*  Early-onset Alzheimer's disease - Wikipedia
This amyloid protein forms plaques and neurofibrillary tangles that progress through the brain. Very rarely the plaque may be ... Eventually, the fragments form oligomers, then fibrils, beta-sheets, and finally plaques. The presence of β-amyloid plaques in ... Beta-amyloid is a small piece of a larger protein called the amyloid precursor protein (APP). Once APP is activated it is cut ... The protein the gene codes for (PS1) is an integral membrane protein. As stated by Ikeuchi (2002)[10] it cleaves the protein ...
  https://en.wikipedia.org/wiki/Early-onset_Alzheimer_disease
*  Diet and Alzheimer's Disease
It binds amyloid proteins and prevents them from grouping together to form plaque. Additionally, turmeric reduces the ... This results in the formation of beta-amyloid plaques.. A brain-healthy diet combined with physical and mental activity, proper ... People with Alzheimer s develop beta-amyloid plaque i.e. clusters of protein that inhibit communication between nerve cells and ... Excess calcium build-up inside brain cells contributes to the production of the beta-amyloid protein, which results in ...
  http://www.medindia.net/patients/lifestyleandwellness/diet-and-alzheimers-disease.htm
*  Study: Chronic Sleep Deprivation Worsens Alzheimer's Disease
The plaques are formed by toxic accumulations of the protein amyloid beta peptide. This is a protein fragment of the plaques ... They measured levels of beta amyloid protein and found concentrations of the plaque-forming peptide are higher when people and ... One of the hallmarks of Alzheimer's disease is the formation in the brain of amyloid plaques - essentially clumps of protein ... Investigators found that sleep-deprived mice showed a 25 percent increase in amyloid beta protein levels. ...
  https://www.voanews.com/a/a-13-2009-09-24-voa58-68662067/354729.html
*  New Lab Rat May Be Star of Future Alzheimer s Research; Confirms Beta-Amyloid as Cause
On a second look, however, the confirmation that increases in the molecule beta-amyloid in the brain causes the disease, and ... Plaque-forming beta-amyloid molecules are derived from a larger protein called amyloid precursor protein (APP). One hypothesis ... include abnormal levels of beta-amyloid protein that form amyloid plaques; tau proteins that clump together inside neurons and ... confirms Alzheimer s brains have abnormal levels of beta-amyloid protein that form amyloid plaques ...
  http://seniorjournal.com/NEWS/Alzheimers/2013/20130419-New_lab_rat.htm
*  Brain tissue with Alzheimer's disease - Stock Image M108/0423 - Science Photo Library
The neuritic plaques are formed mainly of aggregations of the protein amyloid. Alzheimer's disease causes progr- essive ... Neurofibrillary tangles are formed of abnormal filaments of tau protein, an internal structural component of healthy nerve ... The pathogenic abnormal form has no struct- ural role, and damages the cells. ... Two characteristic features are seen here: neurofibrillary tangles (brown) and neuritic plaques (grey). ...
  http://www.sciencephoto.com/media/250096/view
*  Early-onset Alzheimer's disease - Wikipedia
This amyloid protein forms plaques and neurofibrillary tangles that progress through the brain. Very rarely the plaque may be ... Eventually, the fragments form oligomers, then fibrils, beta-sheets, and finally plaques. The presence of β-amyloid plaques in ... Beta-amyloid is a small piece of a larger protein called the amyloid precursor protein (APP). Once APP is activated it is cut ... "Increased β-amyloid release and levels of amyloid precursor protein (APP) in fibroblast cell lines from family members with the ...
  https://en.wikipedia.org/wiki/Early-onset_Alzheimer's_disease
*  Psychology Theory - Thoughts by Dr Arthur Janov
... is formed when a gene known as BACE1 produces an enzyme that cuts long strands of harmless amyloid protein into those plaques ... Page 4), found that when the brain is hyper stimulated there is an increase in the manufacture of amyloid plaque particularly ... Six months later, the oxygen-deprived mice had developed twice as many amyloid plaques as similar animals raised normally. It ... They form an interconnected circuit.. The story of our neurons is one of fear. There is a terror of hidden feelings because ...
  http://www.primaltherapy.com/SEO/community_randomthoughts.shtml
*  Alzheimer fibrils at atomic resolution
... of the beta-amyloid protein form the typical senile plaque present in the brains of patients with Alzheimer's disease. A ... Elongated fibres (fibrils) of the beta-amyloid protein form the typical senile plaque present in the brains of patients with ... Beta-amyloid peptide 1-42 and beta-amyloid peptide 1-40 are the two main forms that appear in senile plaques. We do not know ... Alzheimer's researchers find clues to toxic forms of amyloid beta. June 10, 2016 Much of the research on Alzheimer's disease ...
  https://medicalxpress.com/news/2016-08-alzheimer-fibrils-atomic-resolution.html
*  Sleep Problems May Be Early Sign of Alzheimer's
Amyloid is a protein that can fold and form into plaques. Tau is a protein that forms into tangles. These plaques and tangles ... "For example, disrupted sleep or lack of sleep may lead to amyloid plaque buildup because the brain's clearance system kicks ... Our study looked not only for amyloid but for other biological markers in the spinal fluid as well." ... Those biological markers included signs of amyloid, tau and brain cell damage and inflammation. ...
  http://www.newswise.com/articles/view/677317/?sc=dwhn
*  Merck becomes bigger Alzheimer's player, with new trial - Loveland Reporter-Herald
... by starting a mid-stage study of a drug from a new class of oral medicines that aim to shut down production of a protein ... an enzyme involved in production of toxic beta amyloid proteins that form plaque in the brain believed to be a contributor to ... Merck's drug appears almost to entirely prevent the formation of new beta amyloid, the toxic proteins that lead to plaques in ... whereas beta secretase inhibitors directly interfere with production of the beta amyloid proteins that form the plaque.. "Our ...
  http://www.reporterherald.com/lifestyles/ci_22120536/merck-starts-new-alzheimers-trial
*  APOE2 May Be Therapeutic in Alzheimer's | Medpage Today
... suggesting that the protein could prevent Alzheimer's disease, res ... Bathing the mouse brain in the APOE2 form of apolipoprotein E reduced levels of abnormal beta-amyloid protein compared with ... Beta-amyloid protein levels, including the benign 40-mer and plaque-forming 42-mer versions, were measured in interstitial ... Still unclear, however, is whether ablating beta-amyloid plaques after they have already appeared will be beneficial in ...
  https://www.medpagetoday.com/neurology/alzheimersdisease/43056
*  Cannabinoid receptor type 2 - Wikipedia
In patients with Alzheimer's disease, beta-amyloid proteins form aggregates known as senile plaques, which disrupt neural ... "Cannabinoid CB2 receptors and fatty acid amide hydrolase are selectively overexpressed in neuritic plaque-associated glia in ... Specifically, the CB2 agonist JWH-015 was shown to induce macrophages to remove native beta-amyloid protein from frozen human ... A new mouse model was described in 2014 that expresses a fluorescent protein whenever CB2 is expressed within a cell. This has ...
  https://en.wikipedia.org/wiki/Cannabinoid_receptor_type_2
*  Two proteins may help prevent Alzheimer's brain plaques | EurekAlert! Science News
Louis suggests two proteins work together in mice to prevent formation of brain plaques characteristic of Alzheimer's disease. ... Studies suggest these plaques form when the protein amyloid beta (Abeta) is converted from its soluble to its insoluble form ... Ironically, these proteins also have been implicated in a key stage of plaque formation. The study appears in the Jan. 22 issue ... Louis suggests two proteins work together in mice to prevent formation of brain plaques characteristic of Alzheimer's disease. ...
  https://www.eurekalert.org/pub_releases/2004-01/wuso-tpm012004.php
*  Transcytosis - Wikipedia
... including the species that aggregate to form amyloid plaques associated with Alzheimer's disease. Molecules are transported ... BACE1 is the enzyme which processes amyloid precursor proteins into amyloid-β peptides, ... had the previously developed high-affinity anti-BACE1 binding site that would inhibit BACE1 function and prevent amyloid plaque ... The non-transportable drug, or therapeutic protein, is genetically fused to a transporter protein. The transporter protein may ...
  https://en.wikipedia.org/wiki/Transcytosis
*  Epigenetics of neurodegenerative diseases - Wikipedia
BACE1 is an enzymatic protein that cleaves the Amyloid Precursor Protein into the insoluble amyloid beta form, which then ... and by amyloid-beta senile plaques amyloid-beta senile plaques. Several genetic factors have been identified as contributing to ... and senile plaque deposition. There may be some effect of age in levels of DNA methylation at specific gene promoters, as one ... an enzyme that cleaves APP into the amyloid-beta form, which in turn aggregates into insoluble senile plaques. Repressive ...
  https://en.wikipedia.org/wiki/Epigenetics_of_neurodegenerative_diseases
*  Amyloid precursor protein - Wikipedia
... whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients. ... a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV". The EMBO Journal ... Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of ... Chauhan VP, Ray I, Chauhan A, Wisniewski HM (May 1999). "Binding of gelsolin, a secretory protein, to amyloid beta-protein". ...
  https://en.wikipedia.org/wiki/Amyloid_precursor_protein
*  Haemodynamic response - Wikipedia
In Alzheimer's disease, the fragments accumulate to form hard, insoluble plaques which reduce blood flow. Two proteins are ... When these proteins are active, they turn on SREBP2 which inhibits LRP-1. LRP-1 helps the brain remove amyloid beta. Therefore ... Moreover, only once disruption of the plaque surface has occurred are these prothrombotic effects likely to be significant in ... In this disease, there is a build of the amyloid beta protein in the brain. This ultimately leads to a reduction in the ...
  https://en.wikipedia.org/wiki/Haemodynamic_response
*  Amyloid beta - Wikipedia
The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers, a protein fold shared by ... Aβ is formed after sequential cleavage of the amyloid precursor protein (APP), a transmembrane glycoprotein of undetermined ... Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K (Jun 1985). "Amyloid plaque core protein in Alzheimer ... Arispe, N; Rojas, E; Pollard, H B (1993-01-15). "Alzheimer disease amyloid beta protein forms calcium channels in bilayer ...
  https://en.wikipedia.org/wiki/Amyloid_beta
*  Role of microglia in disease - Wikipedia
Then, the oxygen species encourage the aggregation of beta amyloid in order to form plaques. The growing size of these plaques ... Microglia synthesize amyloid precursor protein (APP) in response to excitotoxic injury. Plaques result from abnormal ... inflammation-like glial responses that may produce neurodegenerative symptoms such as plaque formation, dystrophic neurite ... Plaques in Alzheimer's disease contain activated microglia. A study has shown that direct injection of amyloid into brain ...
  https://en.wikipedia.org/wiki/Role_of_microglia_in_disease
*  Collagen, type XXV, alpha 1 - Wikipedia
2005). "Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates". FEBS J. ... a soluble form of COL25A1 containing the extracellular collagen domains that associates with senile plaques in Alzheimer ... 2005). "Characterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid beta-peptide- ... 2004). "Molecular identification of AMY, an Alzheimer disease amyloid-associated protein". J. Neuropathol. Exp. Neurol. 62 (11 ...
  https://en.wikipedia.org/wiki/Collagen,_type_XXV,_alpha_1
*  Alzheimer's Disease Neuroimaging Initiative - Wikipedia
... which is tested for the AD biomarkers β-amyloid, the main component of amyloid plaques, and tau protein, which forms ... Changes in Cortical Network Topology with Increased Amyloid Plaque Burden". Radiology. 279 (1): 328. doi:10.1148/radiol. ... β-amyloid (indicating deposition of amyloid in plaques outside the cell, measured in CSF and by amyloid PET) Tau (indicating ... β-amyloid positivity. Currently, the phase 3 A4 trial testing the anti-amyloid antibody solanezumab, uses β-amyloid positivity ...
  https://en.wikipedia.org/wiki/Alzheimer's_Disease_Neuroimaging_Initiative
*  Alzheimer's disease - Wikipedia
... caused by plaque accumulation of abnormally folded amyloid beta protein, and tau protein in the brain. Plaques are made up of ... Accumulation of aggregated amyloid fibrils, which are believed to be the toxic form of the protein responsible for disrupting ... Both amyloid plaques and neurofibrillary tangles are clearly visible by microscopy in brains of those afflicted by AD. Plaques ... One such test involves the analysis of cerebrospinal fluid for beta-amyloid or tau proteins, both total tau protein and ...
  https://en.wikipedia.org/wiki/Alzheimer's_disease
*  Transthyretin - Wikipedia
Preventing plaque formation is thought to enable a cell to rid itself of this otherwise toxic protein form and, thus, help ... thereby preventing beta-amyloid's natural tendency to accumulate into the plaques associated with the early stages of ... Treatment of familial TTR amyloid disease has historically relied on liver transplantation as a crude form of gene therapy. ... TTR is also thought to have beneficial side effects, by binding to the infamous beta-amyloid protein, ...
  https://en.wikipedia.org/wiki/Transthyretin
*  Lysozyme Amyloidogenesis Is Accelerated by Specific Nicking and Fragmentation but Decelerated by Intact Protein Binding and...
We have revisited the well-studied heat and acidic amyloid fibril formation pathway (pH 1.6, 65 °C) of hen egg-white lysozyme (HEWL) to map the barriers of the misfolding and amyloidogenesis pathways. A comprehensive kinetic mechanism is presented where all steps involving protein hydrolysis, fragmentation, assembly and conversion into amyloid fibrils are accounted for. Amyloid fibril formation of lysozyme has multiple kinetic barriers. First, HEWL unfolds within minutes, followed by irreversible steps of partial acid hydrolysis affording a large amount of nicked HEWL, the 49-101 amyloidogenic fragment and a variety of other species over 5-40 h. Fragmentation forming the 49-101 fragment is a requirement for efficient amyloid fibril formation, indicating that it forms the ...
  http://liu.diva-portal.org/smash/record.jsf?pid=diva2:262849
*  Most recent papers with the keyword Som | Read by QxMD
Misfolded β-sheet structures of proteins leading to neurodegenerative diseases like Alzheimer's (AD) and Parkinson's diseases (PD) are in the spotlight since long. However, not much was known about the functional amyloids till the last decade. Researchers have become increasingly more concerned with the degree of involvement of these functional amyloids in human physiology. Interestingly, it has been found that the human body is exposed to a tremendous systemic amyloid burden, especially, during aging. Though many findings regarding these functional amyloids come up every day, some questions still remain unanswered like do these functional amyloids directly involve in the fibrillization of Amyloid beta (Aβ) 42 peptide or enhance the Aβ42 aggregation rate; whether functional bacterial ...
  https://www.readbyqxmd.com/keyword/33160
*  Amyloid formation may link Alzheimer disease and type 2 diabetes
Researchers first injected transgenic mice expressing human IAPP with preformed fibrils of synthetic IAPP, proIAPP, or beta-amyloid. After 10 months on a high-fat diet, tissue was analyzed using an amyloid-specific dye. The number of islets with amyloid was significantly increased compared to controls by all three types of fibrils, and the amyloid consisted of IAPP in all groups. No amyloid deposits were found in the spleen, kidney, liver, heart, or lungs. The results demonstrate for the first time that fibril injections could seed amyloid formation in the pancreas and also that brain amyloid could cross-seed fibril formation in the pancreas.. In subsequent experiments the investigators analyzed human tissues from the pancreas and brain. Using antibody-based methods, they ...
  http://www.innovations-report.com/html/reports/medicine-health/amyloid-formation-may-link-alzheimer-disease-and-type-2-diabetes.html
*  More Evidence for Transthyretin Amyloid to Associate with Osteoarthritis - Fight Aging!
Amyloidosis is a protein conformational disorder in which amyloid fibrils accumulate in the extracellular space and induce organ dysfunction. Recently, two different amyloidogenic proteins, transthyretin (TTR) and apolipoprotein A-I (Apo A-I), were identified in amyloid deposits in knee joints in patients with knee osteoarthritis (OA). However, clinicopathological differences related to those two kinds of amyloid deposits in the knee joint remain to be clarified. Here, we investigated the clinicopathological features related to these knee amyloid deposits associated with knee OA and the biochemical characteristics of the amyloid deposits. We found that all of our patients with knee OA had ...
  https://www.fightaging.org/archives/2016/10/more-evidence-for-transthyretin-amyloid-to-associate-with-osteoarthritis/
*  The Molecular Chaperone DNAJB6 - A Suppressor of Disease Related Amyloid Fibril Formation
phdthesis{f475f263-31b6-4989-81bd-1aa466807429, abstract = {Several neurodegenerative diseases are caused by peptides or proteins forming amyloid fibrils such as the Aβ peptide involved in Alzheimer's disease and the huntingtin exon-1 with a prolonged polyglutamine (polyQ) stretch involved in Huntington's disease. The ability to form amyloid fibrils is an intrinsic feature in all proteins. The fibrils are built up of monomers to form elongated structures with β-sheets perpendicular to the fiber axis. Molecular chaperones are involved in maintaining the protein homeostasis in the cells, in preventing protein aggregation, in refolding misfolded proteins and in mediating degradation of proteins and also in preventing amyloid fibril formation. DNAJB6 is a member of the HSP40 chaperone family, and has been found ...
  https://lup.lub.lu.se/search/publication/4779986
*  Localized amyloids important in diseases outside the brain : lessons from the islets of Langerhans and the thoracic aorta
It has long been understood that amyloids can be lethal in systemic diseases. More recently, it has been accepted that local cerebral aggregation of the small peptide A beta is involved in the pathogenesis of Alzheimer's disease. Protein aggregation, with the generation of small amyloid deposits in specific organs, also occurs outside the central nervous system and often is associated with increased cell death. In this review, we discuss two lesser known but common localized amyloid fibril-forming proteins: the polypeptide hormone islet amyloid polypeptide (IAPP) and the lactadherin-derived peptide medin. IAPP aggregates and induces the depletion of islet beta-cells in type 2 diabetes and in islets transplanted into type 1 diabetic subjects. Initial amyloid deposition occurs intracellularly and parts of this ...
  http://uu.diva-portal.org/smash/record.jsf?pid=diva2:451533
*  British Library EThOS: The structure and physical properties of amyloid fibrils
Amyloid fibrils are associated with a range of highly debilitating neurological disorders including Alzheimer's disease, Parkinson's disease and the spongiform encephalopathies. These structures are formed by the misfolding and self-assembly of peptides and proteins varying widely in sequence and in native conformation. Here we combine experimental measurements derived from sold-state NMR, X-ray fibre diffraction and Atomic Force Microscopy to determine the complex, higher order protofilament structure adopted by an 11-amino acid peptide fragment of the human plasma protein transthyretin, TTR(105-115). This determination of the structure of amyloid fibrils to atomic resolution is crucial to the understanding of non-native protein self-assembly and the molecular basis of protein deposition diseases. We then demonstrate that amyloid fibrils, ...
  http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599062
*  Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in...
In this study, we have compared the biological effects of different Aβ assemblies on primary mixed brain cultures to determine whether nonfibrillar or immature, prefibrillar forms of Aβ may be neurotoxic. This potentially important source of neuronal injury has been overlooked until very recently, perhaps because the neuropathological diagnosis of AD requires the presence of abundant fibrillar amyloid in the form of myriad neuritic plaques in postmortem brain tissue. Because mature amyloid plaques surrounded by dystrophic neurites, activated microglia, and reactive astrocytes are composed principally of Aβ fibrils, it has been generally assumed that fibrillar Aβ is the form most likely to be responsible for neuronal and glial injury in AD. The apparent importance of amyloid fibrils has been reinforced by cell culture studies ...
  http://www.jneurosci.org/content/19/20/8876.long
*  Implications of Amyloid Pathology - Full Text View - ClinicalTrials.gov
There is compelling evidence supporting amyloid as one of the key pathologic agents in AD. Autopsy studies suggest the amount and location of fibrillar amyloid deposition does not relate strongly to the degree and type of clinical impairment, compared to tau pathology and neuronal loss. A substantial percentage of individuals known to be cognitively intact prior to death demonstrate significant amyloid pathology at autopsy. PIB-PET studies of older normal individuals have also demonstrated significant amyloid deposition in substantial percentages.. This study will test the hypothesis that amyloid is associated with synaptic dysfunction and neuronal damage. While some individuals are able to compensate for amyloid-related toxicity for an extended time period, sensitive imaging and neuropsychological markers ...
  https://clinicaltrials.gov/ct2/show/NCT00900770?term=alzheimer
*  Amyloid-Like Aggregates of the Yeast Prion Protein Ure2 Enter Vertebrate Cells by Specific Endocytotic Pathways and Induce...
PubMed Central Canada (PMC Canada) provides free access to a stable and permanent online digital archive of full-text, peer-reviewed health and life sciences research publications. It builds on PubMed Central (PMC), the U.S. National Institutes of Health (NIH) free digital archive of biomedical and life sciences journal literature and is a member of the broader PMC International (PMCI) network of e-repositories.
  http://pubmedcentralcanada.ca/pmcc/articles/PMC2932714/?lang=en-ca
*  amyloid
Actually, the photo depicts amyloid plaques, a frequent topic in the context of Alzheimer's disease. Pathologist William Lewis' photo reminds us that amyloid can also appear in the heart.. Amyloidosis of the heart is a set of complex diseases caused by the accumulation of cellular proteins that form an amyloid plaque. Although http://www.oakleyonorder.com/ amyloidosis was described more than 100 years ago, the causative proteins were not identified until recent chemical analyses were conducted. This image shows an amyloid plaque stained with Congo red stain and viewed through a polarized lens. The optical properties of the amyloid-forming protein cause it to ...
  http://www.emoryhealthsciblog.com/tag/amyloid/
*  Two-photon absorption of polyfluorene aggregates stabilized by insulin amyloid fibrils - RSC Advances (RSC Publishing)
We report on the photophysical and optical properties of a polyfluorene derivative (PFO) and its binding to the amyloid-forming protein insulin. The complexation is based on weak supramolecular interactions between amyloid fibrils and PFO in dissolved and aggregated forms. In particular, complexes of polyflu
  http://pubs.rsc.org/en/Content/ArticleLanding/2015/RA/C5RA08302H
*  Fate of Cerebrospinal Fluid-Borne Amyloid β-Peptide: Rapid Clearance into Blood and Appreciable Accumulation by Cerebral...
Abstract: In Alzheimer's disease, the neuritic or senile amyloid plaques in hippocampus and association cortex, the diffuse plaques in brain areas such as the cerebellum and sensorimotor cortex, and the amyloid deposits in the walls of pial and parenchymal blood vessels are mainly composed of amyloid β-peptides. In the present study, either soluble 40-residue amyloid β-peptide radiolabeled with 125I (I-sAβ) or [14C]polyethylene glycol ([14C]-PEG, a reference material) was briefly infused into one lateral ventricle of normal rats. By 3.5 min, 30% of the I-sAβ was cleared from ventricular CSF into blood; another 30% was removed over the next 6.5 min. No [14C]PEG was lost from the CSF-brain system during the first 5 min, and only 20% was cleared by 10 min. Much of the I-sAβ that reached the subarachnoid space ...
  http://onlinelibrary.wiley.com/doi/10.1046/j.1471-4159.1996.67020880.x/abstract
*  From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological...
Serum amyloid A (SAA) is a major acute phase reactant and a small apolipoprotein of high density lipoproteins (HDL) in the serum. In cases of prolonged inflammation, SAA may form amyloid fibrils, leading to the disease of amyloid A (AA) amyloidosis. Recently, we have shown that murine SAA2.2, a non-amyloidogenic isoform in vivo, forms a hexamer in vitro containing a putative central channel. It is reported herein that upon thermal denaturation, hexameric SAA2.2 irreversibly dissociates to a misfolded monomer at physiological temperature, formation of which coincides with a significant loss of alpha-helical and gain of beta-sheet structure. When SAA2.2 is incubated for several days at 37 degrees C, sedimentation analytical ultracentrifugation reveals the presence of soluble high molecular ...
  https://infoscience.epfl.ch/record/142116
*  "Investigating the Modulation of Aggregating Amyloid Beta 40" by Marlee J. Motes
Amyloid beta protein has been linked to the formation of Alzheimer's disease in patients.¹ Plaques form from amyloid beta fibrils. The formation of these plaques between neural connections in the brain are associated with Alzheimer's disease.² The reduction of the formation of fibrils can be linked to utilizing protein mimics. The protocols that are used to reproduce the simulation of amyloid beta in the brain can be very important. Also, the structure of the protein mimic that is being used to inhibit the formation of fibrils can determine how the amyloid beta plaques are reduced.
  http://scholarworks.uark.edu/cheguht/91/
*  Amyloid Fibril Composition as a Predictor of Development of Cardiomyopathy After Liver Transplantation for Hereditary...
Background. Liver transplantation (LTx) is an accepted treatment for hereditary transthyretin (TTR) amyloidosis (ATTR). However, unforeseen heart complications, especially a rapid development of cardiomyopathy after LTx has affected mortality and morbidity. Recently, a relationship between ATTR-fibril composition and cardiomyopathy has been noted. The aim of this study was to investigate whether development of cardiomyopathy and heart failure in LTx ATTR amyloid patients is related to amyloid fibril composition.. Methods. Twenty-four patients with hereditary ATTR amyloidosis who had undergone LTx and have had their amyloid fibril type tested were available for the study. They had been examined by echocardiography including tissue Doppler and speckle tracking echocardiography before and after LTx. Patients were divided into two groups ...
  http://uu.diva-portal.org/smash/record.jsf?pid=diva2:542919
*  Alzheimer's-causing amyloid and bacteria trigger... UC Davis Health System Feature Story
Andreas Bäumler. The protein forming plaques in Alzheimer's patients is normally soluble. When the protein folds improperly, it forms amyloid deposits that are associated with brain inflammation. Until now, scientists have not been able to identify what causes this destructive, chronic inflammation.. Bäumler and his colleagues did not expect to be studying Alzheimer's disease. They were studying inflammation of the gut caused by bacteria when they discovered that the innate immune system was being triggered by a structural feature of bacterial amyloids and not by the amino acids that make up the proteins in the biofilms.. "When we destroyed the ability of the proteins to aggregate, we no longer saw the same immune response," Bäumler said.. When the researchers figured out the amyloid ...
  http://www.ucdmc.ucdavis.edu/welcome/features/20090909_Alzheimers/index.html
*  Amyloid purpura - wikidoc
The precise cause of amyloid purpura is unknown, but several mechanisms are thought to contribute.[2] One may be a decrease in the level of circulating factor X,[2] a clotting factor necessary for coagulation. The proposed mechanism for this decrease in factor X is that circulating amyloid fibrils bind and inactivate factor X.[2] Another contributing factor may be enhanced fibrinolysis,[2] the breakdown of clots. Subendothelial deposits of amyloid may weaken blood vessels and lead to the extravasation of blood.[2][3] Amyloid deposits in the gastrointestinal tract and liver may also play a role in the development of amyloid purpura.[2] ...
  http://wikidoc.org/index.php/Amyloid_purpura
*  Cannabinoid Effects on β Amyloid Fibril and Aggregate Formation, Neuronal and Microglial-Activated Neurotoxicity In Vitro
Cannabinoid (CB) ligands have demonstrated neuroprotective properties. In this study we compared the effects of a diverse set of CB ligands against β amyloid-mediated neuronal toxicity and activated microglial-conditioned media-based neurotoxicity in vitro, and compared this with a capacity to directly alter β amyloid (Aβ) fibril or aggregate formation. Neuroblastoma (SH-SY5Y) cells were exposed to Aβ1-42 directly or microglial (BV-2 cells) conditioned media activated with lipopolysaccharide (LPS) in the presence of the CB1 receptor-selective agonist ACEA, CB2 receptor-selective agonist JWH-015, phytocannabinoids Δ(9)-THC and cannabidiol (CBD), the endocannabinoids 2-arachidonoyl glycerol (2-AG) and anandamide or putative GPR18/GPR55 ligands O-1602 and abnormal-cannabidiol (Abn-CBD). TNF-α and nitrite production was measured in BV-2 cells to compare activation via LPS or albumin with Aβ1-42. Aβ1-42 evoked a concentration-dependent loss of ...
  http://uu.diva-portal.org/smash/record.jsf?pid=diva2:649280
*  Patent US5223482 - Recombinant Alzheimer's protease inhibitory amyloid protein and method of use - Google Patents
DNA sequences encoding β-amyloid-related proteins associated with Alzheimer's disease are disclosed. Also provided herein is a DNA sequence encoding a novel protease inhibitor. These sequences are used in producing or constructing recombinant β-amyloid core protein, β-amyloid-related proteins and recombinant or synthetic immunogenic peptides. Antibodies generated against the recombinant proteins or immunogenic peptides derived therefrom can be used for cerebral fluid or serum protein diagnosis of Alzheimer's disease.
  http://www.google.com/patents/US5223482?dq=oakley+5,387,949
*  Structure and Biomedical Applications of Amyloid Oligomer Nanoparticles
Amyloid oligomers are nonfibrillar polypeptide aggregates linked to diseases, such as Alzheimer's and Parkinson's. Here we show that these aggregates possess a compact, quasi-crystalline architect ...
  http://www.bionity.com/de/fachpublikationen/731150/structure-and-biomedical-applications-of-amyloid-oligomer-nanoparticles.html
*  The Culprit Is in the Cave : The Core Sites Explain the Binding Profiles of Amyloid-Specific Tracers
The design of molecular probes and tracer molecules with specificity toward amyloid beta (A beta) fibrils is of paramount importance for the selective diagnosis of Alzheimer's disease. This requires a detailed understanding of the binding sites in amyloid targets, their number, and their binding mechanism for various tracer molecules. We adopt an integrated approach including molecular docking, molecular dynamics, and generalized Born-based free energy calculations to investigate site-specific interactions of different amyloid binding molecules. Our study reproduces the experimental results on the relative binding affinity of the tracers and amyloid binders and explains the feature of "multiple binding sites" in amyloid targets as probed by competition binding experiments. A major outcome of this study is that it is the core sites of the Afi ...
  http://uu.diva-portal.org/smash/record.jsf?pid=diva2:1010278
*  ALZFORUM | NETWORKING FOR A CURE
This is a beautiful paper that follows a large body of excellent work from these investigators. However, no data is presented as to how the disruption of the interaction between SAP and amyloid fibrils by their drug candidate affects the fate of the amyloid itself. This paper is focused exclusively on the clearance of SAP from the deposits. The authors state that they hope that the clearance of SAP will 'reduce the stability of amyloid deposits and promote their regression'. This is certainly a reasonable hypothesis, given that other studies have shown amyloid deposits can be cleared and that the SAP knockout mouse showed retarded and reduced disease.. However, it is very important to note that the systemic amyloidoses discussed in this paper seem to be caused by the amyloid fibrils themselves, whereas the ...
  http://www.alzforum.org/papers/amyloid-diseases-small-drugs-lead-attack
*  Chemistry: Faculty and Research
Neurofibrillary tangles (NFTs) are one of the two hallmark lesions of Alzheimer's disease (AD) and their accumulation has been used to assess the severity of the disease. They are composed of paired helical filaments (PHF), a form of amyloid resulting from the aggregation of the microtubule-associated protein tau. Our laboratory has found that peptides as short as 3-6 amino acids are able to initiate the formation of twisted filaments, similar to PHF. We believe that these short amyloid-forming peptides provide an excellent model for studying the structural basis of PHF and amyloid, in general. By understanding the structural basis for amyloid formation, a rational design of therapeutic agents able to prevent PHF accumulation can be undertaken. In addition to using short tau-related peptides to understand the basis of ...
  http://www.utdallas.edu/chemistry/faculty/
*  Kinetic theory of amyloid fibril templating
The growth of amyloid fibrils requires a disordered or partially unfolded protein to bind to the fibril and adapt the same conformation and alignment established by the fibril template. Since the H-bonds stabilizing the fibril are interchangeable, it is inevitable that H-bonds form between incorrect pairs of amino acids which are either incorporated into the fibril as defects or must be broken before the correct alignment can be found. This process is modeled by mapping the formation and breakage of H-bonds to a one-dimensional random walk. The resulting microscopic model of fibril growth is governed by two timescales: the diffusion time of the monomeric proteins, and the time required for incorrectly bound proteins to unbind from the fibril. The theory predicts that the Arrhenius behavior observed in experiments is due to off-pathway states rather than an on-pathway transition state. The predicted growth rates are in ...
  http://krex.k-state.edu/dspace/handle/2097/16213