Amyloid. Medical search

A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.

Peptides generated from AMYLOID BETA-PEPTIDES PRECURSOR. An amyloid fibrillar form of these peptides is the major component of amyloid plaques found in individuals with Alzheimer's disease and in aged individuals with trisomy 21 (DOWN SYNDROME). The peptide is found predominantly in the nervous system, but there have been reports of its presence in non-neural tissue.

An ACUTE PHASE REACTION protein present in low concentrations in normal sera, but found at higher concentrations in sera of older persons and in patients with AMYLOIDOSIS. It is the circulating precusor of amyloid A protein, which is found deposited in AA type AMYLOID FIBRILS.

A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.

Accumulations of extracellularly deposited AMYLOID FIBRILS within tissues.

A pancreatic beta-cell hormone that is co-secreted with INSULIN. It displays an anorectic effect on nutrient metabolism by inhibiting gastric acid secretion, gastric emptying and postprandial GLUCAGON secretion. Islet amyloid polypeptide can fold into AMYLOID FIBRILS that have been found as a major constituent of pancreatic AMYLOID DEPOSITS.

A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits.

A heterogeneous group of sporadic or familial disorders characterized by AMYLOID deposits in the walls of small and medium sized blood vessels of CEREBRAL CORTEX and MENINGES. Clinical features include multiple, small lobar CEREBRAL HEMORRHAGE; cerebral ischemia (BRAIN ISCHEMIA); and CEREBRAL INFARCTION. Cerebral amyloid angiopathy is unrelated to generalized AMYLOIDOSIS. Amyloidogenic peptides in this condition are nearly always the same ones found in ALZHEIMER DISEASE. (from Kumar: Robbins and Cotran: Pathologic Basis of Disease, 7th ed., 2005)

Amyloid P component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin) structure. It is an acute phase protein, modulates immunologic responses, inhibits ELASTASE, and has been suggested as an indicator of LIVER DISEASE.

Disorders of the peripheral nervous system associated with the deposition of AMYLOID in nerve tissue. Familial, primary (nonfamilial), and secondary forms have been described. Some familial subtypes demonstrate an autosomal dominant pattern of inheritance. Clinical manifestations include sensory loss, mild weakness, autonomic dysfunction, and CARPAL TUNNEL SYNDROME. (Adams et al., Principles of Neurology, 6th ed, p1349)

Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.

A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)

An acid dye used in testing for hydrochloric acid in gastric contents. It is also used histologically to test for AMYLOIDOSIS.

Inherited disorders of the peripheral nervous system associated with the deposition of AMYLOID in nerve tissue. The different clinical types based on symptoms correspond to the presence of a variety of mutations in several different proteins including transthyretin (PREALBUMIN); APOLIPOPROTEIN A-I; and GELSOLIN.

A tetrameric protein, molecular weight between 50,000 and 70,000, consisting of 4 equal chains, and migrating on electrophoresis in 3 fractions more mobile than serum albumin. Its concentration ranges from 7 to 33 per cent in the serum, but levels decrease in liver disease.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.

Integral membrane protein of Golgi and endoplasmic reticulum. Its homodimer is an essential component of the gamma-secretase complex that catalyzes the cleavage of membrane proteins such as NOTCH RECEPTORS and AMYLOID BETA-PEPTIDES precursors. PSEN1 mutations cause early-onset ALZHEIMER DISEASE type 3 that may occur as early as 30 years of age in humans.

Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.

The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.

A familial disorder marked by AMYLOID deposits in the walls of small and medium sized blood vessels of CEREBRAL CORTEX and MENINGES.

Small proteinaceous infectious particles which resist inactivation by procedures that modify NUCLEIC ACIDS and contain an abnormal isoform of a cellular protein which is a major and necessary component. The abnormal (scrapie) isoform is PrPSc (PRPSC PROTEINS) and the cellular isoform PrPC (PRPC PROTEINS). The primary amino acid sequence of the two isoforms is identical. Human diseases caused by prions include CREUTZFELDT-JAKOB SYNDROME; GERSTMANN-STRAUSSLER SYNDROME; and INSOMNIA, FATAL FAMILIAL.

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

Diseases in which there is a familial pattern of AMYLOIDOSIS.

Abnormal structures located in various parts of the brain and composed of dense arrays of paired helical filaments (neurofilaments and microtubules). These double helical stacks of transverse subunits are twisted into left-handed ribbon-like filaments that likely incorporate the following proteins: (1) the intermediate filaments: medium- and high-molecular-weight neurofilaments; (2) the microtubule-associated proteins map-2 and tau; (3) actin; and (4) UBIQUITINS. As one of the hallmarks of ALZHEIMER DISEASE, the neurofibrillary tangles eventually occupy the whole of the cytoplasm in certain classes of cell in the neocortex, hippocampus, brain stem, and diencephalon. The number of these tangles, as seen in post mortem histology, correlates with the degree of dementia during life. Some studies suggest that tangle antigens leak into the systemic circulation both in the course of normal aging and in cases of Alzheimer disease.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Microtubule-associated proteins that are mainly expressed in neurons. Tau proteins constitute several isoforms and play an important role in the assembly of tubulin monomers into microtubules and in maintaining the cytoskeleton and axonal transport. Aggregation of specific sets of tau proteins in filamentous inclusions is the common feature of intraneuronal and glial fibrillar lesions (NEUROFIBRILLARY TANGLES; NEUROPIL THREADS) in numerous neurodegenerative disorders (ALZHEIMER DISEASE; TAUOPATHIES).

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.

Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.

A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.

Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.

The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.

Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

An enzyme the catalyzes the degradation of insulin, glucagon and other polypeptides. It is inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not phosphoramidon. (Eur J Biochem 1994;223:1-5) EC 3.4.24.56.

Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Vaccines or candidate vaccines used to prevent or treat ALZHEIMER DISEASE.

The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

A curved elevation of GRAY MATTER extending the entire length of the floor of the TEMPORAL HORN of the LATERAL VENTRICLE (see also TEMPORAL LOBE). The hippocampus proper, subiculum, and DENTATE GYRUS constitute the hippocampal formation. Sometimes authors include the ENTORHINAL CORTEX in the hippocampal formation.

A synuclein that is a major component of LEWY BODIES that plays a role in neurodegeneration and neuroprotection.

The thin layer of GRAY MATTER on the surface of the CEREBRAL HEMISPHERES that develops from the TELENCEPHALON and folds into gyri and sulchi. It reaches its highest development in humans and is responsible for intellectual faculties and higher mental functions.

A spectroscopic technique in which a range of wavelengths is presented simultaneously with an interferometer and the spectrum is mathematically derived from the pattern thus obtained.

Histochemical localization of immunoreactive substances using labeled antibodies as reagents.

The delicate interlacing threads, formed by aggregations of neurofilaments and neurotubules, coursing through the CYTOPLASM of the body of a NEURON and extending from one DENDRITE into another or into the AXON.

A class of protein components which can be found in several lipoproteins including HIGH-DENSITY LIPOPROTEINS; VERY-LOW-DENSITY LIPOPROTEINS; and CHYLOMICRONS. Synthesized in most organs, Apo E is important in the global transport of lipids and cholesterol throughout the body. Apo E is also a ligand for LDL receptors (RECEPTORS, LDL) that mediates the binding, internalization, and catabolism of lipoprotein particles in cells. There are several allelic isoforms (such as E2, E3, and E4). Deficiency or defects in Apo E are causes of HYPERLIPOPROTEINEMIA TYPE III.

An autosomal dominant familial prion disease with a wide spectrum of clinical presentations including ATAXIA, spastic paraparesis, extrapyramidal signs, and DEMENTIA. Clinical onset is in the third to sixth decade of life and the mean duration of illness prior to death is five years. Several kindreds with variable clinical and pathologic features have been described. Pathologic features include cerebral prion protein amyloidosis, and spongiform or neurofibrillary degeneration. (From Brain Pathol 1998 Jul;8(3):499-513; Brain Pathol 1995 Jan;5(1):61-75)

Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.

A major and the second most common isoform of apolipoprotein E. In humans, Apo E4 differs from APOLIPOPROTEIN E3 at only one residue 112 (cysteine is replaced by arginine), and exhibits a lower resistance to denaturation and greater propensity to form folded intermediates. Apo E4 is a risk factor for ALZHEIMER DISEASE and CARDIOVASCULAR DISEASES.

The third type of glial cell, along with astrocytes and oligodendrocytes (which together form the macroglia). Microglia vary in appearance depending on developmental stage, functional state, and anatomical location; subtype terms include ramified, perivascular, ameboid, resting, and activated. Microglia clearly are capable of phagocytosis and play an important role in a wide spectrum of neuropathologies. They have also been suggested to act in several other roles including in secretion (e.g., of cytokines and neural growth factors), in immunological processing (e.g., antigen presentation), and in central nervous system development and remodeling.

The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Integral membrane proteins and essential components of the gamma-secretase complex that catalyzes the cleavage of membrane proteins such as NOTCH RECEPTORS and AMYLOID BETA-PEPTIDES precursors. Mutations of presenilins lead to presenile ALZHEIMER DISEASE with onset before age 65 years.

The rate dynamics in chemical or physical systems.

Hereditary and sporadic conditions which are characterized by progressive nervous system dysfunction. These disorders are often associated with atrophy of the affected central or peripheral nervous system structures.

G-protein coupled receptors that are formed through the dimerization of the CALCITONIN RECEPTOR with a RECEPTOR ACTIVITY-MODIFYING PROTEIN. Their affinity for ISLET AMYLOID POLYPEPTIDE is dependent upon which of several receptor activity-modifying protein subtypes they are bound to.

Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.

Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN.

Proteins prepared by recombinant DNA technology.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.

An imaging technique using compounds labelled with short-lived positron-emitting radionuclides (such as carbon-11, nitrogen-13, oxygen-15 and fluorine-18) to measure cell metabolism. It has been useful in study of soft tissues such as CANCER; CARDIOVASCULAR SYSTEM; and brain. SINGLE-PHOTON EMISSION-COMPUTED TOMOGRAPHY is closely related to positron emission tomography, but uses isotopes with longer half-lives and resolution is lower.

An early local inflammatory reaction to insult or injury that consists of fever, an increase in inflammatory humoral factors, and an increased synthesis by hepatocytes of a number of proteins or glycoproteins usually found in the plasma.

A CELL LINE derived from a PHEOCHROMOCYTOMA of the rat ADRENAL MEDULLA. PC12 cells stop dividing and undergo terminal differentiation when treated with NERVE GROWTH FACTOR, making the line a useful model system for NERVE CELL differentiation.

NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.

Learning the correct route through a maze to obtain reinforcement. It is used for human or animal populations. (Thesaurus of Psychological Index Terms, 6th ed)

An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

Elements of limited time intervals, contributing to particular results or situations.

The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

A non-aqueous co-solvent that serves as tool to study protein folding. It is also used in various pharmaceutical, chemical and engineering applications.

A group of genetic, infectious, or sporadic degenerative human and animal nervous system disorders associated with abnormal PRIONS. These diseases are characterized by conversion of the normal prion protein to an abnormal configuration via a post-translational process. In humans, these conditions generally feature DEMENTIA; ATAXIA; and a fatal outcome. Pathologic features include a spongiform encephalopathy without evidence of inflammation. The older literature occasionally refers to these as unconventional SLOW VIRUS DISEASES. (From Proc Natl Acad Sci USA 1998 Nov 10;95(23):13363-83)

The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.

Chemicals and substances that impart color including soluble dyes and insoluble pigments. They are used in INKS; PAINTS; and as INDICATORS AND REAGENTS.

Compounds with a benzene ring fused to a thiazole ring.

The production of a dense fibrous network of neuroglia; includes astrocytosis, which is a proliferation of astrocytes in the area of a degenerative lesion.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Changes in the amounts of various chemicals (neurotransmitters, receptors, enzymes, and other metabolites) specific to the area of the central nervous system contained within the head. These are monitored over time, during sensory stimulation, or under different disease states.

Established cell cultures that have the potential to propagate indefinitely.

Islet amyloid polypeptide/amylin messenger RNA and protein expression in human insulinomas in relation to amyloid formation. (1/3010)

OBJECTIVE: Islet amyloid polypeptide (IAPP), also named amylin, is the predominant protein component of amyloid deposits in human islet beta cell tumours of the pancreas (insulinomas). IAPP is co-produced with insulin by islet beta cells. We investigated IAPP expression in relation to insulin expression and to amyloid formation in eleven insulinomas. DESIGN AND METHODS: RNA and protein extracts were prepared from the same pieces of tumour tissue, and from specimens of two normal human pancreata. IAPP and insulin mRNA and peptide content were quantified using Northern blot analysis and radioimmunoassay (RIA) respectively. Molecular forms of IAPP immunoreactivity were analysed by reversed-phase high-performance liquid chromatography (HPLC). The presence of islet hormones and of amyloid was assessed by (immuno)histochemical staining of paraffin sections. Plasma levels of IAPP and insulin prior to tumour resection were determined by RIA. RESULTS: IAPP and insulin mRNA and peptide content varied widely between the tumour specimens, and there was considerable intratumour heterogeneity of peptide content. HPLC analysis indicated correct proteolytic processing of the IAPP precursor protein. Amyloid deposits were detected only in the three tumours with the highest IAPP content. In contrast to insulin, plasma levels of IAPP were not elevated in the insulinoma patients. CONCLUSIONS: The spectrum of hormone production by insulinomas cannot be inferred from only a few tissue sections due to intratumour heterogeneity. Expression of the IAPP and insulin genes is not coupled in insulinomas, which produce properly processed mature IAPP. In addition to IAPP overproduction, additional factors such as intracellular accumulation of IAPP are involved in amyloidogenesis in insulinomas. (+info)

Prion domain initiation of amyloid formation in vitro from native Ure2p. (2/3010)

The [URE3] non-Mendelian genetic element of Saccharomyces cerevisiae is an infectious protein (prion) form of Ure2p, a regulator of nitrogen catabolism. Here, synthetic Ure2p1-65 were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent beta sheet. Ure2p1-65 specifically induced full-length native Ure2p to copolymerize under conditions where native Ure2p alone did not polymerize. Like Ure2p in extracts of [URE3] strains, these 180- to 220-angstrom-diameter filaments were protease resistant. The Ure2p1-65-Ure2p cofilaments could seed polymerization of native Ure2p to form thicker, less regular filaments. All filaments stained with Congo Red to produce the green birefringence typical of amyloid. This self-propagating amyloid formation can explain the properties of [URE3]. (+info)

Interaction of amylin with calcitonin gene-related peptide receptors in the microvasculature of the hamster cheek pouch in vivo. (3/3010)

1. This study used intravital microscopy to investigate the receptors stimulated by amylin which shares around 50% sequence homology with the vasodilator calcitonin gene-related peptide (CGRP) in the hamster cheek pouch microvasculature in vivo. 2. Receptor agonists dilated arterioles (diameters 20-40 microm). The -log of the concentrations (+/- s.e.mean; n = 8) causing 50% increase in arteriole diameter were: human betaCGRP (10.8 +/- 0.3), human alphaCGRP (10.8 +/- 0.4), rat alphaCGRP (10.4 +/- 0.3). Rat amylin and the CGRP2 receptor selective agonist [Cys(ACM2,7]-human alphaCGRP were 100 fold less potent (estimates were 8.5 +/- 0.4 and 8.2 +/- 0.3 respectively). 3. The GCRP1 receptor antagonist, CGRP8-37 (300 nmol kg(-1); i.v.) reversibly inhibited the increase in diameter evoked by human alphaCGRP (0.3 nM) from 178 +/- 22% to 59 +/- 12% (n = 8; P < 0.05) and by rat amylin (100 nM) from 138 +/- 23% to 68 +/- 24% (n = 6; P < 0.05). CGRP8-37 did not inhibit vasodilation evoked by substance P (10 nM; n = 4: P > 0.05). 4. The amylin receptor antagonist, amylin8-37 (300 nmol kg(-1); i.v.) did not significantly inhibit the increase in diameter evoked by human alphaCGRP (0.3 nM) which was 112 +/- 26% in the absence, and 90 +/- 29% in the presence of antagonist (n = 4; P < 0.05); nor that evoked by rat amylin (100 nM) which was 146 +/- 23% in the absence and 144 +/- 32% in the presence of antagonist (n = 4; P > 0.05). 5. The agonist profile for vasodilatation and the inhibition of this dilatation by CGRP8-37, although not the amylin8-37 indicates that amylin causes vasodilatation through interaction with CGRP1 receptors in the hamster cheek pouch. (+info)

The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. (4/3010)

NIDDM is characterized by islet amyloid deposits and decreased beta-cell mass. Islet amyloid is derived from the locally expressed protein islet amyloid polypeptide (IAPP). While it is now widely accepted that abnormal aggregation of IAPP has a role in beta-cell death in NIDDM, the mechanism remains unknown. We hypothesized that small IAPP aggregates, rather than mature large amyloid deposits, are cytotoxic. Consistent with this hypothesis, freshly dissolved human (h)-IAPP was cytotoxic when added to dispersed mouse and human islet cells, provoking the formation of abnormal vesicle-like membrane structures in association with vacuolization and cell death. Human islet cell death occurred by both apoptosis and necrosis, predominantly between 24 and 48 h after exposure to h-IAPP. In contrast, the addition to dispersed islet cells of matured h-IAPP containing large amyloid deposits of organized fibrils was seldom associated with vesicle-like structures or features of cell death, even though the cells were often encased in the larger amyloid deposits. Based on these observations, we hypothesized that h-IAPP cytotoxicity is mediated by membrane damage induced by early h-IAPP aggregates. Consistent with this hypothesis, application of freshly dissolved h-IAPP to voltage-clamped planar bilayer membranes (a cell-free in vitro system) also caused membrane instability manifested as a marked increase in conductance, increased membrane electrical noise, and accelerated membrane breakage, effects that were absent using matured h-IAPP or rat IAPP solutions. Light-scattering techniques showed that membrane toxicity corresponded to h-IAPP aggregates containing approximately 25-6,000 IAPP molecules, an intermediate-sized amyloid particle that we term intermediate-sized toxic amyloid particles (ISTAPs). We conclude that freshly dissolved h-IAPP is cytotoxic and that this cytotoxicity is mediated through an interaction of ISTAPs with cellular membranes. Once ISTAPs mature into amyloid deposits comprising >10(6) molecules, the capacity of h-IAPP to cause membrane instability and islet cell death is significantly reduced or abolished. These data may have implications for the mechanism of cell death in other diseases characterized by local amyloid formation (such as Alzheimer's disease). (+info)

Specific gene expression in pancreatic beta-cells: cloning and characterization of differentially expressed genes. (5/3010)

Identification and characterization of genes expressed preferentially in pancreatic beta-cells will clarify the mechanisms involved in the specialized properties of these cells, as well as providing new markers of the development of type 1 diabetes. Despite major efforts, relatively few beta-cell-specific genes have been characterized. We applied representational difference analysis to identify genes expressed selectively in the pancreatic beta-cell line betaTC1 compared with the pancreatic alpha-cell line alphaTC1 and isolated 26 clones expressed at higher levels in the beta-cells than in the alpha-cells. DNA sequencing revealed that 14 corresponded to known genes (that is, present in GenBank). Only four of those genes had been shown previously to be expressed at higher levels in beta-cells (insulin, islet amyloid polypeptide, neuronatin, and protein kinase A regulatory subunit [RIalpha]). The known genes include transcription factors (STAT6) and mediators of signal transduction (guanylate cyclase). The remaining 12 genes are absent from the GenBank database or are present as expressed sequence tag (EST) sequences (4 clones). Some of the genes are expressed in a highly specific pattern-expression in betaTC1 and islet cells and in relatively few of the non-beta-cell types examined; others are expressed in most cell types tested. The identification of these differentially expressed genes may aid in attaining a clearer understanding of the mechanisms involved in beta-cell function and of the possible immunogens involved in development of type 1 diabetes. (+info)

Colchicine inhibition of the first phase of amyloid synthesis in experimental animals. (6/3010)

Colchicine was found to inhibit the first phase of casein-induced synthesis of murine amyloid. When mice were treated with colchicine during the first 7 days of an amyloid induction regimen or when colchicine was given to the donor mice in a transfer model, the amyloidogenic stimulus of casein was blocked completely. Amyloid synthesis was however, not interrupted by the administration of colchicine during the last 7 days of the casein regimen nor by colchicine treatment of recipient mice in a transfer model. (+info)

Ancestral origins and worldwide distribution of the PRNP 200K mutation causing familial Creutzfeldt-Jakob disease. (7/3010)

Creutzfeldt-Jakob disease (CJD) belongs to a group of prion diseases that may be infectious, sporadic, or hereditary. The 200K point mutation in the PRNP gene is the most frequent cause of hereditary CJD, accounting for >70% of families with CJD worldwide. Prevalence of the 200K variant of familial CJD is especially high in Slovakia, Chile, and Italy, and among populations of Libyan and Tunisian Jews. To study ancestral origins of the 200K mutation-associated chromosomes, we selected microsatellite markers flanking the PRNP gene on chromosome 20p12-pter and an intragenic single-nucleotide polymorphism at the PRNP codon 129. Haplotypes were constructed for 62 CJD families originating from 11 world populations. The results show that Libyan, Tunisian, Italian, Chilean, and Spanish families share a major haplotype, suggesting that the 200K mutation may have originated from a single mutational event, perhaps in Spain, and spread to all these populations with Sephardic migrants expelled from Spain in the Middle Ages. Slovakian families and a family of Polish origin show another unique haplotype. The haplotypes in families from Germany, Sicily, Austria, and Japan are different from the Mediterranean or eastern European haplotypes. On the basis of this study, we conclude that founder effect and independent mutational events are responsible for the current geographic distribution of hereditary CJD associated with the 200K mutation. (+info)

Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. (8/3010)

The most common form of systemic amyloidosis originates from antibody light chains. The large number of amino acid variations that distinguish amyloidogenic from nonamyloidogenic light chain proteins has impeded our understanding of the structural basis of light-chain fibril formation. Moreover, even among the subset of human light chains that are amyloidogenic, many primary structure differences are found. We compared the thermodynamic stabilities of two recombinant kappa4 light-chain variable domains (V(L)s) derived from amyloidogenic light chains with a V(L) from a benign light chain. The amyloidogenic V(L)s were significantly less stable than the benign V(L). Furthermore, only the amyloidogenic V(L)s formed fibrils under native conditions in an in vitro fibril formation assay. We used site-directed mutagenesis to examine the consequences of individual amino acid substitutions found in the amyloidogenic V(L)s on stability and fibril formation capability. Both stabilizing and destabilizing mutations were found; however, only destabilizing mutations induced fibril formation in vitro. We found that fibril formation by the benign V(L) could be induced by low concentrations of a denaturant. This indicates that there are no structural or sequence-specific features of the benign V(L) that are incompatible with fibril formation, other than its greater stability. These studies demonstrate that the V(L) beta-domain structure is vulnerable to destabilizing mutations at a number of sites, including complementarity determining regions (CDRs), and that loss of variable domain stability is a major driving force in fibril formation. (+info)

The term "amyloid" refers specifically to the type of protein aggregate that forms these plaques, and is derived from the Greek word for "flour-like." Amyloidosis is the general term used to describe the condition of having amyloid deposits in the body, while Alzheimer's disease is a specific type of amyloidosis that is characterized by the accumulation of beta-amyloid peptides in the brain.

Plaques, amyloid play a central role in the pathogenesis of many neurodegenerative diseases, and understanding their formation and clearance is an area of ongoing research. In addition to their role in Alzheimer's disease, amyloid plaques have been implicated in other conditions such as cerebral amyloid angiopathy, primary lateral sclerosis, and progressive supranuclear palsy.

Plaques, amyloid are composed of a variety of proteins, including beta-amyloid peptides, tau protein, and apolipoprotein E (apoE). The composition and structure of these plaques can vary depending on the underlying disease, and their presence is often associated with inflammation and oxidative stress.

In addition to their role in neurodegeneration, amyloid plaques have been implicated in other diseases such as type 2 diabetes and cardiovascular disease. The accumulation of amyloid fibrils in these tissues can contribute to the development of insulin resistance and atherosclerosis, respectively.

Overall, plaques, amyloid are a complex and multifaceted area of research, with many open questions remaining about their formation, function, and clinical implications. Ongoing studies in this field may provide valuable insights into the pathogenesis of various diseases and ultimately lead to the development of novel therapeutic strategies for these conditions.

In conclusion, plaques, amyloid are a hallmark of several neurodegenerative diseases, including Alzheimer's disease, and have been associated with inflammation, oxidative stress, and neurodegeneration. The composition and structure of these plaques can vary depending on the underlying disease, and their presence is often linked to the progression of the condition. Furthermore, amyloid plaques have been implicated in other diseases such as type 2 diabetes and cardiovascular disease, highlighting their potential clinical significance beyond neurodegeneration. Ongoing research into the mechanisms of amyloid plaque formation and clearance may lead to the development of novel therapeutic strategies for these conditions.

There are several types of amyloidosis, each with different causes and symptoms. The most common types include:

1. Primary amyloidosis: This type is caused by the production of abnormal proteins in the bone marrow. It mainly affects older adults and can lead to symptoms such as fatigue, weight loss, and numbness or tingling in the hands and feet.
2. Secondary amyloidosis: This type is caused by other conditions, such as rheumatoid arthritis, tuberculosis, or inflammatory bowel disease. It can also be caused by long-term use of certain medications, such as antibiotics or chemotherapy.
3. Familial amyloid polyneuropathy: This type is inherited and affects the nerves in the body, leading to symptoms such as muscle weakness, numbness, and pain.
4. Localized amyloidosis: This type affects a specific area of the body, such as the tongue or the skin.

The symptoms of amyloidosis can vary depending on the organs affected and the severity of the condition. Some common symptoms include:

1. Fatigue
2. Weakness
3. Pain
4. Numbness or tingling in the hands and feet
5. Swelling in the legs, ankles, and feet
6. Difficulty with speech or swallowing
7. Seizures
8. Heart problems
9. Kidney failure
10. Liver failure

The diagnosis of amyloidosis is based on a combination of physical examination, medical history, laboratory tests, and imaging studies. Laboratory tests may include blood tests to measure the levels of certain proteins in the body, as well as biopsies to examine tissue samples under a microscope. Imaging studies, such as X-rays, CT scans, and MRI scans, may be used to evaluate the organs affected by the condition.

There is no cure for amyloidosis, but treatment can help manage the symptoms and slow the progression of the disease. Treatment options may include:

1. Medications to control symptoms such as pain, swelling, and heart problems
2. Chemotherapy to reduce the production of abnormal proteins
3. Autologous stem cell transplantation to replace damaged cells with healthy ones
4. Dialysis to remove excess fluids and waste products from the body
5. Nutritional support to ensure adequate nutrition and hydration
6. Physical therapy to maintain muscle strength and mobility
7. Supportive care to manage pain, improve quality of life, and reduce stress on the family.

In conclusion, amyloidosis is a complex and rare group of diseases that can affect multiple organs and systems in the body. Early diagnosis and treatment are essential to managing the symptoms and slowing the progression of the disease. It is important for patients with suspected amyloidosis to seek medical attention from a specialist, such as a hematologist or nephrologist, for proper evaluation and treatment.

The term "cerebral" refers to the brain, "amyloid" refers to the abnormal protein deposits, and "angiopathy" refers to the damage caused to the blood vessels. CAA is often associated with other conditions such as Alzheimer's disease, Down syndrome, and other forms of dementia.

CAA is a type of small vessel ischemic disease (SVID), which affects the smaller blood vessels in the brain. The exact cause of CAA is not yet fully understood, but it is thought to be related to a combination of genetic and environmental factors. There is currently no cure for CAA, but researchers are working to develop new treatments to slow its progression and manage its symptoms.

Some common symptoms of CAA include:

* Cognitive decline
* Seizures
* Stroke-like episodes
* Memory loss
* Confusion
* Difficulty with coordination and balance

If you suspect you or a loved one may be experiencing symptoms of CAA, it is important to speak with a healthcare professional for proper diagnosis and treatment. A thorough medical history and physical examination, along with imaging tests such as MRI or CT scans, can help confirm the presence of CAA.

While there is no cure for CAA, there are several treatment options available to manage its symptoms and slow its progression. These may include medications to control seizures, improve cognitive function, and reduce inflammation. In some cases, surgery or endovascular procedures may be necessary to repair or remove damaged blood vessels.

It is important to note that CAA is a complex condition, and its management requires a multidisciplinary approach involving neurologists, geriatricians, radiologists, and other healthcare professionals. With proper diagnosis and treatment, however, many individuals with CAA are able to lead active and fulfilling lives.

Amyloidosis can affect many different parts of the body, including the nervous system, the heart, the kidneys, the liver, and other organs. In the nervous system, amyloid accumulation can lead to various neurodegenerative disorders, such as Alzheimer's disease, Parkinson's disease, prion diseases, and others.

Amyloid deposits in the nervous system can cause a range of symptoms including cognitive decline, memory loss, confusion, language impairment, and difficulty with coordination and movement. In addition, amyloid accumulation can lead to inflammation, oxidative stress, and excitotoxicity, which can further exacerbate neurodegeneration.

There are several types of amyloidosis that can affect the nervous system, including:

1. Alzheimer's disease: This is a progressive neurodegenerative disorder that is characterized by the accumulation of beta-amyloid peptides in the brain, leading to cognitive decline and memory loss.
2. Parkinson's disease: This is a neurodegenerative disorder that affects movement, balance, and coordination. It is characterized by the accumulation of alpha-synuclein protein in the brain.
3. Prion diseases: These are a group of rare, progressive neurodegenerative disorders that are caused by misfolded prion proteins. They can affect both the central and peripheral nervous systems.
4. Other forms of amyloidosis: There are several other forms of amyloidosis that can affect the nervous system, including primary lateral sclerosis, progressive supranuclear palsy, and corticobasal degeneration.

Amyloidosis can be diagnosed through a combination of clinical evaluation, imaging studies, and biopsy. Treatment options for amyloidosis vary depending on the underlying cause and severity of the disease. Some common treatments include:

1. Medications: There are several medications that can be used to treat amyloidosis, including cholinesterase inhibitors, dopamine agonists, and memantine.
2. Physical therapy: Physical therapy can help improve mobility, balance, and coordination in people with amyloidosis.
3. Speech therapy: Speech therapy can help improve communication and swallowing difficulties in people with amyloidosis.
4. Occupational therapy: Occupational therapy can help people with amyloidosis adapt to changes in their daily living activities and maintain their independence.
5. Surgery: In some cases, surgery may be necessary to relieve pressure on the brain or spinal cord caused by amyloid accumulation.

Currently, there is no cure for amyloidosis, but early diagnosis and treatment can help manage symptoms and improve quality of life. Research into new treatments and therapies is ongoing, including clinical trials exploring the use of stem cells, gene therapy, and immunotherapy to treat amyloidosis.

The symptoms of Alzheimer's disease can vary from person to person and may progress slowly over time. Early symptoms may include memory loss, confusion, and difficulty with problem-solving. As the disease progresses, individuals may experience language difficulties, visual hallucinations, and changes in mood and behavior.

There is currently no cure for Alzheimer's disease, but there are several medications and therapies that can help manage its symptoms and slow its progression. These include cholinesterase inhibitors, memantine, and non-pharmacological interventions such as cognitive training and behavioral therapy.

Alzheimer's disease is a significant public health concern, affecting an estimated 5.8 million Americans in 2020. It is the sixth leading cause of death in the United States, and its prevalence is expected to continue to increase as the population ages.

There is ongoing research into the causes and potential treatments for Alzheimer's disease, including studies into the role of inflammation, oxidative stress, and the immune system. Other areas of research include the development of biomarkers for early detection and the use of advanced imaging techniques to monitor progression of the disease.

Overall, Alzheimer's disease is a complex and multifactorial disorder that poses significant challenges for individuals, families, and healthcare systems. However, with ongoing research and advances in medical technology, there is hope for improving diagnosis and treatment options in the future.

Amyloidosis is a condition characterized by extracellular amyloid fibrils that are composed of insoluble, abnormal proteins. These fibrils accumulate in different parts of the body, leading to various symptoms and clinical manifestations depending on the type of protein involved.

There are several types of amyloidosis, including:

* Familial amyloid polyneuropathy (FAP): A rare inherited disorder caused by mutations in the transthyretin (TTR) gene, leading to progressive degeneration of the peripheral nerves.
* Familial amyloid cardiomyopathy: A rare inherited heart condition caused by mutations in the TTR gene, leading to progressive cardiac dysfunction and heart failure.
* Primary lateral sclerosis (PLS): A rare progressive neurodegenerative disorder characterized by weakness of the muscles of the limbs, face, and other parts of the body.
* Callidurin amyloidosis: A rare inherited disorder caused by mutations in the callidurin (CAL) gene, leading to progressive degeneration of the peripheral nerves.

The symptoms of these disorders vary depending on the type and severity of the condition, but may include muscle weakness, atrophy, and wasting; numbness or loss of sensation in the limbs; pain; cramping; and difficulty with walking, balance, and coordination. Diagnosis is typically made through a combination of clinical evaluation, imaging studies (such as MRI), and genetic testing. Treatment options are limited for these disorders and focus on managing symptoms and slowing disease progression.

The term 'familial' refers to the fact that CAA is inherited in an autosomal dominant pattern, meaning that a single copy of the mutated gene is enough to cause the condition. This means that if one parent has the mutation, each child has a 50% chance of inheriting the mutated gene. The age of onset and severity of symptoms can vary widely among individuals with CAA, even within the same family.

There are several types of CAA, including:

1. Cerebral Amyloid Angiopathy, type 1 (CAA1): This is the most common form of CAA and is caused by mutations in the PROAPLIN1 gene.
2. Cerebral Amyloid Angiopathy, type 2 (CAA2): This form of CAA is less common and is caused by mutations in the PROAPLIN2 gene.
3. Cerebral Amyloid Angiopathy, type 3 (CAA3): This rare form of CAA is caused by mutations in the AGT gene.

There is currently no cure for CAA, but research is ongoing to develop new treatments and therapies to slow or halt the progression of the disease. Management of symptoms and prevention of complications are key components of care for individuals with CAA.

The different types of familial amyloidosis include:

1. Familial amyloid polyneuropathy (FAP): This is the most common type of familial amyloidosis and is characterized by the accumulation of amyloid fibers in the nerves, leading to progressive nerve damage and loss of sensation.
2. Familial amyloid cardiomyopathy (FAC): This type of amyloidosis affects the heart and is characterized by the accumulation of amyloid fibers in the heart muscle, leading to progressive heart failure.
3. Familial amyloidotic polyneuropathy (FAP): This type of amyloidosis affects the nerves and is characterized by the accumulation of amyloid fibers in the nerves, leading to progressive nerve damage and loss of sensation.
4. Primary amyloidosis (AL): This is a type of amyloidosis that is not inherited and is characterized by the accumulation of amyloid fibers in various organs and tissues throughout the body.

The symptoms of familial amyloidosis can vary depending on the specific type and the organs affected. Common symptoms include:

* Nerve damage and loss of sensation
* Heart failure
* Weakness and fatigue
* Pain
* Nausea and vomiting
* Diarrhea
* Constipation
* Weight loss

The diagnosis of familial amyloidosis is based on a combination of clinical findings, laboratory tests, and genetic analysis. Laboratory tests may include:

* Blood tests to measure the level of amyloid fibers in the blood
* Urine tests to measure the level of amyloid fibers in the urine
* Imaging studies such as X-rays, CT scans, or MRI scans to visualize the accumulation of amyloid fibers in the organs and tissues.

Treatment for familial amyloidosis is aimed at managing the symptoms and slowing the progression of the disease. Treatment options may include:

* Medications to manage pain, nausea, and vomiting
* Physical therapy to maintain muscle strength and mobility
* Dietary modifications to manage weight loss and malnutrition
* Heart failure medications to manage heart failure
* Kidney dialysis or transplantation to manage kidney failure
* Stem cell transplantation to slow the progression of the disease.

The prognosis for familial amyloidosis is generally poor, and the disease can be fatal within a few years after diagnosis. However, with early diagnosis and appropriate treatment, some people with familial amyloidosis may experience a better quality of life and longer survival time. It is important to note that there is currently no cure for familial amyloidosis, and research is ongoing to develop new and more effective treatments for the disease.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

The disorder is caused by an abnormal expansion of a CAG repeat in the inclusions in certain neurons in the brain, leading to a deficiency of the enzyme glucocerebrosidase. This results in the accumulation of a fatty substance called glucocerebroside in the brain, which leads to progressive damage to brain cells and loss of cognitive and motor functions.

Symptoms of GSSD typically begin in adulthood and can include difficulty with speech, language, and cognition, as well as problems with coordination, balance, and movement. As the disease progresses, patients may experience seizures, vision loss, and ultimately, dementia and death.

GSSD is a rare disorder that affects approximately one in a million people worldwide. It is usually inherited in an autosomal recessive pattern, meaning that a person must inherit two copies of the abnormal gene (one from each parent) to develop the disease. There is currently no cure for GSSD, and treatment is focused on managing symptoms and slowing the progression of the disease.

Some common examples of neurodegenerative diseases include:

1. Alzheimer's disease: A progressive loss of cognitive function, memory, and thinking skills that is the most common form of dementia.
2. Parkinson's disease: A disorder that affects movement, balance, and coordination, causing tremors, rigidity, and difficulty with walking.
3. Huntington's disease: An inherited condition that causes progressive loss of cognitive, motor, and psychiatric functions.
4. Amyotrophic lateral sclerosis (ALS): A disease that affects the nerve cells responsible for controlling voluntary muscle movement, leading to muscle weakness, paralysis, and eventually death.
5. Prion diseases: A group of rare and fatal disorders caused by misfolded proteins in the brain, leading to neurodegeneration and death.
6. Creutzfeldt-Jakob disease: A rare, degenerative, and fatal brain disorder caused by an abnormal form of a protein called a prion.
7. Frontotemporal dementia: A group of diseases that affect the front and temporal lobes of the brain, leading to changes in personality, behavior, and language.

Neurodegenerative diseases can be caused by a variety of factors, including genetics, age, lifestyle, and environmental factors. They are typically diagnosed through a combination of medical history, physical examination, laboratory tests, and imaging studies. Treatment options for neurodegenerative diseases vary depending on the specific condition and its underlying causes, but may include medications, therapy, and lifestyle changes.

Preventing or slowing the progression of neurodegenerative diseases is a major focus of current research, with various potential therapeutic strategies being explored, such as:

1. Stem cell therapies: Using stem cells to replace damaged neurons and restore brain function.
2. Gene therapies: Replacing or editing genes that are linked to neurodegenerative diseases.
3. Small molecule therapies: Developing small molecules that can slow or prevent the progression of neurodegenerative diseases.
4. Immunotherapies: Harnessing the immune system to combat neurodegenerative diseases.
5. Lifestyle interventions: Promoting healthy lifestyle choices, such as regular exercise and a balanced diet, to reduce the risk of developing neurodegenerative diseases.

In conclusion, neurodegenerative diseases are a complex and diverse group of disorders that can have a profound impact on individuals and society. While there is currently no cure for these conditions, research is providing new insights into their causes and potential treatments. By continuing to invest in research and developing innovative therapeutic strategies, we can work towards improving the lives of those affected by neurodegenerative diseases and ultimately finding a cure.

The term "acute-phase" describes the rapid onset and short duration of this reaction, which typically lasts for hours to days before resolving as the body's inflammatory response subsides. APR is characterized by a series of molecular events that result in altered expression of genes involved in inflammation, immune response, and tissue repair.

Some key components of an acute-phase reaction include:

1. Cytokine production: Cytokines are signaling molecules released by immune cells, such as white blood cells, that coordinate the immune response. During an APR, cytokine levels increase, triggering a cascade of downstream effects.
2. Leukocyte trafficking: White blood cells migrate towards sites of inflammation or infection, where they phagocytose (engulf and digest) pathogens and cellular debris. This process helps to limit the spread of infection and initiate tissue repair.
3. Coagulation cascade: The APR triggers a complex series of events involving blood coagulation factors, leading to the formation of blood clots and preventing excessive bleeding.
4. Anti-inflammatory response: As the APR progresses, anti-inflammatory cytokines, such as interleukin-10 (IL-10), are produced to dampen the inflammatory response and promote tissue repair.
5. Cellular proliferation: To replace damaged cells and tissues, the APR stimulates cellular proliferation and tissue regeneration.
6. Nutrient mobilization: The APR enhances nutrient uptake and utilization by immune cells, allowing them to mount an effective response to the stress.
7. Hormonal changes: The APR is accompanied by changes in hormone levels, such as the increase in corticotropin-releasing factor (CRF) and cortisol, which help to mobilize energy resources and regulate metabolism.
8. Immune tolerance: The APR helps to establish immune tolerance, preventing excessive or inappropriate immune responses that can lead to autoimmune diseases or allergies.
9. Tissue remodeling: The APR stimulates the remodeling of damaged tissues, allowing for the restoration of normal tissue function.
10. Memory formation: The APR sets the stage for the formation of immunological memory, which enables the immune system to mount a more effective response to future infections or stressors.

The most common form of prion disease in humans is Creutzfeldt-Jakob disease (CJD), which typically affects people over the age of 60. Other forms of prion diseases include variably protease-sensitive prionopathy (VPSPr) and fatal familial insomnia (FFI).

The symptoms of prion diseases vary depending on the specific form of the disease, but they often include:

* Cognitive decline and memory loss
* Coordination and balance problems
* Slurred speech and difficulty with communication
* Difficulty with movement and muscle control
* Depression and anxiety
* Sleep disturbances
* Loss of appetite and weight loss

Prion diseases are diagnosed through a combination of clinical evaluation, imaging studies, and laboratory tests. There is no cure for prion diseases, and treatment is focused on managing symptoms and supporting the patient's quality of life.

Prevention of prion diseases is important, as there is no effective treatment once the disease has developed. Measures to prevent the spread of prion diseases include:

* Implementing strict infection control measures in healthcare settings, such as wearing personal protective equipment and sterilizing equipment and surfaces
* Avoiding exposure to infected tissues and fluids, such as through medical procedures or consumption of contaminated beef products
* Monitoring and testing individuals who have been exposed to prion diseases, such as healthcare workers and family members of affected individuals
* Developing and distributing vaccines and other treatments to prevent and treat prion diseases.

Overall, prion diseases are a group of devastating neurodegenerative disorders that can have a significant impact on the lives of those affected. Understanding the causes, symptoms, diagnosis, treatment, and prevention of these diseases is crucial for improving outcomes and supporting individuals and families affected by prion diseases.

Gliosis is made up of glial cells, which are non-neuronal cells that provide support and protection to neurons. When neural tissue is damaged, glial cells proliferate and form a scar-like tissue to fill in the gap and repair the damage. This scar tissue can be made up of astrocytes, oligodendrocytes, or microglia, depending on the type of injury and the location of the damage.

Gliosis can have both beneficial and harmful effects on the brain. On one hand, it can help to prevent further damage by providing a physical barrier against invading substances and protecting the surrounding neural tissue. It can also promote healing by bringing in immune cells and growth factors that aid in the repair process.

On the other hand, gliosis can also have negative effects on brain function. The scar tissue can disrupt normal communication between neurons, leading to impaired cognitive and motor function. In addition, if the scar tissue is too extensive or severe, it can compress or displaces surrounding neural tissue, leading to long-term neurological deficits or even death.

There are several ways to diagnose gliosis, including magnetic resonance imaging (MRI), positron emission tomography (PET), and histopathology. Treatment options for gliosis depend on the underlying cause of the condition and can include medications, surgery, or a combination of both.

In summary, gliosis is a type of scar tissue that forms in the brain and spinal cord as a result of damage to neural tissue. It can have both beneficial and harmful effects on brain function, and diagnosis and treatment options vary depending on the underlying cause of the condition.

Wikimedia Commons has media related to Amyloid. Bacterial Inclusion Bodies Contain Amyloid-Like Structure at SciVee Amyloid ... November 2000). "Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, ... The "stacks" of beta sheet are short and traverse the breadth of the amyloid fibril; the length of the amyloid fibril is built ... Prions are an infectious form of amyloids that can act as a template to convert other non-infectious forms. Amyloids may also ...

https://en.wikipedia.org/wiki/Amyloid

"Amyloid, The ISA Journal". isaamyloidosis.org. "Journal Citation Reports". Clarivate Analytics. Retrieved 2017-12-18. "Amyloid ... Amyloid: the Journal of Protein Folding Disorders is a peer-reviewed scientific journal that publishes original research and ... Alan Cohen was the founding editor and from 1994 until 2010 the first Editor-in-Chief of Amyloid: The Journal of Protein ... The present editor in chief is Per Westermark (Uppsala University, Sweden). "Amyloid-Aims and Scope". informahealthcare.com. " ...

https://en.wikipedia.org/wiki/Amyloid_(journal)

... may be primarily vascular, as in cerebral amyloid angiopathy, or in amyloid plaques in white matter. One sensitive ... Amyloid beta (Aβ or Abeta) denotes peptides of 36-43 amino acids that are the main component of the amyloid plaques found in ... March 2020). "Prominent amyloid plaque pathology and cerebral amyloid angiopathy in APP V717I (London) carrier - phenotypic ... By NMR-guided simulations, amyloid beta 1-40 and amyloid beta 1-42 also seem to feature highly different conformational states ...

https://en.wikipedia.org/wiki/Amyloid_beta

Amyloid deposits in the gastrointestinal tract and liver may also play a role in the development of amyloid purpura. Amyloid ... Its cause is unknown, but coagulation defects caused by amyloid are thought to contribute.[citation needed] Amyloid purpura ... Amyloid purpura". N. Engl. J. Med. 356 (23): 2406. doi:10.1056/NEJMicm061510. PMID 17554122. Gamba G, Montani N, Anesi E, et al ... Amyloid purpura is a condition marked by bleeding under the skin (purpura) in some individuals with amyloidosis. ...

https://en.wikipedia.org/wiki/Amyloid_purpura

The amyloid can be seen under polarized light in congo red stained biopsy.[citation needed] Amyloid cardiomyopathy is ... Amyloid cardiomyopathy (stiff heart syndrome) is a condition resulting in the death of part of the myocardium (heart muscle). ... Outcomes for amyloid cardiomyopathy are generally very poor, with fewer than 10% of patients surviving more than 5 years. ... In developed countries, amyloid cardiomyopathy is estimated to be involved in 0.1% of deaths. "Cardiac amyloidosis: MedlinePlus ...

https://en.wikipedia.org/wiki/Amyloid_cardiomyopathy

Look up amyloid in Wiktionary, the free dictionary. An amyloid is any of certain insoluble fibrous protein aggregates. Amyloid ... may also refer to: Amyloid (mycology), a chemical reaction used in characterization of fungi Amyloid (journal), the Amyloid: ... This disambiguation page lists articles associated with the title Amyloid. If an internal link led you here, you may wish to ...

https://en.wikipedia.org/wiki/Amyloid_(disambiguation)

In mycology a tissue or feature is said to be amyloid if it has a positive amyloid reaction when subjected to a crude chemical ... The term "amyloid" is derived from the Latin amyloideus ("starch-like"). It refers to the fact that starch gives a similar ... The term amyloid comprises both variants. A hemiamyloid element of the cell wall does not directly stain blue with iodine ... Among the amyloid reaction, two types can be distinguished: Euamyloid reaction, in which the material turns blue without ...

https://en.wikipedia.org/wiki/Amyloid_(mycology)

... (also known as neuritic plaques, amyloid beta plaques or senile plaques) are extracellular deposits of the ... 2019). "Different aspects of Alzheimer's disease-related amyloid β-peptide pathology and their relationship to amyloid positron ... Amyloid beta (Aβ) is a small protein, most often 40 or 42 amino acids in length, that is released from a longer parent protein ... Amyloid plaques naturally occur in the aging brains of nonhuman species ranging from birds to great apes. In nonhuman primates ...

https://en.wikipedia.org/wiki/Amyloid_plaques

... (CAA) is a form of angiopathy in which amyloid beta peptide deposits in the walls of small to ... However, there are types involving other amyloid peptides: the "Icelandic type" is associated with Cystatin C amyloid (ACys). ... Familial amyloidosis-Finnish type is associated with gelsolin amyloid (AGel). The vascular amyloid pathology characteristic of ... the "British type" and "Danish type" are associated with British amyloid (ABri) and Danish amyloid (ADan) respectively. Both ...

https://en.wikipedia.org/wiki/Cerebral_amyloid_angiopathy

Occasionally, biopsy of skin, nerve, or muscle may be performed, which can show signs of denervation and amyloid deposition ... The tetramer has to dissociate into misfolded monomers to aggregate into a variety of structures including amyloid fibrils. ... Shin, Susan C.; Robinson-Papp, Jessica (November 2012). "Amyloid Neuropathies". The Mount Sinai Journal of Medicine, New York. ... Scott LJ (August 2014). "Tafamidis: a review of its use in familial amyloid polyneuropathy". Drugs. 74 (12): 1371-8. doi: ...

https://en.wikipedia.org/wiki/Familial_amyloid_polyneuropathy

"Amyloid". "Amyloid". Akiya S, Nishio Y, Ibi K, et al. (July 1996). "Lattice corneal dystrophy type II associated with familial ... The familial amyloid neuropathies (or familial amyloidotic neuropathies, neuropathic heredofamilial amyloidosis, familial ... "ATTR Famililial Amyloidosis". BU - Amyloid Treatment & Research Program. Archived from the original on 2008-07-06. Said, G; ... July 2006). "Impact of liver transplantation on cardiac autonomic denervation in familial amyloid polyneuropathy". Medicine ( ...

https://en.wikipedia.org/wiki/Familial_amyloid_neuropathy

"Serum amyloid A binding to CLA-1 (CD36 and LIMPII analogous-1) mediates serum amyloid A protein-induced activation of ERK1/2 ... "Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo". Scandinavian Journal of ... Serum amyloid A1 (SAA1) is a protein that in humans is encoded by the SAA1 gene. SAA1 is a major acute-phase protein mainly ... Sun L, Zhou H, Zhu Z, Yan Q, Wang L, Liang Q, Ye RD (May 2015). "Ex vivo and in vitro effect of serum amyloid a in the ...

https://en.wikipedia.org/wiki/Serum_amyloid_A1

... (FAC), or transthyretin amyloid cardiomyopathy (ATTR-CM) results from the aggregation and ... Transthyretin cardiac amyloid study (TRACS). Circ.: Heart Failure 4, 121-128. Miller, A. L., Falk, R. H., Levy, B. D. & ... Amyloid 10 Suppl 1, 48-54. Falk, R. H. & Elkayam, U. (2010). Cardiomyopathy: the importance of recognizing the uncommon ... Amyloid Transthyretin Senile systemic amyloidosis Restrictive cardiomyopathy Jacobson, D. R., Pastore, R. D., Yaghoubian, R., ...

https://en.wikipedia.org/wiki/Familial_amyloid_cardiomyopathy

... (SAA) is also an acute phase marker that responds rapidly. Similar to CRP, levels of acute-phase SAA increase ... Acute-phase serum amyloid A proteins (A-SAAs) are secreted during the acute phase of inflammation. These proteins have several ... Serum amyloid A (SAA) proteins are a family of apolipoproteins associated with high-density lipoprotein (HDL) in plasma. ... de Beer MC, Kindy MS, Lane WS, de Beer FC (February 1994). "Mouse serum amyloid A protein (SAA5) structure and expression". The ...

https://en.wikipedia.org/wiki/Serum_amyloid_A

... accumulates mainly in the heart, where it causes stiffness and often thickening of its walls, ... Wild-type transthyretin amyloid (WTTA), also known as senile systemic amyloidosis (SSA), is a disease that typically affects ... Some patients may develop carpal tunnel syndrome as an initial symptom of wild-type transthyretin amyloid. There appears to be ...

https://en.wikipedia.org/wiki/Wild-type_transthyretin_amyloid

"Amyloid Related Imaging Abnormalities (ARIA) in Amyloid Modifying Therapeutic Trials: Recommendations from the Alzheimer's ... Amyloid-related imaging abnormalities (ARIA) are abnormal differences seen in magnetic resonance imaging of the brain in ... ARIA is associated with amyloid-modifying therapies, particularly human monoclonal antibodies such as aducanumab. There are two ... "Paris: Renamed ARIA, Vasogenic Edema Common to Anti-Amyloid Therapy , ALZFORUM". www.alzforum.org. Retrieved 2016-12-11. ...

https://en.wikipedia.org/wiki/Amyloid-related_imaging_abnormalities

Mutations in critical regions of amyloid precursor protein, including the region that generates amyloid beta (Aβ), cause ... Zheng H, Koo EH (2006). "The amyloid precursor protein: beyond amyloid". Molecular Neurodegeneration. 1 (1): 5. doi:10.1186/ ... whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients. ... "Prominent amyloid plaque pathology and cerebral amyloid angiopathy in APP V717I (London) carrier - phenotypic variability in ...

https://en.wikipedia.org/wiki/Amyloid-beta_precursor_protein

The serum amyloid P component (SAP) is the identical serum form of amyloid P component (AP), a 25kDa pentameric protein first ... The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent ... Tennent GA, Lovat LB, Pepys MB (May 1995). "Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer ... "Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene". Nature Medicine. 3 (8): ...

https://en.wikipedia.org/wiki/Serum_amyloid_P_component

... produces the amyloid-beta peptide fragment that aggregates into clumps called amyloid plaques in the brains affected by ... If alpha-secretase (α-secretase) acts on APP first instead of BACE, no amyloid beta is formed because α-secretase recognizes a ... Among other roles in the cell, secretases act on the amyloid-beta precursor protein (APP) to cleave the protein into three ...

https://en.wikipedia.org/wiki/Amyloid-beta_precursor_protein_secretase

... (HCCAA) is a rare, fatal amyloid disease in young people in Iceland caused by a ... Levy, E; Jaskolski, M; Grubb, A (January 2006). "The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology ... Levy E, Lopez-Otin C, Ghiso J, Geltner D, Frangione B (May 1989). "Stroke in Icelandic patients with hereditary amyloid ... Mutations in the cystatin 3 gene are responsible for the Icelandic type of hereditary cerebral amyloid angiopathy, a condition ...

https://en.wikipedia.org/wiki/Hereditary_cystatin_C_amyloid_angiopathy

It has been found repeatedly that the mere presence of LECT2 amyloid tissue deposits does not necessarily indicate the presence ... It is important to accurately diagnose ALECT2-based amyloid disease in order to avoid treatment for other forms of amyloidosis ... They may have histological evidence of LECT2 amyloid deposition in the liver, lung, spleen, kidney, and adrenal glands of ... Kidney biopsy shows the presence of LECT2-based amyloid predominantly in the renal cortex interstitium, glomeruli, and ...

https://en.wikipedia.org/wiki/LECT2

Amyloidosis such as familial amyloid neuropathy, AL amyloidosis, and AA amyloidosis [publication pending]. During the course of ... Amyloid: The International Journal of Experimental and Clinical Investigation. 27 (3): 215-216. doi:10.1080/13506129.2020. ... Amyloid. 25 (4): 267-268. doi:10.1080/13506129.2018.1545639. PMID 30773060. S2CID 73476147. Montcuquet, A.; Duchesne, M.; ... in the assessment of patients with familial amyloid polyneuropathy". Clinical Neurophysiology. 129 (8): 1565-1569. doi:10.1016/ ...

https://en.wikipedia.org/wiki/Electrochemical_skin_conductance

December 2005). "Quantitative serum free light chain assay in the diagnostic evaluation of AL amyloidosis". Amyloid. 12 (4): ...

https://en.wikipedia.org/wiki/Bence_Jones_protein

"Amyloid". Gillmore JD, Lachmann HJ, Rowczenio D, Gilbertson JA, Zeng CH, Liu ZH, Li LS, Wechalekar A, Hawkins PN (2009). " ... 56: 253-4. Ostertag, B. (1950). "Familiaere Amyloid-erkrankung". Z. Menschl. Vererb. Konstitutionsl. 30: 105-115. v t e ( ... Amyloid. 5 (3): 188-92. doi:10.3109/13506129809003844. PMID 9818055. Soutar AK, Hawkins PN, Vigushin DM, et al. (August 1992 ...

https://en.wikipedia.org/wiki/Familial_renal_amyloidosis

"AA amyloidosis associated with a mutated serum amyloid A4 protein". Amyloid. 16 (2): 84-8. doi:10.1080/13506120902879905. PMID ... "Entrez Gene: Serum amyloid A4, constitutive". Retrieved 2020-03-14. Kumon Y, Suehiro T, Faulkes DJ, Hosakawa T, Ikeda Y, Woo P ... Serum amyloid A4, constitutive is a protein that in humans is encoded by the SAA4 gene. GRCh38: Ensembl release 89: ... August 2014). "Expression of serum amyloid A4 in human trophoblast-like choriocarcinoma cell lines and human first trimester/ ...

https://en.wikipedia.org/wiki/SAA4

"Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee". Amyloid. ... Chiti, Fabrizio; Dobson, Christopher M. (2017-06-20). "Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of ... Chiti, Fabrizio; Dobson, Christopher M. (2017-06-20). "Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of ... of the aging process with contributions that led to the discovery of a group of abnormal protein aggregates known as amyloids, ...

https://en.wikipedia.org/wiki/Edward_C._Franklin

According to the Amyloid hypothesis, the accumulation of extracellular amyloid betapeptides (Aβ) into plaques via ... However, anti-Aβ vaccines can promote antibody-mediated clearance of Aβ plaques in transgenic mice models with amyloid ... Panza, F.; Imbimbo, B. P.; Logroscino, G. (2014). "Amyloid-directed monoclonal antibodies for the treatment of Alzheimer's ... van Dyck, Christopher (August 24, 2017). "Anti-Amyloid-β Monoclonal Antibodies for Alzheimer's Disease: Pitfalls and Promise". ...

https://en.wikipedia.org/wiki/Monoclonal_antibody_therapy

December 2005). "Quantitative serum free light chain assay in the diagnostic evaluation of AL amyloidosis". Amyloid. 12 (4): ... A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis, Tours, France, 18-22 April 2004". ...

https://en.wikipedia.org/wiki/Serum_free_light-chain_measurement

Amyloid. 5(1):55-66. (Articles with short description, Short description matches Wikidata, Syndromes affecting the retina, ...

https://en.wikipedia.org/wiki/Ardalan–Shoja–Kiuru_syndrome

The combination of amyloid pathology and neurofibrillary tangles has led to comparison with the pathology of Alzheimer's ... 2001). "Chromosome 13 dementia syndromes as models of neurodegeneration". Amyloid. 8 (4): 277-84. doi:10.3109/13506120108993826 ...

https://en.wikipedia.org/wiki/Familial_British_dementia

... is a condition in which proteins called amyloid build up on the walls of the arteries in the brain. CAA causes bleeding into ... Cerebral amyloid angiopathy (CAA) is a condition in which proteins called amyloid build up on the walls of the arteries in the ... People with CAA have deposits of amyloid protein in the walls of blood vessels in the brain. The protein is usually not ... Emerging concepts in sporadic cerebral amyloid angiopathy. Brain. 2017;140(7):1829-1850. PMID: 28334869 pubmed.ncbi.nlm.nih.gov ...

https://medlineplus.gov/ency/article/000719.htm

The increasing knowledge of the exact biochemical nature of the localized and systemic amyloid disorders has made a logical and ... A primer of amyloid nomenclature Amyloid. 2007 Sep;14(3):179-83. doi: 10.1080/13506120701460923. ... All amyloid types are today preferably named by their major fibril protein. This makes a simple and rational nomenclature for ... The increasing knowledge of the exact biochemical nature of the localized and systemic amyloid disorders has made a logical and ...

https://pubmed.ncbi.nlm.nih.gov/17701465/?dopt=Abstract

... from amyloid precursor protein with eventual deposition of amyloid (Aβ) plaques is the mechanism of pathogenesis. The aim of ... The β-amyloid cascade hypothesis75 has been central to the development of treatment strategies over recent years. Essentially, ... 1.6 Radiotracers for β-amyloid. The degree of morbidity and mortality inflicted on individuals and society by Alzheimers ... that such radiotracers will eventually have more utility for investigating pathophysiology and the validity of the β-amyloid ...

https://www.nimh.nih.gov/research/research-conducted-at-nimh/research-areas/clinics-and-labs/mib/sprs/research/16-radiotracers-for-b-amyloid

The search for a potential anti-amyloid drug has led to the discovery of hundreds of compounds, none of which have passed all ... as well as directly inhibit amyloid formation. However, the conditions under which this effect is seen could lead to oxidation ... Food protein-derived amyloids do not accelerate amyloid β aggregation. 31 January 2023 ... Foderà, V. et al. Thioflavin T hydroxylation at basic pH and its effect on amyloid fibril detection. J. Phys. Chem. B 112, ...

https://www.nature.com/articles/s41598-020-70982-3?error=cookies_not_supported

... conducted by New York University researchers suggests that partially inhibiting an enzyme that initiates the release of amyloid ... Amyloid Plays an Important Role in Memory. Scientists at NYU Langone Medical Center have discovered that the beta amyloid ... Partial Amyloid Beta Inhibition Improves Memory in Alzheimers Personalised Printable Document (PDF). Please complete this form ... Amyloidosis is a rare disease due to build up of abnormal proteins called amyloid in different tissues and ... ...

https://www.medindia.net/news/partial-amyloid-beta-inhibition-improves-memory-in-alzheimers-39870-1.htm

Amyloid deposition is rare in B6C3F1 mice but more common in the liver (and also the gallbladder) of CD-1 mice. It is usually ...

https://www.niehs.nih.gov/research/resources/visual-guides/liverpath/degenerative/amyloid/index.cfm

Amyloid Hypothesis For Alzheimers In Doubt After Lillys Drug Failure : Shots - Health News The failure of an experimental ... "The low magnitude of effects would lend support to the idea that it might be time to move on from amyloid," says Weill Cornell ... "Ive never been a firm believer in the amyloid hypothesis being the be-all and end-all as to the cause of Alzheimers," says ... Diseased brain tissue from an Alzheimers patient showing amyloid plaques (in blue) located in the gray matter of the brain. Dr ...

https://www.npr.org/sections/health-shots/2016/12/29/506592761/where-does-alzheimer-s-treatment-go-from-here?ft=nprml&f=506592761

Study of AV-1959, an Amyloid Beta Vaccine. The safety and scientific validity of this study is the responsibility of the study ... A Phase I, Randomized, Double-Blind Study to Evaluate Safety and Tolerability of Amyloid-β Vaccine, AV-1959D, in Patients With ... Prior administration of any amyloid-beta or tau immunotherapy (vaccine, antibody). *Magnetic resonance imaging (MRI) showing ... Phase 1 clinical trial of AV-1959 amyloid-β vaccine for Alzheimers disease (AD). ...

https://clinicaltrials.gov/ct2/show/NCT05642429?draw=2&rank=1

17-40 Beta-Amyloid peptides. Pyroglutamate-modified (Pyr) beta-Amyloid 3-40 and 11-40 have been described as major compounds in ... Beta-Amyloid 1-42 forms a major component of amyloid plaques in neurons of Alzheimers disease (AD) brains, while beta-Amyloid ... Beta-Amyloid x-42. A large collection of Beta-Amyloid X-42 fragments from 2 to 23-42 ... Beta-Amyloid x-40 x from 1 to 9. *Beta-Amyloid (2-40) ... Beta-Amyloid x-40. x from 10 to 19. *Beta-Amyloid (11-40) ...

https://www.anaspec.com/en/beta-amyloid-x-40-peptides

Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o). Nature. 1993 Mar 4;362(6415):75-9. PubMed. ...

https://www.alzforum.org/papers/alzheimer-amyloid-protein-precursor-complexes-brain-gtp-binding-protein-go

Knockout Tested Rabbit recombinant monoclonal Amyloid Precursor Protein antibody [EPR5118-34]. Validated in WB, IHC, Flow Cyt ( ... beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid 42. ... Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and ... amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal ...

https://www.abcam.com/products/primary-antibodies/amyloid-precursor-protein-antibody-epr5118-34-ab126732.html

Amyloid is defined as in vivo deposited material distinguished by the following: Fibrillar appearance on electron micrography ... Amyloid. Amyloid is defined as in vivo deposited material distinguished by the following:. * Fibrillar appearance on electron ... Mechanisms of Amyloid Formation. Amyloid protein structures. In all forms of amyloidosis, the cell secretes the precursor ... Nonfibrillar Components of Amyloid. All types of amyloid deposits contain not only the major fibrillar component (solubility in ...

http://emedicine.medscape.com/article/335414-overview

All volunteers will undergo a positron emission tomography (PET) scan to be determine their brain amyloid levels. ... HomeAnti-Amyloid Treatment in Asymptomatic Alzheimers Disease (A4). ... PET scan that shows evidence of amyloid in the brain at screening ... Anti-Amyloid Treatment in Asymptomatic Alzheimers Disease (A4 ... can slow the progression of memory problems associated with amyloid, a protein that forms plaques in the brains of people with ...

https://www.nia.nih.gov/alzheimers/clinical-trials/anti-amyloid-treatment-asymptomatic-alzheimers-disease-a4

A new study finds that amyloids may also have a normal biological function. ... Amyloids are best known for their role in diseases such as Alzheimers. ... Amyloids are best known for their role in diseases such as Alzheimers. A new study finds that amyloids may also have a normal ... These dense plaques are made of proteins that are normally found in the body but have misfolded to form amyloids. Amyloid can ...

https://www.nih.gov/news-events/nih-research-matters/broader-role-amyloids

... amyloid-β) and tau are both proteins synonymous with Alzheimers Disease. A clinical picture of an Alzheimers patient usually ... Table of comparison between amyloid and tau. Summary. When processes involving amyloids (beta amyloid or APP) go rogue, brain ... How does amyloid affect tau?. Studies show that when beta amyloids start forming plaques, once formed from the amyloid ... Does tau cause amyloid?. No. Just like amyloid, tau is a normal protein that occurs throughout the body. It is found in most ...

http://www.differencebetween.net/science/health/difference-between-amyloid-and-tau/

Click below to subscribe to AMPlify Advocacy, a monthly newsletter containing outreach news, updates and Ideas.. ...

https://www.amprogress.org/research-news/2019/03/on-the-frontier-of-an-alzheimers-cure/tsai-martorell-amyloid-cortex-3-22-19/

Learn Transthyretin Amyloid Cardiomyopathy - ATTR-CM causes, diagnosis and treatment from National Heart Centre Singapore (NHCS ... Transthyretin amyloid cardiomyopathy (ATTR-CM) is a type of cardiomyopathy which is underdiagnosed and potentially fatal. ... Home , Patient Care , Conditions and Treatment , Transthyretin Amyloid Cardiomyopathy (ATTR-CM) Transthyretin Amyloid ... Transthyretin Amyloid Cardiomyopathy (ATTR-CM) - What it is Transthyretin amyloid cardiomyopathy, also known as ATTR-CM, is a ...

https://www.singhealth.com.sg/patient-care/conditions-treatments/transthyretin-amyloid-cardiomyopathy

Heterotypic Amyloid Interactions and their Impact on Amyloid Assembly. Add to your list(s) Download to your calendar using vCal ... University of Cambridge , Talks.cam , Babraham Seminar , Heterotypic Amyloid Interactions and their Impact on Amyloid Assembly ... Heterotypic amyloid interactions between related protein sequences have been observed in functional and disease amyloids. While ... We find that these heterotypic amyloid interactions can result in the subcellular mislocalisation of these proteins. Moreover, ...

https://talks.cam.ac.uk/talk/index/193711

Investigations of the Effects of Amyloid-Beta Proteins on hSlo1.1, a BK Channel, in a Xenopus Oocyte Model ... The disease was classically characterized by widespread deposition of insoluble amyloid-beta (Aβ) plaques throughout the cortex ...

https://www.moleculardevices.com/en/assets/tutorials-videos/reagents/investigations-effects-amyloid-beta-proteins-hslo11-bk-channel-xenopus-oocyte

This IHC staining protocol is for the detection of amyloid beta aggregates and plaques in formalin-fixed parafin-embedded (FFPE ... Protocol can be used for Beta Amyloid products that list "IHC" as an application on the datasheet (e.g. clones 4G8, 6E10, etc). ...

https://www.biolegend.com/de-at/protocols/immunohistochemistry-protocol-for-beta-amyloid-products-using-usa-detection-kit

It clinched the case that these antibodies can mop up brain amyloid, bringing many people with early symptomatic Alzheimers ... After years of fits and starts, anti-amyloid immunotherapies are finally hitting their target effectively. At least four drugs ... "Several of the antibodies are looking good at removing amyloid, but the clinical efficacy still needs to be demonstrated." ... Four Immunotherapies Now Proven to Reduce Amyloid-β in the Aging Brain. Permalink Read 6 Comments Add a Comment Posted by ...

https://www.fightaging.org/archives/2018/08/four-immunotherapies-now-proven-to-reduce-amyloid-%CE%B2-in-the-aging-brain/

APOE modulates microglial immunometabolism in response to age, amyloid pathology, and inflammatory challenge. View ORCID ... APOE modulates microglial immunometabolism in response to age, amyloid pathology, and inflammatory challenge ... APOE modulates microglial immunometabolism in response to age, amyloid pathology, and inflammatory challenge ... APOE modulates microglial immunometabolism in response to age, amyloid pathology, and inflammatory challenge ...

https://www.biorxiv.org/content/10.1101/2022.05.17.492361v1

https://www.brightfocus.org/grant/mechanisms-amyloidogenesis-beta-amyloid-peptide

Tag: amyloid beta elisa. INPP5K and Atlastin-1 maintain the nonuniform distribution of ER-plasma membrane contacts in neurons. ...

https://www.aabioetica.org/tag/amyloid-beta-elisa/

... Presented at: Thermo Fisher Scientific - Electron Microscopy Webinars ... Review amyloid filaments and neurodegenerative diseases. *Define what are taupathies and how are they related to ... providing a new database for the greater amyloid field. Understanding their molecular mechanism holds important implications ...

https://www.labroots.com/webinar/tale-amyloid-filaments-neurodegenerative-diseases

Associations of Dietary Protein and Fiber Intake with Brain and Blood Amyloid-β. ...

https://www.j-alz.com/content/associations-dietary-protein-and-fiber-intake-brain-and-blood-amyloid-%CE%B2

P-Glycoprotein Efflux and Other Factors Limit Brain Amyloid β Reduction by β-Site Amyloid Precursor Protein-Cleaving Enzyme 1 ... P-Glycoprotein Efflux and Other Factors Limit Brain Amyloid β Reduction by β-Site Amyloid Precursor Protein-Cleaving Enzyme 1 ... P-Glycoprotein Efflux and Other Factors Limit Brain Amyloid β Reduction by β-Site Amyloid Precursor Protein-Cleaving Enzyme 1 ... P-Glycoprotein Efflux and Other Factors Limit Brain Amyloid β Reduction by β-Site Amyloid Precursor Protein-Cleaving Enzyme 1 ...

https://jpet.aspetjournals.org/content/326/2/502

Serum amyloid A proteins bind retinol with nanomolar affinity, and do so by forming oligomers that create a hydrophobic pocket ... 2004) Hypothetical structure of human serum amyloid A protein Amyloid 11:71-80. ... 1986) Amyloid A gene family expression in different mouse tissues The Journal of Experimental Medicine 164:2006-2017. ... 2005) Serum amyloid A promotes cholesterol efflux mediated by scavenger receptor B-I The Journal of Biological Chemistry 280: ...

https://elifesciences.org/articles/03206

People with CAA have deposits of amyloid protein in the walls of blood vessels in the brain. (medlineplus.gov)
All amyloid types are today preferably named by their major fibril protein. (nih.gov)
Essentially, under this hypothesis over-production of the peptides Aβ 40 and, especially Aβ 42 , from amyloid precursor protein with eventual deposition of amyloid (Aβ) plaques is the mechanism of pathogenesis. (nih.gov)
But the frustration brought by this particular failure could signal a shift in Alzheimer's research - a shift away from targeting accumulations of so-called amyloid protein in the brain, long considered by many in the field to be the crux of Alzheimer's pathology. (npr.org)
Ever since Dr. George G. Glenner's 1984 discovery that amyloid is the main component of the plaques that riddle the Alzheimer's-afflicted brain, it has been assumed that the protein somehow contributes to the disorder - that it jams up cellular machinery, rendering neurons unable to effectively communicate, to form new memories, to remember where the keys are. (npr.org)
A different type of investigational medication, so-called BACE inhibitors, prevent amyloid formation in the first place, by neutralizing an enzyme that cuts away amyloid from a larger protein. (npr.org)
Sequential proteolytic cleavage of the Amyloid Precursor Protein (APP) by secretases (α, β, γ) generates beta-Amyloid peptide fragments. (anaspec.com)
Nishimoto I, Okamoto T, Matsuura Y, Takahashi S, Murayama Y, Ogata E . Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o) . (alzforum.org)
Amyloid fibrils are protein polymers comprising identical monomer units (homopolymers). (medscape.com)
All types of amyloid consist of one major fibrillar protein that defines the type of amyloid. (medscape.com)
Polymorphisms that slightly vary native peptides or inflammatory processes set the stage for abnormal protein folding and amyloid fibril deposition. (medscape.com)
The amyloidoses are referred to with a capital A (for amyloid) followed by an abbreviation for the fibril protein. (medscape.com)
Synthetic peptide within Human Amyloid Precursor Protein aa 50-150 (extracellular). (abcam.com)
This study will test whether an investigational drug, solanezumab, can slow the progression of memory problems associated with amyloid, a protein that forms plaques in the brains of people with Alzheimer disease. (nih.gov)
They are made of highly organized protein arrangements called β-sheets that stack perpendicularly along the axis of the amyloid fiber. (nih.gov)
With funding from NIH's National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), the researchers explored whether protein hormones could form amyloids. (nih.gov)
Abstract: Heterotypic amyloid interactions between related protein sequences have been observed in functional and disease amyloids. (cam.ac.uk)
Associations of Dietary Protein and Fiber Intake with Brain and Blood Amyloid-β. (j-alz.com)
Based on this hypothesis, β-site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) inhibitors are an attractive therapeutic approach for AD because cleavage of the APP by BACE1 is required to form Aβ. (aspetjournals.org)
The trafficking and metabolism of amyloid precursor protein (APP). (nih.gov)
What can PAT1 do for amyloid precursor protein? (nih.gov)
Thus, structurally distinct amyloids composed of the same protein were differentially sensitive to the anti-amyloid activity of DnaJB6 both in vitro and in vivo. (nih.gov)
In a stroke of luck, one of Yankner's insertions encoded a precursor to a protein called amyloid. (nih.gov)
These patients were identified by the presence of amyloid or tau protein in PET measurements. (medscape.com)
The Laboratory of Protein Conformation and Dynamics integrates complementary biophysical and biochemical techniques to understand the molecular mechanisms of amyloid formation. (nih.gov)
Dr. Lee focuses her research efforts on studying changes in protein conformation and dynamics important for the mechanisms by which amyloid structures assemble under normal and pathological conditions. (nih.gov)
To determine the critical features guiding amyloid formation, Dr. Lee is characterizing how individual amino acid residues affect protein-protein interaction during the amyloid assembly process. (nih.gov)

Diseased brain tissue from an Alzheimer's patient showing amyloid plaques (in blue) located in the gray matter of the brain. (npr.org)
Biogen's aducanumab, another experimental drug that's far along in clinical testing , binds to and clears amyloid that is already ensnared in plaques. (npr.org)
Earlier this year the FDA granted aducanumab fast-track status after results from a small, early-stage study suggested that it reduces amyloid plaques and slows cognitive decline in people with very early stage disease. (npr.org)
Beta-Amyloid 1-42 forms a major component of amyloid plaques in neurons of Alzheimer's disease (AD) brains, while beta-Amyloid 1-40 is taken as a negative control of beta-Amyloid 1-42 in most studies. (anaspec.com)
Pyroglutamate-modified (Pyr) beta-Amyloid 3-40 and 11-40 have been described as major compounds in the senile AD plaques. (anaspec.com)
These dense plaques are made of proteins that are normally found in the body but have misfolded to form amyloids. (nih.gov)
Beta amyloids chunks become stuck to one another and end up as hardened deposited plaques in the brain cell connections. (differencebetween.net)
The disease was classically characterized by widespread deposition of insoluble amyloid-beta (Aβ) plaques throughout the cortex, leading to synaptic dysfunction and neuronal loss. (moleculardevices.com)
In Aubrey de Grey's August bi monthly review of Theses relevant to combating aging he highlighted a paper suggesting that perhaps amyloid beta plaques don't actually cause damage in Alzheimers, it is the fact that they rupture cellular endosomes that results in cell death. (fightaging.org)
The identification of amyloid-rich plaques has long been a diagnostic tool for pathologists investigating Alzheimer's disease (AD). (nih.gov)
The APOE -Aß interaction regulates Aß aggregation and clearance and therefore directly influences the development of amyloid plaques , congophilic amyloid angiopathy and subsequent tau related pathology . (bvsalud.org)
Injection of NEP-expressing lentivirus, but not inactive NEP-expressing lentivirus, GFP-expressing lentivirus, or vehicle, into the hippocampus of 12-20-mo-old hAPP transgenic mice led to an approx 50% reduction in the number of amyloid plaques. (nih.gov)

Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)
NIEHS scientists discovered that beta-amyloid peptide, found in patients with Alzheimer's disease, can disrupt brain signals that may contribute to the memory loss associated with Alzheimer's disease. (nih.gov)
2001. Beta-amyloid(1-42) peptide directly modulates nicotinic receptors in the rat hippocampal slice. (nih.gov)

Cerebral amyloid angiopathy (CAA) is a condition in which proteins called amyloid build up on the walls of the arteries in the brain. (medlineplus.gov)
Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
[ 5 ] Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)
[ 6 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)
Amyloids are actually defined by their structure, not the specific proteins that form them. (nih.gov)
Beta amyloid (amyloid-β) and tau are both proteins synonymous with Alzheimer's Disease. (differencebetween.net)
Amyloid proteins are commonly known in the medical world for their contribution to Alzheimer's disease . (differencebetween.net)
Beta amyloids are parented by amyloid precursor proteins, commonly known as APP. (differencebetween.net)
A number of professionals say that the beta amyloid proteins allow brain cells to send signals. (differencebetween.net)
These enzymes cut APP up into chunks of proteins, beta amyloids, which is not able to be metabolized by the brain. (differencebetween.net)
Both proteins (amyloid and tau) become stuck in clumps when their processes are disrupted. (differencebetween.net)
We find that these heterotypic amyloid interactions can result in the subcellular mislocalisation of these proteins. (cam.ac.uk)
Our findings suggest a structural mechanism by which the proteomic background can modulate the aggregation propensity of amyloidogenic proteins and we discuss how such sequence specific proteostatic perturbations could contribute to the selective cellular susceptibility of amyloid disease progression. (cam.ac.uk)
Serum amyloid A (SAA) proteins are strongly induced in the liver by systemic infection and in the intestine by bacterial colonization, but their exact functions remain unclear. (elifesciences.org)
It had been suggested that Serum Amyloid A (SAA) proteins, a family of proteins made by some liver and intestinal cells, could be involved in the response to infection, because these proteins' levels increase during infection. (elifesciences.org)
Although the roles of APP, the presenilins, and other molecules implicated in AD still require significant investigation, the characterization of genes and proteins that are linked to amyloid plaque formation may help build a picture of the events that lead to AD. (nih.gov)
The person in the position will perform experiments with human brain samples and transgenic mice and amyloid fibrils and oligomers formed from synthetic and recombinant purified proteins under the direction of Dr. Charles Glabe. (uci.edu)
Experience working with amyloids and insoluble proteins and proteomic analysis are preferred. (uci.edu)
Yeast prions [URE3] and [PSI] propagate as amyloid forms of Ure2 and Sup35 proteins, respectively. (nih.gov)
Aggregation of proteins into amyloid structures is a hallmark of human diseases such as Alzheimer's, Parkinson's, and Hungtington's. (nih.gov)
To begin to understand these differences, Dr. Lee is currently investigating the mechanisms of amyloid formation for two human proteins: α-synuclein, which is localized to nerve terminals and associated with Parkinson's disease, and Pmel17, which serves as structural scaffolding for melanin deposition in skin and eyes. (nih.gov)

Phase 1 clinical trial of AV-1959 amyloid-β vaccine for Alzheimer's disease (AD). (clinicaltrials.gov)
A Phase I, Randomized, Double-Blind Study to Evaluate Safety and Tolerability of Amyloid-β Vaccine, AV-1959D, in Patients With Early Alzheimer's Disease. (clinicaltrials.gov)
Immunotherapies that target aggregation of amyloid-β in order to treat Alzheimer's disease have a long and expensive history of failure. (fightaging.org)
The present consensus on Alzheimer's disease is that amyloid-β accumulation is an early phase, damaging yes, but nowhere near as damaging as the tau aggregation that occurs later on. (fightaging.org)
It clinched the case that these antibodies can mop up brain amyloid, bringing many people with early symptomatic Alzheimer's disease (AD) below the threshold for amyloid positivity. (fightaging.org)
Those experiments and later ones from Yankner's own lab showed definitively that high concentrations of amyloid, as found in the brains of people with Alzheimer's disease, are toxic to neural cells [1]. (nih.gov)
In summary, this means that at present we have two monoclonal antibodies against beta-amyloid that showed efficacy in the early stages of Alzheimer's disease. (medscape.com)

In these experiments, one of the methods used to track the existence or formation of amyloids is an amyloidophilic dye molecule-thioflavin-T (ThT), which fluorescence emission intensity increases significantly when it binds to the beta-sheet grooves on the surface of amyloid fibrils 23 . (nature.com)
Amyloidosis is a clinical disorder caused by extracellular and/or intracellular deposition of insoluble abnormal amyloid fibrils that alter the normal function of tissues. (medscape.com)
The modern era of amyloidosis classification began in the late 1960s with the development of methods to solubilize amyloid fibrils. (medscape.com)
Along with tafamidis, the first approved therapy for ATTR-cardiomyopathy (CM), several other agents are in late-stage clinical development for ATTR-CM. TTR-stabilizing and -silencing agents with various mechanisms target TTR, preventing disaggregation of tetrameric TTR, and subsequent misfolding of TTR and formation of amyloid fibrils in the myocardium. (nih.gov)
This NIH-funded project aims at developing methods for the purification and preparation of homogeneous amyloid oligomers and fibrils of different structural polymorphs and tools for studying amyloid polymorphism in vitro and in vivo. (uci.edu)
Interestingly, amyloid fibrils can also serve essential biological roles in organisms ranging from bacteria to humans. (nih.gov)

Pyro-Glu modified beta-Amyloid forms are more resistant to degradation, show higher toxicity and have increased aggregation propensity compared to the non-modified beta-Amyloid equivalent. (anaspec.com)
The researcher also will work on the seeded aggregation and replication of these amyloids isolated from human brain. (uci.edu)
Ultimately, Dr. Lee wants to understand the mechanisms of amyloid aggregation and function at a detailed level in the context of the multiple cellular compartments with which they interact. (nih.gov)

The prion domain readily forms amyloid in vitro and, when mixed with the native full-length Ure2p, also induces the latter to form amyloid. (nih.gov)
Moreover, many polypeptides with widely varying amino acid sequences and folded states can form amyloid in vitro, implying common formation pathways. (nih.gov)

As the beta-amyloid is central to AD pathology, beta-amyloid is being pursued as a therapeutic target, including through passive immunotherapy against beta-amyloid. (nih.gov)
She would like to not only describe the self-assembly process and its critical features, but also determine points of intervention in which amyloid assembly is linked to pathology. (nih.gov)
β-Amyloid (Aβ) pathology is common in patients with probable dementia with Lewy bodies (DLB). (nih.gov)
Confirm the presence of amyloid beta pathology prior to initiating treatment. (nih.gov)

Emerging concepts in sporadic cerebral amyloid angiopathy. (medlineplus.gov)
Greenberg SM, Charidimou A. Diagnosis of cerebral amyloid angiopathy: evolution of the Boston criteria. (medlineplus.gov)
Although cortical superficial siderosis has many possible causes, it is emerging as a key feature of cerebral amyloid angiopathy, a common and important age-related cerebral small vessel disorder leading to intracerebral haemorrhage and dementia. (eur.nl)
In this review we focus on recent developments in neuroimaging and detection, aetiology, prevalence, pathophysiology and clinical significance of cortical superficial siderosis, with a particular emphasis on cerebral amyloid angiopathy. (eur.nl)

Amyloid deposits in the glomeruli of the kidney are usually the cause of death in animals that die with amyloidosis. (nih.gov)
Recent efforts in basic science have elucidated the pathobiology of amyloid transthyretin (ATTR) amyloidosis, leading to the development of the first generation of transthyretin (TTR)-targeted therapies for this disease. (nih.gov)
Anti-amyloid treatments represent another strategy for treating patients with advanced ATTR amyloidosis. (nih.gov)

The hypothesis to be examined is that different types of amyloid accumulate in different phenotypic variants of disease. (uci.edu)

In the esophagus and small intestine, the disease appears to begin as a deposition of amyloid in the submucosa. (nih.gov)

76 Radiotracers are sought for imaging Aβ preceding clinical signs of dementia, although we have argued that such radiotracers will eventually have more utility for investigating pathophysiology and the validity of the β-amyloid cascade hypothesis. (nih.gov)
Further, Alzheimer's patients also tend to have other forms of neurodegeneration , such as vascular dementia , that are unlikely to be greatly affected by amyloid-β clearance. (fightaging.org)
Anti-Beta-Amyloid Passive Immunotherapy for Alzheimer’s Dementia and Amyloid Related Imaging Abnormalities (ARIA): What’s Next? (nih.gov)

Like many other failed medications for symptomatic Alzheimer's, solanezumab works by attacking amyloid in the brain. (npr.org)
By the time symptoms of Alzheimer's arise, the brain is already speckled with amyloid. (npr.org)
All volunteers will undergo a positron emission tomography (PET) scan to be determine their brain amyloid levels. (nih.gov)
Amyloid can also cause problems beyond the brain. (nih.gov)
The amyloids produced inside the brain are processed by the alpha secretase enzyme. (differencebetween.net)
When processes involving amyloids (beta amyloid or APP) go rogue, brain cell connections and guidance are negatively impacted. (differencebetween.net)
These studies showed that all three BACE1 inhibitors decreased brain Aβ1-40 in P-gp KO mice, demonstrating that P-gp is a major limitation for development of BACE1 inhibitors to test the amyloid hypothesis. (aspetjournals.org)
This funding opportunity announcement (FOA) solicits applications designed to increase understanding of cellular and molecular mechanisms that can be targeted to protect the blood-brain barrier (BBB), and thus brain blood vessels, during therapeutic interventions that target beta-amyloid. (nih.gov)
This includes applications that promote the discovery of cellular and molecular mechanisms that underlie brain blood vessels responses to passive anti-beta-amyloid immunotherapy that result in amyloid-related imaging abnormalities (ARIA) and other potentially adverse cerebrovascular responses. (nih.gov)
Because of the translational potential of passive anti-beta-amyloid immunotherapy on the ADRD disease processes, understanding the effect of this therapy on the blood-brain barrier and brain blood vessels in the intact living brain is critically important. (nih.gov)
Imaging brain amyloid : progress and promise / Chester A. Mathis. (nih.gov)

Those people did have amyloid deposits visible with positron emission tomography imaging. (npr.org)
These trials also suggest that the best chance for a significant effect on cognition is likely to be treating asymptomatic people with amyloid deposits on imaging. (npr.org)
Whenever present, amyloid deposits should be diagnosed as "amyloid" and graded based on the extent of the amyloid deposits. (nih.gov)
Various descriptive classification systems were proposed based on the organ distribution of amyloid deposits and clinical findings. (medscape.com)

APOE-amyloid interaction: Therapeutic targets. (bvsalud.org)
The interaction between APOE and amyloid ß (Aß) plays a key role in AD pathogenesis . (bvsalud.org)

Solanezumab, an antibody, works by attacking amyloid floating in cerebrospinal fluid. (npr.org)
We had a positive trial with an antibody against beta-amyloid at the beginning of this year, called lecanemab, which is now approved in the United States. (medscape.com)

Such a nomenclature, biochemically based, has been used for several years but the current literature is still mixed up with many clinical and histochemically based designations from the time when amyloid in general was poorly understood. (nih.gov)
The search for a potential anti-amyloid drug has led to the discovery of hundreds of compounds, none of which have passed all clinical trials. (nature.com)
Yet, Burke adds, if these trials don't show a significant clinical benefit, the focus on amyloid will likely end. (npr.org)
Several of the antibodies are looking good at removing amyloid, but the clinical efficacy still needs to be demonstrated. (fightaging.org)
Amyloid Related Imaging Abnormalities (ARIA): Enhanced clinical vigilance for ARIA is recommended during the first 14 weeks of treatment with LEQEMBI. (nih.gov)

The β-amyloid cascade hypothesis 75 has been central to the development of treatment strategies over recent years. (nih.gov)

Transthyretin amyloid cardiomyopathy, also known as ATTR-CM, is a type of cardiomyopathy which is underdiagnosed and potentially fatal. (singhealth.com.sg)

A central question under investigation is: what are the distinguishing features between functional and pathological amyloids? (nih.gov)
For example, do functional amyloids aggregate such that specific pathogenic conformations are avoided? (nih.gov)

Monoclonal antibodies directed against aggregated forms of beta amyloid, including LEQEMBI, can cause amyloid related imaging abnormalities (ARIA), characterized as ARIA with edema (ARIA-E) and ARIA with hemosiderin deposition (ARIA-H). ARIA is usually asymptomatic, although rarely serious and life-threatening events can occur. (nih.gov)
Monoclonal antibodies directed against aggregated forms of beta amyloid, including LEQEMBI, can cause amyloid related imaging abnormalities (ARIA), characterized as ARIA with edema (ARIA-E) and ARIA with hemosiderin deposition (ARIA-H). Incidence and timing of ARIA vary among treatments. (nih.gov)

PSI] prions can propagate as weak or strong variants, which differ only in the structural conformation of their amyloid cores. (nih.gov)

Amyloid deposition around blood vessels in the portal areas. (nih.gov)

We found that the amyloid of Ure2p consists of a beta-sheet core region (Ure2 residues 1-65) (Fig. 2), a C-terminal domain similar in structure to glutathione-S-transferases (Ure2 residues 95-354), and a flexible tether connecting these two regions (Ure2 residues 66-94). (nih.gov)
In Ure2 amyloid, monomers are connected by interactions between the N-terminal domains. (nih.gov)

Amyloid appears as an amorphous, eosinophilic, hyaline, extracellular substance (Figure 1, arrow) that, with progressive accumulation, results in pressure atrophy of adjacent cel s and tissue. (nih.gov)
But still: researchers claimed that two years of treatment with high-dose gantenerumab essentially resets a person's trajectory of amyloid accumulation. (fightaging.org)

The increasing knowledge of the exact biochemical nature of the localized and systemic amyloid disorders has made a logical and easily understood nomenclature absolutely necessary. (nih.gov)
Dr. Lee's laboratory integrates a variety of biophysical and biochemical techniques to understand the molecular mechanisms of amyloid formation. (nih.gov)

E4 microglia display increased Hif1α expression, a disrupted TCA cycle, and are inherently pro-glycolytic, while spatial transcriptomics and MALDI mass spectrometry imaging highlight an E4-specific response to amyloid that is characterized by widespread alterations in lipid metabolism. (biorxiv.org)

Interestingly enough, amyloids are not harmful until things go wrong. (differencebetween.net)

Amorphous eosinophilic interstitial amyloid observed on a renal biopsy. (medscape.com)

There is a cellular, eosinophilic material (amyloid) in the submucosa of the esophagus (arrow). (nih.gov)

Serum Amyloid A: Where next for this biomarker? (avacta.com)

Therefore, this FOA invites basic disease-related molecular mechanisms applications that use age-appropriate beta-amyloid animal models to understand genetic, cellular, and molecular factors that result in adverse responses at and/or proximal to the BBB due to passive anti-beta-amyloid immunotherapy. (nih.gov)

New York University researchers, after a successful animal study, suggest that partially inhibiting an enzyme that initiates the release of amyloid beta may help improve memory dysfunction. (medindia.net)

This study led to the high-resolution structure determination 76 structures of recombinant tau filaments assembled in vitro, providing a new database for the greater amyloid field. (labroots.com)
We showed that amyloid of recombinant Ure2p is infectious for yeast cells, infecting them with the [URE3] prion. (nih.gov)
Cells infected with amyloid of recombinant Ure2p carry any of a large number of heritable prion variants. (nih.gov)

Gallic acid has been shown to both modulate factors leading to the onset of neurodegenerative disorders, as well as directly inhibit amyloid formation. (nature.com)

N-terminally truncated beta-Amyloid 3-40 ad 11-40 , both having a Glu as first residue, are subjected to pyro-glutamination. (anaspec.com)
[ 2 ] Many classic eponymic diseases were later found to be related to a diverse array of misfolded polypeptides (amyloid) that contain the common beta-pleated sheet architecture. (medscape.com)
Other professionals are of the opinion that the beta amyloids are important in early development stages and guide cells on how to attach to each other. (differencebetween.net)
Tau is better understood by scientists in comparison to the nature of beta amyloids and disease. (differencebetween.net)
Protocol can be used for Beta Amyloid products that list "IHC" as an application on the datasheet ( e.g . clones 4G8, 6E10, etc). (biolegend.com)
Mutations in the presenilins increase the production of beta-amyloid, suggesting that they influence the metabolism of APP in some way. (nih.gov)
Human chaperone DnaJB6, an Hsp70 co-chaperone whose defects cause myopathies, protects cells from polyglutamine toxicity and prevents purified polyglutamine and A-beta peptides from forming amyloid. (nih.gov)

In line with its anti-prion effects, DnaJB6 prevented purified Sup35 from forming amyloids at 37 °C, which produce predominantly weak [PSI] variants when used to infect yeast, but not at 4 °C, which produces mostly strong [PSI] variants. (nih.gov)

The challenge for amyloid-β clearance therapies is now to show benefits in patients, and there are good reasons to believe that this will be challenging in the late disease state. (fightaging.org)

Special stains such as Congo red can be used to confirm that the material is amyloid. (nih.gov)
Congo red stains amyloid orange to orange red and under polarized light imparts a characteristic light green birefringence that is often referred to as apple green. (nih.gov)
Congo red staining of a cardiac biopsy specimen containing amyloid, viewed under polarized light. (medscape.com)

This makes a simple and rational nomenclature for the increasing number of amyloid disorders known in humans and animals. (nih.gov)
These findings have important implications for strategies using DnaJB6 as a target for therapy in amyloid disorders. (nih.gov)

It may not be amyloids themselves that cause disease, but rather conditions that lead too much amyloid to form in the wrong places. (nih.gov)

Or is the formation and degradation of amyloids regulated more efficiently in healthy cells? (nih.gov)

The tide finally seems to be turning, however, with the advent of several treatments that can reduce amyloid-β levels without resulting in an unacceptable level of risk for the patients. (fightaging.org)

Since amyloids are thought to be toxic to neuronal cells, the researchers tested whether the ones they'd created were toxic to a neuronal cell line in the laboratory. (nih.gov)

Amyloid β (Aβ) peptides are hypothesized to cause the initiation and progression of AD based on pathologic data from AD patients, genetic analysis of mutations that cause early onset forms of AD, and preclinical studies. (aspetjournals.org)

These experiments provide evidence that secretory granules contain amyloids, and that amyloids help the body store and release hormones. (nih.gov)

Seizures, also called amyloid spells, may be treated with anti-seizure drugs. (medlineplus.gov)

Anatomy11

Organisms2

Diseases14

Chemicals and Drugs36

Analytical, Diagnostic and Therapeutic Techniques and Equipment12

Psychiatry and Psychology2

Phenomena and Processes17

Disciplines and Occupations1

Information Science2

Islet amyloid polypeptide/amylin messenger RNA and protein expression in human insulinomas in relation to amyloid formation. (1/3010)

Prion domain initiation of amyloid formation in vitro from native Ure2p. (2/3010)

Interaction of amylin with calcitonin gene-related peptide receptors in the microvasculature of the hamster cheek pouch in vivo. (3/3010)

The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. (4/3010)

Specific gene expression in pancreatic beta-cells: cloning and characterization of differentially expressed genes. (5/3010)

Colchicine inhibition of the first phase of amyloid synthesis in experimental animals. (6/3010)

Ancestral origins and worldwide distribution of the PRNP 200K mutation causing familial Creutzfeldt-Jakob disease. (7/3010)

Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. (8/3010)

Amyloid

Amyloid beta-Peptides

Serum Amyloid A Protein

Amyloid beta-Protein Precursor

Plaque, Amyloid

Islet Amyloid Polypeptide

Amyloidosis

Cerebral Amyloid Angiopathy

Serum Amyloid P-Component

Amyloid Neuropathies

Amyloid Precursor Protein Secretases

Alzheimer Disease

Congo Red

Amyloid Neuropathies, Familial

Prealbumin

Peptide Fragments

Aspartic Acid Endopeptidases

Presenilin-1

Thiazoles

Mice, Transgenic

Brain

Cerebral Amyloid Angiopathy, Familial

Prions

Protein Structure, Secondary

Amyloidosis, Familial

Neurofibrillary Tangles

Amino Acid Sequence

tau Proteins

Molecular Sequence Data

Protein Multimerization

Microscopy, Electron, Transmission

Microscopy, Atomic Force

Protease Nexins

Protein Folding

beta 2-Microglobulin

Aniline Compounds

Neurons

Disease Models, Animal

Endopeptidases

Circular Dichroism

Insulysin

Microscopy, Electron

Protein Conformation

Presenilin-2

Protein Binding

Mutation

Models, Molecular

Protein Structure, Tertiary

Alzheimer Vaccines

Protein Structure, Quaternary

Peptides

Hippocampus

alpha-Synuclein

Cerebral Cortex

Spectroscopy, Fourier Transform Infrared

Immunohistochemistry

Neurofibrils

Mice, Inbred C57BL

Apolipoproteins E

Gerstmann-Straussler-Scheinker Disease

Peptide Termination Factors

Apolipoprotein E4

Microglia

Aging

Cells, Cultured

Presenilins

Kinetics

Neurodegenerative Diseases

Receptors, Islet Amyloid Polypeptide

Nerve Tissue Proteins

Neprilysin

Islets of Langerhans

Recombinant Proteins

Protein Processing, Post-Translational

Protein Denaturation

Positron-Emission Tomography

Acute-Phase Reaction

PC12 Cells

Nuclear Magnetic Resonance, Biomolecular

Maze Learning