflammatory and anti-oxidant properties. The purpose of this study was to investigate whether the EGCG reduces the death of the cultured hippocampal tissues exposed to the beta-amyloid 1-42 fragments (A beta1-42). METHOD: We cultured the hippocampus of postnatal 7 days old Sprague-Dawley rat into slices of 450 micrometer. The tissue slices had been exposed with 100 micro M A beta1-42 at an interval of 3 days since 12 DIV (days in vitro). Following co-treatment of the tissue with 10 micro M EGCG and A beta1-42, we evaluated EGCG effect on A beta1-42 induced neurotoxicity by measuring the expression of Bcl-2 and NeuN protein and by morphological observation of the hippocampus slice cultures with propidium iodide (PI) and bromodeoxyuridine (BrdU) staining. RESULTS: The EGCG exerted a significant role in restoration of NeuN protein expression inhibited by A beta1-42, showed inhibitory effects fluorescence in PI stained tissues, and increased the anti-BrdU stained cell. CONCLUSIONS: 10 micro M EGCG reduced the A beta1-42 induced neurotoxicity of the hippocampus slice culture.
Alzheimer Disease ; Amyloid ; Amyloid beta-Peptides* ; Animals ; Bromodeoxyuridine ; Fluorescence ; Hippocampus ; Propidium ; Rats* ; Rats, Sprague-Dawley

Cerebral amyloid angiopathy-related inflammation (CAA-RI) is a rare but increasingly recognized subtype of CAA. CAA-RI consists of two subtypes: inflammatory cerebral amyloid angiopathy and amyloid β (Aβ)-related angiitis. Acute or subacute onset of cognitive decline or behavioral changes is the most common symptom of CAA-RI. Rapid progressive dementia, headache, seizures, or focal neurological deficits, with patchy or confluent hyperintensity on T2 or fluid-attenuated inversion recovery sequences and evidence of strictly lobar microbleeds or cortical superficial siderosis on susceptibility-weighted imaging imply CAA-RI. The gold standard for diagnosis is autopsy or brain biopsy. However, biopsy is invasive; consequently, most clinically diagnosed cases have been based on clinical and radiological data. Other diagnostic indexes include the apolipoprotein E ε4 allele, Aβ and anti-Aβ antibodies in cerebral spinal fluid and amyloid positron emission tomography. Many diseases with similar clinical manifestations should be carefully ruled out. Immunosuppressive therapy is effective both during initial presentation and in relapses. The use of glucocorticoids and immunosuppressants improves prognosis. This article reviews the pathology and pathogenesis, clinical and imaging manifestations, diagnostic criteria, treatment, and prognosis of CAA-RI, and highlights unsolved problems in the existing research.
Amyloid beta-Peptides ; Cerebral Amyloid Angiopathy ; Cerebral Hemorrhage ; Humans ; Inflammation ; Magnetic Resonance Imaging ; Vasculitis

Amyloid beta-peptide (A beta) contributes to the pathogenesis of Alzheimer's disease (AD), causing neuronal death through apoptosis. In this study, the neuroprotective role of BF-7, extracted form sericultural product, was examined against A beta -induced toxicity in cultured human neuronal cell SKN-SH. In order to know if the BF-7 has positive role on the cognition and memory in human, the mixture of BF-7, DHA and EPA (BDE) was examined using Rey Kim and K-WAIS test with 50 healthy high school student. We report here that BDE significantly attenuated A beta-induced apoptosis through the reduction of ROS accumulation, and diminished caspase-like protease activity. Moreover, the memory index and memory preservation, and attentative concentration of BDE treated group for 1 month were significantly improved, in contrast to the case of placebo control treated with DHA and EPA. This result represent that the BF-7 play significant positive role on learning memory. Taken together, our result suggested the natural product BF-7 is a good substance for the brain functionally and physiologically.
Alzheimer Disease ; Amyloid ; Amyloid beta-Peptides ; Apoptosis ; Brain ; Cognition ; Humans ; Learning ; Memory ; Neurons

Alzheimer disease (AD) is the most common type of dementia characterized by the progressive cognitive and social decline. Clinical drug targets have heavily focused on the amyloid hypothesis, with amyloid beta (Aβ), and tau proteins as key pathophysiologic markers of AD. However, no effective treatment has been developed so far, which prompts researchers to focus on other aspects of AD beyond Aβ, and tau proteins. Additionally, there is a mounting epidemiologic evidence that various environmental factors influence the development of dementia and that dementia etiology is likely heterogenous. In the past decades, new risk factors or potential etiologies have been widely studied. Here, we review several novel epidemiologic and clinical research developments that focus on sleep, hypoxia, diet, gut microbiota, and hearing impairment and their links to AD published in recent years. At the frontiers of AD research, these findings and updates could be worthy of further attention.
Alzheimer Disease/etiology* ; Amyloid ; Amyloid beta-Peptides ; Humans ; Risk Factors ; tau Proteins