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Amino Acid
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Amyloid Proteins
Amyloid Proteins
Amyloid proteins are a diverse group of fibrillar proteins that can aggregate and accumluate in tissues, leading to a range of amyloid-related disorders.
These misfolded proteins can self-assemble into insoluble, cross-beta sheet structures that are resistant to degradation.
Amyloid proteins play a key role in neurodegenerative diseases like Alzheimer's and Parkinson's, as well as systemic amyloidoses affecting the heart, kidneys, and other organs.
Understanding the structure, formation, and biological effects of amyloid proteins is crucial for developing effective treatments and therapies.
This MeSH term provides a concise overview of this important class of proteins and their clinical significance.
These misfolded proteins can self-assemble into insoluble, cross-beta sheet structures that are resistant to degradation.
Amyloid proteins play a key role in neurodegenerative diseases like Alzheimer's and Parkinson's, as well as systemic amyloidoses affecting the heart, kidneys, and other organs.
Understanding the structure, formation, and biological effects of amyloid proteins is crucial for developing effective treatments and therapies.
This MeSH term provides a concise overview of this important class of proteins and their clinical significance.
Most cited protocols related to «Amyloid Proteins»
Amygdaloid Body
Amyloid Proteins
Angular Gyrus
AV-1451
Cerebellum
Cortex, Cerebral
Gray Matter
Leg
Pittsburgh compound B
Pons
Posterior Cingulate Cortex
Precuneus
Temporal Lobe
Vermis, Cerebellar
White Matter
Amyloid Proteins
Biological Markers
Patients
Alzheimer's Disease
Amyloid angiopathy
Amyloid Proteins
Autopsy
Brain
Cerebral Infarction
Dementia
Diagnosis
Infarction
Lewy Bodies
Lewy Body Disease
MAPT protein, human
Microscopy
Neurofibrillary Tangle
protein TDP-43, human
Senile Plaques
Silver
SNCA protein, human
Stains
Substantia Nigra
In both cohorts, human brain PET imaging for amyloid deposition was performed using the radiotracer N-methyl-[11C]2-(4-methylaminophenyl)-6-hydroxybenzothiazole (PiB). Preparation of PiB was carried out according to the published protocol [37] . Dynamic PET imaging was conducted with a Siemens 962 HR+ ECAT scanner in three-dimensional mode after intravenous administration of approximately 12mCi of PiB. The images were reconstructed on a 128×128×63 matrix (2.12×2.12×2.43 mm) using filtered back-projection. Typical dynamic scans had 25×5 seconds frames, 9×20 seconds frames, 10×1 minute frames, and 9×5 minutes frames.
For G1, anatomic MRI images were acquired with T1-weighted magnetization-prepared rapid gradient echo (MPRAGE) sequence (1 mm isotropic voxels) variably using a Siemens Trio 3T scanner (N = 72), a Siemens Vision 1.5T (N = 3), or a Siemens Avanto 1.5 T scanner (N = 2). For G2, two MPRAGE scans were acquired during the same MR session for each participant on the Siemens Trio 3T scanner to investigate the impact of FreeSurfer segmentation variability on PET quantification.
For G1, anatomic MRI images were acquired with T1-weighted magnetization-prepared rapid gradient echo (MPRAGE) sequence (1 mm isotropic voxels) variably using a Siemens Trio 3T scanner (N = 72), a Siemens Vision 1.5T (N = 3), or a Siemens Avanto 1.5 T scanner (N = 2). For G2, two MPRAGE scans were acquired during the same MR session for each participant on the Siemens Trio 3T scanner to investigate the impact of FreeSurfer segmentation variability on PET quantification.
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6-hydroxybenzothiazole
Amyloid Proteins
Brain
ECHO protocol
Homo sapiens
Intravenous Infusion
Neoplasm Metastasis
Radionuclide Imaging
Reading Frames
TRIO protein, human
Vision
Amyloid Proteins
CAT SCANNERS X RAY
ECHO protocol
Hypersensitivity
PET protocol
Protocol Compliance
Radionuclide Imaging
Reading Frames
Reconstructive Surgical Procedures
Scan, CT PET
TRIO protein, human
Most recents protocols related to «Amyloid Proteins»
Authorizations for reporting these three cases were granted by the Eastern Ontario Regional Forensic Unit and the Laboratoire de Sciences Judiciaires et de Médecine Légale du Québec.
The sampling followed a relatively standardized protocol for all TBI cases: samples were collected from the cortex and underlying white matter of the pre-frontal gyrus, superior and middle frontal gyri, temporal pole, parietal and occipital lobes, deep frontal white matter, hippocampus, anterior and posterior corpus callosum with the cingula, lenticular nucleus, thalamus with the posterior limb of the internal capsule, midbrain, pons, medulla, cerebellar cortex and dentate nucleus. In some cases, gross pathology (e.g. contusions) mandated further sampling along with the dura and spinal cord if available. The number of available sections for these three cases was 26 for case1, and 24 for cases 2 and 3.
For the detection of ballooned neurons, all HE or HPS sections, including contusions, were screened at 200×.
Representative sections were stained with either hematoxylin–eosin (HE) or hematoxylin-phloxin-saffron (HPS). The following histochemical stains were used: iron, Luxol-periodic acid Schiff (Luxol-PAS) and Bielschowsky. The following antibodies were used for immunohistochemistry: glial fibrillary acidic protein (GFAP) (Leica, PA0026,ready to use), CD-68 (Leica, PA0073, ready to use), neurofilament 200 (NF200) (Leica, PA371, ready to use), beta-amyloid precursor-protein (β-APP) (Chemicon/Millipore, MAB348, 1/5000), αB-crystallin (EMD Millipore, MABN2552 1/1000), ubiquitin (Vector, 1/400), β-amyloid (Dako/Agilent, 1/100), tau protein (Thermo/Fisher, MN1020 1/2500), synaptophysin (Dako/Agilent, ready to use), TAR DNA binding protein 43 (TDP-43) ((Protein Tech, 10,782-2AP, 1/50), fused in sarcoma binding protein (FUS) (Protein tech, 60,160–1-1 g, 1/100), and p62 (BD Transduc, 1/25). In our index cases, the following were used for the evaluation of TAI: β-APP, GFAP, CD68 and NF200; for the neurodegenerative changes: αB-crystallin, NF200, ubiquitin, tau protein, synaptophysin, TDP-43, FUS were used.
For the characterization of the ballooned neurons only, two cases of fronto-temporal lobar degeneration, FTLD-Tau, were used as controls. One was a female aged 72 who presented with speech difficulties followed by neurocognitive decline and eye movement abnormalities raising the possibility of Richardson’s disorder. The other was a male aged 67 who presented with a primary non-fluent aphasia progressing to fronto-temporal demαentia. In both cases, the morphological findings were characteristic of a corticobasal degeneration.
The sampling followed a relatively standardized protocol for all TBI cases: samples were collected from the cortex and underlying white matter of the pre-frontal gyrus, superior and middle frontal gyri, temporal pole, parietal and occipital lobes, deep frontal white matter, hippocampus, anterior and posterior corpus callosum with the cingula, lenticular nucleus, thalamus with the posterior limb of the internal capsule, midbrain, pons, medulla, cerebellar cortex and dentate nucleus. In some cases, gross pathology (e.g. contusions) mandated further sampling along with the dura and spinal cord if available. The number of available sections for these three cases was 26 for case1, and 24 for cases 2 and 3.
For the detection of ballooned neurons, all HE or HPS sections, including contusions, were screened at 200×.
Representative sections were stained with either hematoxylin–eosin (HE) or hematoxylin-phloxin-saffron (HPS). The following histochemical stains were used: iron, Luxol-periodic acid Schiff (Luxol-PAS) and Bielschowsky. The following antibodies were used for immunohistochemistry: glial fibrillary acidic protein (GFAP) (Leica, PA0026,ready to use), CD-68 (Leica, PA0073, ready to use), neurofilament 200 (NF200) (Leica, PA371, ready to use), beta-amyloid precursor-protein (β-APP) (Chemicon/Millipore, MAB348, 1/5000), αB-crystallin (EMD Millipore, MABN2552 1/1000), ubiquitin (Vector, 1/400), β-amyloid (Dako/Agilent, 1/100), tau protein (Thermo/Fisher, MN1020 1/2500), synaptophysin (Dako/Agilent, ready to use), TAR DNA binding protein 43 (TDP-43) ((Protein Tech, 10,782-2AP, 1/50), fused in sarcoma binding protein (FUS) (Protein tech, 60,160–1-1 g, 1/100), and p62 (BD Transduc, 1/25). In our index cases, the following were used for the evaluation of TAI: β-APP, GFAP, CD68 and NF200; for the neurodegenerative changes: αB-crystallin, NF200, ubiquitin, tau protein, synaptophysin, TDP-43, FUS were used.
For the characterization of the ballooned neurons only, two cases of fronto-temporal lobar degeneration, FTLD-Tau, were used as controls. One was a female aged 72 who presented with speech difficulties followed by neurocognitive decline and eye movement abnormalities raising the possibility of Richardson’s disorder. The other was a male aged 67 who presented with a primary non-fluent aphasia progressing to fronto-temporal demαentia. In both cases, the morphological findings were characteristic of a corticobasal degeneration.
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Amyloid beta-Protein Precursor
Amyloid Proteins
Antibodies
Broca Aphasia
Cloning Vectors
Congenital Abnormality
Contusions
Corpus Callosum
Cortex, Cerebellar
Cortex, Cerebral
Corticobasal Degeneration
Crystallins
Dura Mater
Eosin
Eye Abnormalities
Eye Movements
Frontotemporal Lobar Degeneration
FUBP1 protein, human
Glial Fibrillary Acidic Protein
Hematoxylin
Immunohistochemistry
Internal Capsule
Iron
Males
Medial Frontal Gyrus
Medulla Oblongata
Mesencephalon
Movement
Movement Disorders
neurofilament protein H
Neurons
Nucleus, Dentate
Nucleus, Lenticular
Occipital Lobe
Periodic Acid
phloxine
Pons
Proteins
protein TDP-43, human
RNA-Binding Protein FUS
Saffron
Sarcoma
Seahorses
Speech
Spinal Cord
Staining
Synaptophysin
Temporal Lobe
Thalamus
Ubiquitin
White Matter
Woman
The INCREASE study was a randomized controlled trial enrolling community-dwelling adults 65 years and older who did not have dementia and were using at least one PIM as defined in the 2015 Beers Criteria (the most recent version at the time of the study) [13 ]. Complete details of the INCREASE protocol and results are available elsewhere and briefly described below [11 (link), 12 (link)]. After 1:1 randomization that was stratified based on baseline amyloid burden, participants randomized to the control group received usual care with educational pamphlets on medication appropriateness for older adults and risks associated with polypharmacy. In addition to educational materials, participants randomized to the MTM intervention met with the BCGP and a non-pharmacist study clinician (e.g., nurse practitioner, neurologist) to discuss the baseline recommendations. This meeting allowed for 1) participant education on risks, benefits, and alternatives to optimize medication use; and 2) the collection of additional relevant information, including participant beliefs, preferences, and treatment goals. During the MTM team meeting, final recommendations were formalized, and the details of any relevant revisions to the baseline recommendation were noted in the pre-specified data collection forms.
The INCREASE study was approved by the University of Kentucky Institutional Review Board (IRB #43239) and all the study participants provided informed consent. The protocol for the study was registered on clinicaltrials.gov (NCT02849639) on 29/07/2016, in accordance with the relevant guidelines and regulations or in accordance with the Declaration of Helsinki. Study data were collected and managed using the Research Electronic Data Capture (REDCap), a secure, web-based software platform designed to support data capture for research studies [14 (link), 15 (link)].
The INCREASE study was approved by the University of Kentucky Institutional Review Board (IRB #43239) and all the study participants provided informed consent. The protocol for the study was registered on clinicaltrials.gov (NCT02849639) on 29/07/2016, in accordance with the relevant guidelines and regulations or in accordance with the Declaration of Helsinki. Study data were collected and managed using the Research Electronic Data Capture (REDCap), a secure, web-based software platform designed to support data capture for research studies [14 (link), 15 (link)].
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Adult
Aged
Amyloid Proteins
Dementia
Neurologists
Pharmaceutical Preparations
Polypharmacy
Practitioner, Nurse
BDNF (Cusabio, China; CSB-E04505m) and amyloid β1-42 (ThermoFisher Scientific; kit KHB3441) levels in the cerebral cortex homogenate were detected by ELISA according to manufacturer’s instruction. In both cases, 7 animals per group were analyzed and absorbances were read in a Varioskan LUX Multimode Microplate Reader (Thermo Fisher Scientific). Amyloid β1-42 data is expressed in pg/μg protein and BDNF levels are expressed in pg/mg protein.
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Amyloid Proteins
Animals
Cortex, Cerebral
Enzyme-Linked Immunosorbent Assay
Proteins
To analyse differences between sleep groups in demographic characteristics and concurrent health measures (n = 619), we used chi-square or Fisher’s exact test for categorical variables, analysis of variance (ANOVA) for continuous variables [mean (SD) reported] and Kruskal–Wallis tests for Likert-scale variables [median (Q1–Q3) reported]. Post hoc pairwise group differences at unadjusted P < 0.05 were reported. We excluded people who took insulin medication (n = 9) when comparing the HOMA-IR difference across the sleep groups (see Wallace et al.68 (link)). Linear regression was used to assess the relationship between sleep group and concurrent cognitive composite scores after adjusting for covariates [age, sex, education, WRAT3 reading score and the number of prior exposures to the cognitive tests (the practice effect)].
Similarly, to analyse differences between sleep groups and concurrent amyloid burden, we examined data from the subset that had completed at least one PiB PET study [n(%) = 108 (17.4%)]. Kruskal–Wallis tests were used to assess the difference between sleep groups in estimated concurrent global PiB DVR and amyloid chronicity, and Fisher’s exact test was used to analyse the concurrent amyloid PET status difference between sleep groups. In sensitivity analyses, we tested whether there was significant difference of amyloid burden at the most recent PET scan across the alternative sleep group assignments. In the imputed data set, 285 (23.0%) had at least one PiB PET scan, and we tested the difference in estimated concurrent and most recent global PiB DVR and amyloid chronicity among sleep groups.
We compared corrected Akaike information criteria (AICc) model fit statistics across otherwise identical models and considered |ΔAICc| values <2 to represent comparable models. Linear regression was performed for the association between sleep groups and concurrent cognitive composite scores after we removed stroke (n = 10), epilepsy/seizures (n = 13), multiple sclerosis (n = 5) and Parkinson’s disease (n = 2). Since APOE genotype associates with cognition, additional linear regression was performed including APOE e4 carriers in the model, and we compared model fits with the fits of the model in Aim 2 with the participants who have APOE data (n = 538). ΔAICc values were reported.
Similarly, to analyse differences between sleep groups and concurrent amyloid burden, we examined data from the subset that had completed at least one PiB PET study [n(%) = 108 (17.4%)]. Kruskal–Wallis tests were used to assess the difference between sleep groups in estimated concurrent global PiB DVR and amyloid chronicity, and Fisher’s exact test was used to analyse the concurrent amyloid PET status difference between sleep groups. In sensitivity analyses, we tested whether there was significant difference of amyloid burden at the most recent PET scan across the alternative sleep group assignments. In the imputed data set, 285 (23.0%) had at least one PiB PET scan, and we tested the difference in estimated concurrent and most recent global PiB DVR and amyloid chronicity among sleep groups.
We compared corrected Akaike information criteria (AICc) model fit statistics across otherwise identical models and considered |ΔAICc| values <2 to represent comparable models. Linear regression was performed for the association between sleep groups and concurrent cognitive composite scores after we removed stroke (n = 10), epilepsy/seizures (n = 13), multiple sclerosis (n = 5) and Parkinson’s disease (n = 2). Since APOE genotype associates with cognition, additional linear regression was performed including APOE e4 carriers in the model, and we compared model fits with the fits of the model in Aim 2 with the participants who have APOE data (n = 538). ΔAICc values were reported.
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Amyloid Proteins
Apolipoproteins E
Cerebrovascular Accident
Cognition
Cognitive Testing
Epilepsy
Genotype
Hypersensitivity
Insulin
Multiple Sclerosis
Pharmaceutical Preparations
Positron-Emission Tomography
Seizures
Sleep
A subset of WRAP participants complete [11C]PiB58 (link) amyloid PET imaging at the University of Wisconsin—Madison Waisman Brain Imaging Laboratory. Detailed imaging methods have been previously described.59 (link),60 (link) Amyloid burden is assessed as global cortical PiB distribution volume ratio (DVR)20 (link) for continuous analyses, and one DVR threshold of ≥1.2 as defined previously61 (link) is applied for determining PiB positivity (A+). Estimated amyloid chronicity (i.e. estimated years A+) is calculated at time of sleep assessment using previously published methods.62 ,63 (link)
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Amyloid Proteins
Brain
Cortex, Cerebral
Sleep
Top products related to «Amyloid Proteins»
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Innotest β-amyloid1–42 is a laboratory assay kit used to measure the concentration of the β-amyloid1–42 peptide in biological samples. It is designed to provide quantitative in vitro diagnostic results.
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INNOTEST hTAU-Ag is a quantitative in vitro diagnostic test for the measurement of total tau protein in human cerebrospinal fluid. It is intended for use as an aid in the diagnosis of Alzheimer's disease.
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The INNOTEST® PHOSPHO-TAU(181P) is a quantitative in vitro diagnostic test used to measure the concentration of phosphorylated tau protein at threonine 181 (P-tau181) in human cerebrospinal fluid. The test is designed to provide analytical data for clinical laboratory use.
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INNOTEST is a compact and versatile lab equipment that performs immunoassay analysis. It is designed to detect and quantify target analytes in biological samples.
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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Thioflavin S is a fluorescent dye used in research as a labeling agent. It has the ability to selectively bind to and stain specific structures, such as amyloid fibrils. Thioflavin S exhibits an increased fluorescence upon binding, which makes it a useful tool for the detection and quantification of these structures in various applications.
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Thioflavin T (ThT) is a fluorescent dye used as a research tool. It has the ability to bind to amyloid fibrils, a type of protein aggregation, and emit fluorescence upon binding. The core function of ThT is to serve as a detection and quantification method for amyloid formation in various biological samples.
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Thioflavin T is a fluorescent dye used in the detection and quantification of amyloid fibrils. It exhibits enhanced fluorescence upon binding to these protein aggregates. The dye is commonly utilized in various research applications, including the study of protein misfolding and amyloidosis.
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The Eclipse 80i microscope is a high-performance optical microscope designed for a variety of scientific applications. It features a sturdy and ergonomic design, advanced optical components, and a range of accessories to accommodate diverse research needs. The Eclipse 80i provides clear, high-resolution imaging capabilities to support laboratory tasks.
More about "Amyloid Proteins"
Amyloid proteins, also known as amyloidogenic proteins or amyloid fibrils, are a diverse group of misfolded, fibrillar proteins that can aggregate and accumulate in various tissues, leading to a range of amyloid-related disorders.
These insoluble, cross-beta sheet structures are resistant to degradation and play a crucial role in neurodegenerative diseases like Alzheimer's and Parkinson's, as well as systemic amyloidoses affecting the heart, kidneys, and other organs.
Understanding the structure, formation, and biological effects of amyloid proteins is essential for developing effective treatments and therapies.
Techniques like the Innotest β-amyloid1–42, INNOTEST hTAU-Ag, and INNOTEST® PHOSPHO-TAU(181P) assays, as well as the use of dyes like Thioflavin S and Thioflavin T (ThT), are valuable tools for studying amyloid proteins.
The aggregation and deposition of amyloid fibrils can be influenced by various factors, including the presence of DMSO and the use of Bovine serum albumin as a blocking agent.
Microscopic techniques, such as the Eclipse 80i microscope, can be employed to visualize and analyze the morphology of these amyloid structures.
Amyloid proteins are a complex and fascinating class of biomolecules, and their study holds great promise for advancing our understanding of neurodegenerative diseases and developing effective therapies.
By leveraging the latest research methods and technologies, scientists can unlock the power of amyloid protein research and drive innovation in this critical field of study.
These insoluble, cross-beta sheet structures are resistant to degradation and play a crucial role in neurodegenerative diseases like Alzheimer's and Parkinson's, as well as systemic amyloidoses affecting the heart, kidneys, and other organs.
Understanding the structure, formation, and biological effects of amyloid proteins is essential for developing effective treatments and therapies.
Techniques like the Innotest β-amyloid1–42, INNOTEST hTAU-Ag, and INNOTEST® PHOSPHO-TAU(181P) assays, as well as the use of dyes like Thioflavin S and Thioflavin T (ThT), are valuable tools for studying amyloid proteins.
The aggregation and deposition of amyloid fibrils can be influenced by various factors, including the presence of DMSO and the use of Bovine serum albumin as a blocking agent.
Microscopic techniques, such as the Eclipse 80i microscope, can be employed to visualize and analyze the morphology of these amyloid structures.
Amyloid proteins are a complex and fascinating class of biomolecules, and their study holds great promise for advancing our understanding of neurodegenerative diseases and developing effective therapies.
By leveraging the latest research methods and technologies, scientists can unlock the power of amyloid protein research and drive innovation in this critical field of study.