Metal binding to the amyloid beta-peptide is suggested to be involved in the pathogenesis of Alzheimers disease. We used high-resolution NMR to study zinc binding to amyloid beta-peptide 1-40 at physiologic pH. Metal binding induces a structural change in the peptide, which is in chemical exchange on an intermediate rate, between the apo-form and the holo-form, with respect to the NMR timescale. This causes loss of NMR signals in the resonances affected by the binding. Heteronuclear correlation experiments, N-15-relaxation and amide proton exchange experiments on amyloid beta-peptide 1-40 revealed that zinc binding involves the three histidines (residues 6, 13 and 14) and the N-terminus, similar to a previously proposed copper-binding site [Syme CD, Nadal RC, Rigby SE, Viles JH (2004) J Biol Chem279, 18169-18177]. Fluorescence experiments show that zinc shares a common binding site with copper and that the metals have similar affinities for amyloid beta-peptide. The dissociation constant K-d of ...
Recent preliminary data suggest that vaccination with Alzheimers Abeta might reduce senile plaque load and stabilize cognitive decline in human Alzheimers disease. To examine the mechanisms and consequences of anti-Abeta-antibody formation in a species more closely related to humans, rhesus monkeys (Macaca mulatta) were vaccinated with aggregated Abeta(1-42). Immunized monkeys developed anti-Abeta titers exceeding 1:1000, and their plasma Abeta levels were 5-10-fold higher than the plasma Abeta levels observed in monkeys vaccinated with aggregated amylin. These data support the use of non-human primates to model certain phenomena associated with vaccination of humans with aggregated Alzheimers Abeta. ...
Soluble oligomeric aggregates of the amyloid-beta peptide (Abeta) have been implicated in the pathogenesis of Alzheimers disease (AD). Although the conformation adopted by Abeta within these aggregates is not known, a beta-hairpin conformation is known to be accessible to monomeric Abeta. Here we show that this beta-hairpin is a building block of toxic Abeta oligomers by engineering a double-cysteine mutant (called Abetacc) in which the beta-hairpin is stabilized by an intramolecular disulfide bond. Abeta(40)cc and Abeta(42)cc both spontaneously form stable oligomeric species with distinct molecular weights and secondary-structure content, but both are unable to convert into amyloid fibrils. Biochemical and biophysical experiments and assays with conformation-specific antibodies used to detect Abeta aggregates in vivo indicate that the wild-type oligomer structure is preserved and stabilized in Abetacc oligomers. Stable oligomers are expected to become highly toxic and, accordingly, we find ...
Amyloid-beta peptide (Abeta) binding alcohol dehydrogenase (ABAD), an enzyme present in neuronal mitochondria, is a cofactor facilitating Abeta-induced cell stress. We hypothesized that ABAD provides a direct link between Abeta and cytotoxicity via mitochondrial oxidant stress. Neurons cultured from …
Alzheimers disease (AD) is the most common cause of dementia and accounts for 50%-75% of all cases. It has been identified as a protein misfolding disease caused by plaque accumulation of abnormally folded beta amyloid and tau amyloid proteins in the brain.[2] Plaques are made up of small peptides, 39-43 amino acids in length, called beta-amyloid (Aβ) which is a fragment from a larger protein called amyloid precursor protein (APP), which is critical to neuron growth, survival and post-injury repair.[3][4] In AD, a proteolysis process causes APP to be divided into smaller fragments [5] which gives rise to fibrils of beta-amyloid that deposit outside neurons in dense formations known as senile plaques.[1][6]. Exactly how disturbances of production and aggregation of the beta-amyloid peptide gives rise to the pathology of AD is not known.[7][8 ...
The amyloid cascade hypothesis postulates that the initial event which triggers neuronal degradation in Alzheimers disease is enhanced amyloid-β generation and aggregation.
Amyloid beta-protein (Aβ) is the major component of senile plaques and cerebrovascular amyloid deposits in individuals with Alzheimers disease. Aβ is known to increase free radical production in neur
There is striking overlap between the spatial distribution of amyloid-β pathology in patients with Alzheimers disease and the spatial distribution of high intrinsic functional connectivity in healthy persons. This overlap suggests a mechanistic link between amyloid-β and intrinsic connectivity, and indeed there is evidence in patients for the detrimental effects of amyloid-β plaque accumulation on intrinsic connectivity in areas of high connectivity in heteromodal hubs, and particularly in the default mode network. However, the observed spatial extent of amyloid-β exceeds these tightly circumscribed areas, suggesting that previous studies may have underestimated the negative impact of amyloid-β on intrinsic connectivity. We hypothesized that the known positive baseline correlation between patterns of amyloid-β and intrinsic connectivity may mask the larger extent of the negative effects of amyloid-β on connectivity. Crucially, a test of this hypothesis requires the within-patient comparison of
Cows wring protein allergy is a woman of the most common food allergies in the first year of existencePlatelet microparticles as carriers of soluble Alzheimers amyloid beta (sAbeta), Ann N Y Acad Sci VolRoflumilast in moderate-to-severe long-lasting obstructive pulmonary infirmity treated with desire acting bronchodilators: two randomised clinical trialsHay fever (allergic rhinitis) can agent sneezing, congestion, and itchy abrade, eyes and nose, as stream as a cough ,a href=https://clubusa.net/collect/buy-cialis-extra-dosage/,purchase cialis extra dosage 100mg amex,/a,. This is solicitous with the need felt at near the being to handle a substance because it makes him or her feel propitious in some personality or helps him or her to handleTo whatever manner, the inordinate liability liabilities of copiously may call dehydration and this may be life-threatening in the precise boyish and older people, whose water control systems may be embryonic or weak spotIn the ?ve cases where both tunnels ...
ABSTRACT: Alzheimer's disease (AD) is the most common cause of senile dementia worldwide. AD is a neurodegenerative disorder characterized by the loss of memory and language skill, collapse of the cognitive function, and distortion of social behavior. As of today, the onset mechanisms of AD and cure are unknown; however, three hallmarks are commonly encountered: extra and intracellular accumulation of amyloid beta (Abeta) peptide plaques, formation of intracellular neurofibrillary tangles, and inevitable neuronal death. Hypothetically, a possible scenario provoking or involved in the onset of AD is a cascade effect that starts with an imbalance in the production and clearance of Abeta peptide that consequently leads to its accumulation, formation of tau protein tangles and neuronal death. This work studied and characterized the mechanisms governing Abeta peptide aggregation and the effects of using anti-Abeta monoclonal antibodies to modify this process. These mechanisms play an important ...
Today, Crossbeta Biosciences and AdAlta announced that they have established a collaborative relationship in which AdAlta will deploy its i-body technology to develop oligomer-specific i-bodies for therapeutic and diagnostic applications in Alzheimers disease using Crossbetas stabilized beta-amyloid oligomers.. Alzheimers disease is the most common form of dementia, primarily affecting people above the age of 60. Over 26 million people are suffering from Alzheimers disease today, a number that is projected to triple over the coming 40 years. Alzheimers disease remains to be an area of great unmet need with huge and growing social and economic impact. Beta-amyloid oligomers are implicated in Alzheimers disease pathology and there is no effective treatment yet.. AdAltas innovative i-body technology represents the next generation of biological therapeutics merging the highly selective specificity of antibodies with the advantages of drug-like molecules, such as small size and extreme ...
beta-Amyloid (Abeta) pathology is an essential pathogenic component in Alzheimers disease (AD). However, the significance of Abeta pathology, including Abeta deposits/oligomers and glial reactions, to neurodegeneration is unclear. In particular, despite the Abeta neurotoxicity indicated by in vitro studies, mouse models with significant Abeta deposition lack robust and progressive loss of forebrain neurons. Such results have fueled the view that Abeta pathology is insufficient for neurodegeneration in vivo. In this study, because monoaminergic (MAergic) neurons show degenerative changes at early stages of AD, we examined whether the APPswe/PS1DeltaE9 mouse model recapitulates progressive MAergic neurodegeneration occurring in AD cases. We show that the progression forebrain Abeta deposition in the APPswe/PS1DeltaE9 model is associated with progressive losses of the forebrain MAergic afferents. Significantly, axonal degeneration is associated with significant atrophy of cell bodies and ...
Alzheimers disease is characterized by the presence of neurotoxic beta amyloid (Aß) deposits in the brain. This article briefly explains the production of Aß from amyloid precursor protein (APP).
In Alzheimers disease (AD), abnormal accumulations of beta-amyloid are present in the brain and degenerating neurons exhibit cytoskeletal aberrations (neurofibrillary tangles). Roles for beta-amyloid in the neuronal degeneration of AD have been suggested based on recent data obtained in rodent studies demonstrating neurotoxic actions of beta- amyloid. However, the cellular mechanism of action of beta-amyloid is unknown, and there is no direct information concerning the biological activity of beta-amyloid in human neurons. We now report on experiments in human cerebral cortical cell cultures that tested the hypothesis that beta-amyloid can destabilize neuronal calcium regulation and render neurons more vulnerable to environmental stimuli that elevate intracellular calcium levels. Synthetic beta-amyloid peptides (beta APs) corresponding to amino acids 1-38 or 25-35 of the beta-amyloid protein enhanced glutamate neurotoxicity in cortical cultures, while a peptide with a scrambled sequence was ...
Readers,. Amyloid plaques and neurofibrillary tangles (NFTs) are the two classic hallmarks of Alzheimers disease (AD), but the connection between their two respective proteins-beta-amyloid and tau-has remained mysterious. Now, a paper published on July 21 in the prestigious journal Cell details a molecular mechanism that links tau to beta-amyloid toxicity at the synapse. The groundbreaking new study was led by Professor Jürgen Götz and Dr Lars Ittner, based at the University of Sydney.. Back in 2004, scientists from the University of California at Irvine injected anti-beta-amyloid antibodies in the brains of transgenic mice that develop both beta-amyloid deposits and NFTs. This treatment led to a rapid reduction of beta-amyloid deposits and reversed the accumulation of abnormal tau (Oddo et al., 2004). When the anti-beta-amyloid antibodies were removed, the beta-amyloid pathology re-emerged. This was followed by the reappearance of tau pathology. These findings from animal models provided ...
Beta-amyloid production results from cleavage in the extracellular domain of APP by the beta-secretase (BACE1) , which results in the production of the APP C-terminal fragment C99. This fragment is further cleaved by the gamma-secretase at residues 40-42 to produce beta-amyloid 40 and 42 peptides. Beta-amyloid aggregation and neuritic plaque formation are pathologic hallmarks of Alzheimer disease. This peptide corresponds to the human beta-amyloid 1-40 peptide ...
Although the amyloid hypothesis offers a broad framework to explain AD pathogenesis, it is currently lacking in detail, and certain observations do not fit easily with the simplest version of the hypothesis. The most frequently voiced objection is that the number of amyloid deposits in the brain does not correlate well with the degree of cognitive impairment that the patient experienced in life. Indeed, some humans without symptoms of AD have many cortical Aβ deposits. However, the latter are almost exclusively diffuse forms of amyloid plaques that are not associated with surrounding neuritic and glial pathology. Such diffuse Aβ deposits may be analogous to early fatty streaks of cholesterol that are the harbingers of mature, symptom-producing atherosclerotic plaques. Moreover, the degree of dementia in AD correlates much better with Aβ assayed biochemically than with histologically determined plaque counts, and the concentration of soluble Aβ species (which are invisible to ...
Transgenic mouse models that overexpress APP develop senile plaques over time that resemble those found in human Alzheimers disease. These animals are a valuable tool toward understanding the physiology and pathology of senile plaques in living tissue and are ideal for evaluating therapeutics aimed at clearance of amyloid-β deposits in the brain. With the recent success using immunotherapy for prevention of amyloid-β deposits in these animals (Schenk et al., 1999; Bard et al., 2000), as well as clearance of existing plaques (Bacskai et al., 2001), this treatment seems very promising. Recent reports have also indicated that immunotherapy may have positive effects on behavioral deficits exhibited in transgenic mouse models (Janus et al., 2000; Morgan et al., 2000). These findings are important for predicting whether anti-amyloid therapies will prove beneficial not just in arresting deposition of amyloid-β but also in prevention of the associated dementia. Microglial cells were implicated in ...
Antibodies , OptimAb Antibodies , OptimAbᵀᴹ Beta-Amyloid 17-24 , Monoclonal Antibody, purified; Beta-Amyloid forms are deposited in the CNS of patients with Alzheimer s disease and Down s syndrome. Biochemical analysis of the amyloid peptides isolated from Alzheimer s disease brain indicates that Beta-Amyloid (1-42) is the principal species associated with senile plaque amyloids, while Beta-Amyloid (1-40) is more abundant in cerebrovascular amyloid deposits. Both result from the cleavage of Amyloid Precursor Protein (APP) by secretases. The mAb 4G8 reacts to the abnormally processed isoforms, as well as precursor forms.; Host:Mouse
Clone: 4G8
Isotype: IgG2b
Reactivity: Human, Mouse
Immunogen: This antibody is reactive to residues 17-24 of Beta-Amyloid. The epitope lies within amino acids 18-22 of Beta-Amyloid (VFFAE)
Concentration:1 mg/mL
Formulation:PBS (no preservatives); The Ab was purified on Protein G
Applications:The Ab is effective in immunoblotting (WB),
Amyloid-β PET and CSF Aβ42 yield discordant results in 10-20% of memory clinic patients, possibly providing unique information. Although the predictive power of demographic, clinical, genetic, and imaging features for amyloid positivity has previously been investigated, it is unknown whether these features differentially predict amyloid-β status based on PET or CSF or whether this differs by disease stage. We included 768 patients (subjective cognitive decline (SCD, n = 194), mild cognitive impairment (MCI, n = 127), dementia (AD and non-AD, n = 447) with amyloid-β PET and CSF Aβ42 measurement within 1 year. Ninety-seven (13%) patients had discordant PET/CSF amyloid-β status. We performed parallel random forest models predicting separately PET and CSF status using 17 patient features (demographics, APOE4 positivity, CSF (p)tau, cognitive performance, and MRI visual ratings) in the total patient group and stratified by syndrome diagnosis. Thereafter, we selected features with the highest variable
Sigma-Aldrich offers abstracts and full-text articles by [Juliet A Moncaster, Roberto Pineda, Robert D Moir, Suqian Lu, Mark A Burton, Joy G Ghosh, Maria Ericsson, Stephanie J Soscia, Anca Mocofanescu, Rebecca D Folkerth, Richard M Robb, Jer R Kuszak, John I Clark, Rudolph E Tanzi, David G Hunter, Lee E Goldstein].
P05067: Amyloid beta A4 protein; ABPP; APPI; APP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; PreA4; Protease nexin-II; PN-II; N-APP; Soluble APP-alpha; S-APP-alpha; Soluble APP-beta; S-APP-beta; C99; Beta-amyloid protein 42; Beta-APP42; Beta-amyloid protein 40; Beta-APP40; C83; P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59; Amyloid intracellular domain 59; AICD-59; AID(59); Gamma-CTF(59); Gamma-secretase C-terminal fragment 57; Amyloid intracellular domain 57; AICD-57; AID(57); Gamma-CTF(57); Gamma-secretase C-terminal fragment 50; Amyloid intracellular domain 50; AICD-50; AID(50); Gamma-CTF(50); C31; ...
Live discussion held 5 December 2001, noon-1 p.m. (EST).. Participants: Dick Lloyd, Sam Gandy, June Kinoshita, Richard Bowen, Nico Stanculescu, Seth Shaw, Mark Smith, Steve Fiander, Gunnar Gouras, Larry Tusick, Alan Lerner, Alexei R. Koudinov, Mike Shelanski, Rena Li, Gabrielle Strobel, Craig Atwood, and the mysterious Guest 2.. Note: The transcript has been edited for clarity and accuracy.. June: First, let me welcome you all to todays live discussion.. Sam Gandy: Thanks for organizing it, June.. June: I know that Richard Bowen has been eager to discuss some of the points in your discussion. Richard, would you like to ask the first question?. Richard L. Bowen: Yes, June: I wanted to know if Sam has looked at the ovariectomized mice and beta amyloid study, and have you had a chance to look at gonadotrophin levels?. Sam Gandy: We havent studied gonadotrophin levels under any circumstances. A paper on ovariectomy effects on Ab load in transgenic mice is in press at J. Neurochem. Co-authors are ...
Physical exercise has been suggested to reduce the risk of developing Alzheimers disease (AD) as well as ameliorate the progression of the disease. However, we recently published results from two large epidemiological studies showing no such beneficial effects on the development of AD. In addition, long-term, voluntary running in the 5xFAD mouse model of AD did not affect levels of soluble amyloid beta (Aβ), synaptic proteins or cognitive function. In this follow-up study, we investigate whether running could impact other pathological aspects of the disease, such as insoluble Aβ levels, the neuroinflammatory response and non-cognitive behavioral impairments. We investigated the effects of 24 weeks of voluntary wheel running in female 5xFAD mice (n = 30) starting at 2-3 months of age, before substantial extracellular plaque formation. Running mice developed hindlimb clasping earlier (p = 0.009) compared to sedentary controls. Further, running exacerbated the exploratory behavior in Elevated plus maze
Dear Amyloid/Ageing subscribers: I began to study Alzheimers amyloid beta (Ab) protein in 1992, at the time when it was becoming clear that this protein exists normally in a soluble form (soluble Ab) and that it is not just a pathological protein. My research activities yielded an on-going project, devoted to understanding in more detail the normal biology of amyloid beta. Understanding the normal biology of Ab would answer the questions of why soluble Ab does not undergo fibrillogenesis in biological fluids but does polymerize into amyloid fibrils in the disease, and what the biological consequences of Ab deposition within the brain tissue are. This, in turn, would be crucial for understanding the pathophysiology of Alzheimers disease and for delineating pathologically grounded new approaches to therapy. My current postdoctoral position at NYU Medical Center just expired. Thus, to continue my research I have to find another position. I would be happy to continue my research as a part of your ...
Beta-amyloid is a protein fragment at the focus of research into the causes of Alzheimers disease. It is normally found in the brain but during the disease process, it forms small clumps known as oligomers, which are thought to be toxic to nerve cells. Eventually, beta-amyloid oligomers combine to form even larger structures known as fibrils, which then form amyloid plaques in the brain, one of the characteristic features of Alzheimers disease. Stephen Meredith, M.D., Ph.D., and colleagues have been studying the detailed molecular structure of beta-amyloid fibrils and working to identify what may trigger their development in Alzheimers disease. They have found that fibrils can have different structures from one person to the next, but that the fibrils found in different parts of the brain of a single person are generally the same. The researchers hypothesize that formation of an initial oligomer or fibril in one area of the brain may trigger the accumulation of other oligomers and subsequent ...
Proteolytic cleavage of amyloid-β-protein precursor (AβPP) by β- and γ-secretases results in production of the amyloid-β peptide (Aβ) that accumulates in the brains of sufferers of Alzheimers disease (AD). We have developed a monoclonal antibody, 2B
Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. GTP hydrolysis in protein synthesis: two for Tu?
Soluble β-amyloid peptide (βAP) is measured in biological fluids at very low concentrations, typically in the range from 0.1 ng/ml to 10 ng/ml. The measurement of βAP concentrations in animals or conditioned medium from cultured cells can be used for drug screening, where test compounds are administered to the animals or exposed to the cultured cells and the accumulation of βAP in the animal or culture medium observed. It has been found that elevated levels of βAP in body fluids, such as blood and cerebrospinal fluid, is associated with the presence of a βAP-related condition in a patient, such as Alzheimers Disease. Methods for diagnosing and monitoring βAP-related conditions comprise measuring the levels of βAP in such body fluids from a patient.
Alzheimers disease researchers have been intrigued by the selective regional vulnerability of the brain to amyloid-ß plaques and tau neurofibrillary tangles. Post-mortem studies indicate that in ageing and Alzheimers disease tau tangles deposit early in the transentorhinal cortex, a region located in the anterior-temporal lobe that is critical for object memory. In contrast, amyloid-ß pathology seems to target a posterior-medial network that subserves spatial memory. In the current study, we tested whether anterior-temporal and posterior-medial brain regions are selectively vulnerable to tau and amyloid-ß deposition in the progression from ageing to Alzheimers disease and whether this is reflected in domain-specific behavioural deficits and neural dysfunction. 11C-PiB PET and 18F-flortaucipir uptake was quantified in a sample of 131 cognitively normal adults (age: 20-93 years; 47 amyloid-ß-positive) and 20 amyloid-ß-positive patients with mild cognitive impairment or Alzheimers disease ...
misc{6494bef1-596c-4a8f-a511-b3b2760e7a57, author = {Linse, Sara and Thulin, Eva and Hellstrand, Erik and Sparr, Emma and Walsh, D.}, issn = {1742-464X}, language = {eng}, note = {Conference Abstract}, pages = {11--11}, publisher = {Federation of European Neuroscience Societies and Blackwell Publishing Ltd}, series = {The FEBS Journal}, title = {Towards physico-chemical understanding of fibril formation of the Alzheimer disease-associated amyloid beta-peptide}, volume = {276}, year = {2009 ...
21st Century Biochemicals - Catalog: Beta Amyloid Peptides (also known as: Abeta peptides | Amyloid beta A4 | A beta P | amyloid beta-peptide | aa 1-40/42)
21st Century Biochemicals - Catalog: Beta Amyloid Peptides (also known as: Abeta peptides | Amyloid beta A4 | A beta P | amyloid beta-peptide | aa 1-40/42)
In the past, scientists thought amyloid plaques was the problem associated with the disease. Claudio Soto from the University of Texas Medical School of Houston said that it is now clear that those aggregates are not the major culprit but it is the aggregatess precursors. The precursors are a group of molecules called Amyloid-Beta (Aβ) oligomers. Soto continues by saying that it is the main molecule that could be the finest, most reliable means to make an early diagnosis. He also says that is the largest problem in the medical field because physicians cannot identify them until patients are already ill. Soto adds that the amyloid beta oligomers can be in a persons body years or even decades before they show cognitive symptoms.. Soto and his colleagues used a technology they developed to detect misfolded proteins in prion diseases such as Mad Cow Disease. The technology, called protein misfolding cyclic amplification, works by exaggerating existing proteins that misfolded and separating them ...
Harper JD, Lieber CM, Lansbury PT. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimers disease amyloid-beta protein ...
Dennis J. Selkoe, MD, Co-director of the Ann Romney Center for Neurologic Diseases at Brigham and Womens Hospital, discusses progress in the development of Alzheimers disease treatments that target the amyloid beta protein.
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Alzheimers disease (AD) is a conformational disease that is characterized by amyloid-β (Aβ) deposition in the brain. Aβ exerts its toxicity in part by receptor-mediated interactions that cause down-stream protein misfolding and aggregation, as well as mitochondrial dysfunction. Recent reports indicate that Aβ may also interact directly with intracellular proteins such as the mitochondrial enzyme ABAD (Aβ binding alcohol dehydrogenase) in executing its toxic effects. Mitochondrial dysfunction occurs early in AD, and Aβs toxicity is in part mediated by inhibition of ABAD as shown previously with an ABAD decoy peptide. Here, we employed AG18051, a novel small ABAD-specific compound inhibitor, to investigate the role of ABAD in Aβ toxicity. Using SH-SY5Y neuroblastoma cells, we found that AG18051 partially blocked the Aβ-ABAD interaction in a pull-down assay while it also prevented the Aβ42-induced down-regulation of ABAD activity, as measured by levels of estradiol, a known hormone and ...
Alzheimer disorder (AD), the most typical source of dementia inside the seniors, is usually seen as a modern cerebral buildup with amyloid-? (A?) stores in a choice dense-core senile plaques or maybe soften amorphous plaques (Just one). Within vivo image scientific tests strongly include the amyloid speculation, which postulates that will structure with senile plaques triggers any pathological cascade leading to recruitment with microglia in addition to induction connected with community neuritic changes nearby the plaques (A pair of, 3 or more). A? is made up generally of 40- plus 42-amino chemical p proteins made on the amyloid forerunner aminoacids (Application) through constant proteolytic cleavages mediated by way of ?- and ?-secretases (Four). Many anti-amyloid treatments are currently inside improvement only several currently have successfully inverted existing amyloid pathology (Two, Five). In regulatable Practical application transgenic rats, any conceptual model for treatments aimed ...
New insights on what causes Alzheimers disease could arise from a recent discovery made by bioengineers from the University of California, San Diego. The finding concerns the infamous amyloid beta peptides (Aβ) -- fragments of which form plaques thought to play a role in Alzheimers disease. The bioengineers found that amyloid beta peptides spontaneously trigger calcium waves in purified cultures of astrocyte cells extracted from the cortex region of rat brains and grown in the lab.
The progressive accumulation of extracellular amyloid plaques in the brain is a common hallmark of Alzheimers disease (AD). We recently
Five point mutations within the amyloid beta-protein (Abeta) sequence of the APP gene are associated with hereditary diseases which are similar or identical to Alzheimers disease and encode: the A21G (Flemish), E22G (Arctic), E22K (Italian), E22Q (Dutch) and the D23N (Iowa) amino acid substitutions. Although a substantial body of data exists on the effects of these mutations on Abeta production, whether or not intra-Abeta mutations alter degradation and how this relates to their aggregation state remain unclear. Here we report that the E22G, E22Q and the D23N substitutions significantly increase fibril nucleation and extension, whereas the E22K substitution exhibits only an increased rate of extension and the A21G substitution actually causes a decrease in the extension rate. These substantial differences in aggregation together with our observation that aggregated wild type Abeta(1-40) was much less well degraded than monomeric wild type Abeta(1-40), prompted us to assess whether or not ...
1IYT: Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain.
Introduction: We recently showed that amyloid beta (Aβ) 40 accumulates in erythrocytes and possibly causes cell damage as evidenced from an increased number of
A systematic analysis of Alzheimer disease amyloid β peptide variants inDrosophila brain demonstrates that their predicted propensity to form protofibrillar aggregates correlates best with toxicity.
Depression is one of the most common psychiatric diseases and the prevalence of depressive symptoms in women is almost twice compared to men, although the reasons of this gender difference are not fully understood yet. Recently, soluble amyloid beta (Aβ)1-42 peptide has been receiving great importance in the development of depression, also considering that depression is highly comorbid with Alzheimers disease and other neurodegenerative illnesses. The central role played by Aβ in the development of depressive-like symptoms in rodents has been evidenced in environmental rodent model of depression. Indeed, we have previously found that lifelong exposure to n-3 polyunsaturated fatty acids (PUFA) deficient diet in female rats at 8 weeks of life leads to depressive like- symptoms and higher susceptibility to stress associated with increased Aβ levels. In order to understand if such effects were maintained over time, rats were exposed to the same diet regimen until 6 or 21 weeks of life. We found ...
References for Abcams beta-Amyloid Peptide (35-25) (ab120977). Please let us know if you have used this product in your publication
Natàlia Carullas research group provides information that questions the widely accepted premise regarding the number of molecules and the shape of the first aggregates formed by amyloid beta protein. Amyloid beta protein aggregation, the process by which molecules of this protein adhere to each other is strongly associated with the development of Alzheimers disease. Carullas work ultimately seeks to identify molecules that interfere with the initial stages of aggregation as a strategy to combat the disease.. ...
Clippingdale, Andrew B., Wade, John D. and Barrow, Colin J. 2001, The amyloid-β peptide and its role in Alzheimers disease, Journal of peptide science, vol. 7, no. 5, pp. 227-249, doi: 10.1002/psc.324. ...
Cirrito JR, Disabato BM, Restivo JL, Verges DK, Goebel WD, Sathyan A, Hayreh D, DAngelo G, Benzinger T, Yoon H, Kim J, Morris JC, Mintun MA, Sheline YI (2011). Proc Natl Acad Sci USA, 108(36):14968-73