alpha-Synuclein: A synuclein that is a major component of LEWY BODIES that plays a role in neurodegeneration and neuroprotection.Synucleins: A family of homologous proteins of low MOLECULAR WEIGHT that are predominately expressed in the BRAIN and that have been implicated in a variety of human diseases. They were originally isolated from CHOLINERGIC FIBERS of TORPEDO.gamma-Synuclein: A homolog of ALPHA-SYNUCLEIN that plays a role in neurofilament network integrity. It is overexpressed in a variety of human NEOPLASMS and may be involved in modulating AXON architecture during EMBRYONIC DEVELOPMENT and in the adult. Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.Impulse Control Disorders: Disorders whose essential features are the failure to resist an impulse, drive, or temptation to perform an act that is harmful to the individual or to others. Individuals experience an increased sense of tension prior to the act and pleasure, gratification or release of tension at the time of committing the act.beta-Synuclein: A synuclein that is closely related to ALPHA-SYNUCLEIN. It may play a neuroprotective role against some of the toxic effects of aggregated ALPHA-SYNUCLEIN.Parkinson Disease: A progressive, degenerative neurologic disease characterized by a TREMOR that is maximal at rest, retropulsion (i.e. a tendency to fall backwards), rigidity, stooped posture, slowness of voluntary movements, and a masklike facial expression. Pathologic features include loss of melanin containing neurons in the substantia nigra and other pigmented nuclei of the brainstem. LEWY BODIES are present in the substantia nigra and locus coeruleus but may also be found in a related condition (LEWY BODY DISEASE, DIFFUSE) characterized by dementia in combination with varying degrees of parkinsonism. (Adams et al., Principles of Neurology, 6th ed, p1059, pp1067-75)Dopamine: One of the catecholamine NEUROTRANSMITTERS in the brain. It is derived from TYROSINE and is the precursor to NOREPINEPHRINE and EPINEPHRINE. Dopamine is a major transmitter in the extrapyramidal system of the brain, and important in regulating movement. A family of receptors (RECEPTORS, DOPAMINE) mediate its action.Protein D-Aspartate-L-Isoaspartate Methyltransferase: A PROTEIN O-METHYLTRANSFERASE that recognizes and catalyzes the methyl esterification of ISOASPARTIC ACID and D-ASPARTIC ACID residues in peptides and proteins. It initiates the repair of proteins damaged by the spontaneous decomposition of normal L-aspartic acid and L-asparagine residues.Lewy Bodies: Intracytoplasmic, eosinophilic, round to elongated inclusions found in vacuoles of injured or fragmented neurons. The presence of Lewy bodies is the histological marker of the degenerative changes in LEWY BODY DISEASE and PARKINSON DISEASE but they may be seen in other neurological conditions. They are typically found in the substantia nigra and locus coeruleus but they are also seen in the basal forebrain, hypothalamic nuclei, and neocortex.Nerve Tissue ProteinsParkinsonian Disorders: A group of disorders which feature impaired motor control characterized by bradykinesia, MUSCLE RIGIDITY; TREMOR; and postural instability. Parkinsonian diseases are generally divided into primary parkinsonism (see PARKINSON DISEASE), secondary parkinsonism (see PARKINSON DISEASE, SECONDARY) and inherited forms. These conditions are associated with dysfunction of dopaminergic or closely related motor integration neuronal pathways in the BASAL GANGLIA.Neurodegenerative Diseases: 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.Molecular Sequence Data: 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.Neurons: 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.Amino Acid Sequence: 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.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Brain: 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.Receptors, Adrenergic, alpha: One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.Mice, Transgenic: Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.Hypoxia-Inducible Factor 1, alpha Subunit: Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.alpha7 Nicotinic Acetylcholine Receptor: A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.Integrin alpha3beta1: Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.Integrin alpha4: An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.Integrin alpha6: An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.Integrin alpha5beta1: An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Interleukin-1alpha: An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.Integrin alpha2beta1: An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.Receptors, Adrenergic, alpha-1: A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.Integrin alpha5: This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.Receptors, Adrenergic, alpha-2: A subclass of alpha-adrenergic receptors found on both presynaptic and postsynaptic membranes where they signal through Gi-Go G-PROTEINS. While postsynaptic alpha-2 receptors play a traditional role in mediating the effects of ADRENERGIC AGONISTS, the subset of alpha-2 receptors found on presynaptic membranes signal the feedback inhibition of NEUROTRANSMITTER release.Integrin alpha6beta1: A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Access to Information: Individual's rights to obtain and use information collected or generated by others.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.National Institutes of Health (U.S.): An operating division of the US Department of Health and Human Services. It is concerned with the overall planning, promoting, and administering of programs pertaining to health and medical research. Until 1995, it was an agency of the United States PUBLIC HEALTH SERVICE.Research Report: Detailed account or statement or formal record of data resulting from empirical inquiry.PrimatesAging: The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.Gene Duplication: Processes occurring in various organisms by which new genes are copied. Gene duplication may result in a MULTIGENE FAMILY; supergenes or PSEUDOGENES.Multiple System Atrophy: A syndrome complex composed of three conditions which represent clinical variants of the same disease process: STRIATONIGRAL DEGENERATION; SHY-DRAGER SYNDROME; and the sporadic form of OLIVOPONTOCEREBELLAR ATROPHIES. Clinical features include autonomic, cerebellar, and basal ganglia dysfunction. Pathologic examination reveals atrophy of the basal ganglia, cerebellum, pons, and medulla, with prominent loss of autonomic neurons in the brain stem and spinal cord. (From Adams et al., Principles of Neurology, 6th ed, p1076; Baillieres Clin Neurol 1997 Apr;6(1):187-204; Med Clin North Am 1999 Mar;83(2):381-92)Metencephalon: The anterior portion of the developing hindbrain. It gives rise to the CEREBELLUM and the PONS.Lewy Body Disease: A neurodegenerative disease characterized by dementia, mild parkinsonism, and fluctuations in attention and alertness. The neuropsychiatric manifestations tend to precede the onset of bradykinesia, MUSCLE RIGIDITY, and other extrapyramidal signs. DELUSIONS and visual HALLUCINATIONS are relatively frequent in this condition. Histologic examination reveals LEWY BODIES in the CEREBRAL CORTEX and BRAIN STEM. SENILE PLAQUES and other pathologic features characteristic of ALZHEIMER DISEASE may also be present. (From Neurology 1997;48:376-380; Neurology 1996;47:1113-1124)Journalism, Medical: The collection, writing, and editing of current interest material on topics related to biomedicine for presentation through the mass media, including newspapers, magazines, radio, or television, usually for a public audience such as health care consumers.Psychiatry: The medical science that deals with the origin, diagnosis, prevention, and treatment of mental disorders.
Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. (1/1546)
alpha-Synuclein is a soluble presynaptic protein which is pathologically redistributed within intracellular lesions characteristic of several neurodegenerative diseases. Here we demonstrate that wild type and two mutant forms of alpha-synuclein linked to familial Parkinson's disease (Ala30 --> Pro and Ala53 --> Thr) self-aggregate and assemble into 10-19-nm-wide filaments with distinct morphologies under defined in vitro conditions. Immunogold labeling demonstrates that the central region of all these filaments are more robustly labeled than the N-terminal or C-terminal regions, suggesting that the latter regions are buried within the filaments. Since in vitro generated alpha-synuclein filaments resemble the major ultrastructural elements of authentic Lewy bodies that are hallmark lesions of Parkinson's disease, we propose that self-aggregating alpha-synuclein is the major subunit protein of these filamentous lesions. (+info)Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation. (2/1546)
Parkinson's disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major component of which are filaments consisting of alpha-synuclein. Two recently identified point mutations in alpha-synuclein are the only known genetic causes of PD, but their pathogenic mechanism is not understood. Here we show that both wild type and mutant alpha-synuclein form insoluble fibrillar aggregates with antiparallel beta-sheet structure upon incubation at physiological temperature in vitro. Importantly, aggregate formation is accelerated by both PD-linked mutations. Under the experimental conditions, the lag time for the formation of precipitable aggregates is about 280 h for the wild type protein, 180 h for the A30P mutant, and only 100 h for the A53T mutant protein. These data suggest that the formation of alpha-synuclein aggregates could be a critical step in PD pathogenesis, which is accelerated by the PD-linked mutations. (+info)Copper(II)-induced self-oligomerization of alpha-synuclein. (3/1546)
alpha-Synuclein is a component of the abnormal protein depositions in senile plaques and Lewy bodies of Alzheimer's disease (AD) and Parkinson's disease respectively. The protein was suggested to provide a possible nucleation centre for plaque formation in AD via selective interaction with amyloid beta/A4 protein (Abeta). We have shown previously that alpha-synuclein has experienced self-oligomerization when Abeta25-35 was present in an orientation-specific manner in the sequence. Here we examine this biochemically specific self-oligomerization with the use of various metals. Strikingly, copper(II) was the most effective metal ion affecting alpha-synuclein to form self-oligomers in the presence of coupling reagents such as dicyclohexylcarbodi-imide or N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline. The size distribution of the oligomers indicated that monomeric alpha-synuclein was oligomerized sequentially. The copper-induced oligomerization was shown to be suppressed as the acidic C-terminus of alpha-synuclein was truncated by treatment with endoproteinase Asp-N. In contrast, the Abeta25-35-induced oligomerizations of the intact and truncated forms of alpha-synuclein were not affected. This clearly indicated that the copper-induced oligomerization was dependent on the acidic C-terminal region and that its underlying biochemical mechanism was distinct from that of the Abeta25-35-induced oligomerization. Although the physiological or pathological relevance of the oligomerization remains currently elusive, the common outcome of alpha-synuclein on treatment with copper or Abeta25-35 might be useful in understanding neurodegenerative disorders in molecular terms. In addition, abnormal copper homoeostasis could be considered as one of the risk factors for the development of disorders such as AD or Parkinson's disease. (+info)alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. (4/1546)
Parkinson's disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major components of which are filaments consisting of alpha-synuclein. Two recently identified point mutations in alpha-synuclein are the only known genetic causes of PD. alpha-Synuclein fibrils similar to the Lewy body filaments can be formed in vitro, and we have shown recently that both PD-linked mutations accelerate their formation. This study addresses the mechanism of alpha-synuclein aggregation: we show that (i) it is a nucleation-dependent process that can be seeded by aggregated alpha-synuclein functioning as nuclei, (ii) this fibril growth follows first-order kinetics with respect to alpha-synuclein concentration, and (iii) mutant alpha-synuclein can seed the aggregation of wild type alpha-synuclein, which leads us to predict that the Lewy bodies of familial PD patients with alpha-synuclein mutations will contain both, the mutant and the wild type protein. Finally (iv), we show that wild type and mutant forms of alpha-synuclein do not differ in their critical concentrations. These results suggest that differences in aggregation kinetics of alpha-synucleins cannot be explained by differences in solubility but are due to different nucleation rates. Consequently, alpha-synuclein nucleation may be the rate-limiting step for the formation of Lewy body alpha-synuclein fibrils in Parkinson's disease. (+info)alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. (5/1546)
alpha-Synuclein has been implicated in the pathophysiology of many neurodegenerative diseases, including Parkinson's disease (PD) and Alzheimer's disease. Mutations in alpha-synuclein cause some cases of familial PD (Polymeropoulos et al., 1997; Kruger et al., 1998). In addition, many neurodegenerative diseases show accumulation of alpha-synuclein in dystrophic neurites and in Lewy bodies (Spillantini et al., 1998). Here, we show that alpha-synuclein shares physical and functional homology with 14-3-3 proteins, which are a family of ubiquitous cytoplasmic chaperones. Regions of alpha-synuclein and 14-3-3 proteins share over 40% homology. In addition, alpha-synuclein binds to 14-3-3 proteins, as well as some proteins known to associate with 14-3-3, including protein kinase C, BAD, and extracellular regulated kinase, but not Raf-1. We also show that overexpression of alpha-synuclein inhibits protein kinase C activity. The association of alpha-synuclein with BAD and inhibition of protein kinase C suggests that increased expression of alpha-synuclein could be harmful. Consistent with this hypothesis, we observed that overexpression of wild-type alpha-synuclein is toxic, and overexpression of alpha-synuclein containing the A53T or A30P mutations exhibits even greater toxicity. The activity and binding profile of alpha-synuclein suggests that it might act as a protein chaperone and that accumulation of alpha-synuclein could contribute to cell death in neurodegenerative diseases. (+info)Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies. (6/1546)
Alzheimer's disease and Parkinson's disease are the most common neurodegenerative diseases. They are characterized by the degeneration of selected populations of nerve cells that develop filamentous inclusions before degeneration. The neuronal inclusions of Alzheimer's disease are made of the microtubule-associated protein tau, in a hyperphosphorylated state. Recent work has shown that the filamentous inclusions of Parkinson's disease are made of the protein alpha-synuclein and that rare, familial forms of Parkinson's disease are caused by missense mutations in the alpha-synuclein gene. Besides Parkinson's disease, the filamentous inclusions of two additional neurodegenerative diseases, namely dementia with Lewy bodies and multiple system atrophy, have also been found to be made of alpha-synuclein. Abundant filamentous tau inclusions are not limited to Alzheimer's disease. They are the defining neuropathological characteristic of frontotemporal dementias such as Pick's disease, and of progressive supranuclear palsy and corticobasal degeneration. The recent discovery of mutations in the tau gene in familial forms of frontotemporal dementia has provided a direct link between tau dysfunction and dementing disease. The new work has established that tauopathies and alpha-synucleinopathies account for most late-onset neurodegenerative diseases in man. The formation of intracellular filamentous inclusions might be the gain of toxic function that leads to the demise of affected brain cells. (+info)alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. (7/1546)
alpha-Synuclein has been implicated in the pathogenesis of several neurodegenerative disorders based on the direct linking of missense mutations in alpha-synuclein to autosomal dominant Parkinson's disease and its presence in Lewy-like lesions. To gain insight into alpha-synuclein functions, we have investigated whether it binds neuronal proteins and modulates their functional state. The microtubule-associated protein tau was identified as a ligand by alpha-synuclein affinity chromatography of human brain cytosol. Direct binding assays using (125)I-labeled human tau40 demonstrated a reversible binding with a IC(50) about 50 pM. The interacting domains were localized to the C terminus of alpha-synuclein and the microtubule binding region of tau as determined by protein fragmentation and the use of recombinant peptides. High concentrations of tubulin inhibited the binding between tau and alpha-synuclein. Functionally, alpha-synuclein stimulated the protein kinase A-catalyzed phosphorylation of tau serine residues 262 and 356 as determined using a phospho-epitope-specific antibody. We propose that alpha-synuclein modulates the phosphorylation of soluble axonal tau and thereby indirectly affects the stability of axonal microtubules. (+info)The genetics of disorders with synuclein pathology and parkinsonism. (8/1546)
Despite being considered the archetypal non-genetic neurological disorder, genetic analysis of Parkinson's disease has shown that there are at least three genetic loci. Furthermore, these analyses have suggested that the phenotype of the pathogenic loci is wider than simple Parkinson's disease and may include Lewy body dementia and some forms of essential tremor. Identification of alpha-synuclein as the first of the loci involved in Parkinson's disease and the identification of this protein in pathological deposits in other disorders has led to the suggestion that it may share pathogenic mechanisms with multiple system atrophy, Alzheimer's disease and prion disease and that these mechanisms are related to a synuclein pathway to cell death. Finally, genetic analysis of the synuclein diseases and the tau diseases may indicate that this synuclein pathway is an alternative to the tau pathway to cell death. (+info)
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Clumps of rogue Parkinson's proteins spread to new neurons and seed more clumps - PhenomenaSpillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M (August 1997). "Alpha-synuclein in Lewy bodies". Nature ... alpha-synuclein was discovered to be the major component of Lewy bodies within brain cells of PD patients; according to the ... alpha-synuclein. Lazzarini worked with the Italian Instituto de Scienze Neurologiche to get blood samples from the family ... that fragments of alpha-synuclein bind to other proteins to form the Lewy body, an insoluble proteinaceous material ...
The NIH team and a team led by Maria Spillantini reported on alpha-synuclein deposits in Lewy bodies as well as alpha-synuclein ... Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M (1997). "Alpha-synuclein in Lewy bodies". Nature. 388 ( ... Mezey E, Dehejia A, Harta G, Papp MI, Polymeropoulos MH, Brownstein MJ (1998). "Alpha synuclein in neurodegenerative disorders ... 1997). "Mutation in the alpha-synuclein gene identified in families with Parkinson's disease". Science. 276 (5321): 2045-7. doi ...
... alpha-synuclein. Within days of the publication of the PARK1 findings, alpha-synuclein was discovered to be the major component ... Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M (August 1997). "Alpha-synuclein in Lewy bodies". Nature ... Schulz-Schaeffer WJ (August 2010). "The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, ... "Mutation in the alpha-synuclein gene identified in families with Parkinson's disease". Science. 276 (5321): 2045-7. doi:10.1126 ...
She is most noted for identifying the protein alpha-synuclein as the major component of Lewy bodies, the characteristic protein ... Spillantini, MG; Schmidt, ML; Lee, VM; Trojanowski, JQ; Jakes, R; Goedert, M (Aug 28, 1997). "Alpha-synuclein in Lewy bodies". ... In particular her work studies the role of microtubule-associated protein tau and alpha-synuclein aggregation in the ...
"Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct". Science (New York, N.Y.). 294 ( ... "Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein". Neuron. 34 (4): ... Wild-type alpha-synuclein fibrils are known to be the primary component of Lewy bodies, which are found in the brain of ... A53T alpha-synuclein has also been linked to early on-set familial Parkinson's disease. Advancements in technology have allowed ...
Preclinical research also targets alpha-synuclein. Selegiline is in a group of medications called monoamine oxidase type B (MAO ...
Preclinical research also targets alpha-synuclein. A vaccine that primes the human immune system to destroy alpha-synuclein, ... In 1997, alpha-synuclein was found to be the main component of Lewy bodies by Spillantini, Trojanowski, Goedert and others. ... SNCA gene mutations are important in PD because the protein that gene encodes, alpha-synuclein, is the main component of the ... One mechanism consists of an abnormal accumulation of the protein alpha-synuclein bound to ubiquitin in the damaged cells. This ...
Alpha-synuclein is the primary structural component of Lewy body fibrils. In addition, an alpha-synuclein fragment, known as ... Transglutaminase substrates: Amyloid-beta, tau, alpha-synuclein and huntingtin have been proved to be substrates of ... alpha-synuclein: can aggregate to form insoluble fibrils in pathological conditions characterized by Lewy bodies, such as ... Alpha-synuclein can damage membranes by inducing membrane curvature,[12] and cause extensive tubulation and vesiculation when ...
"Alpha-synuclein and tau: teammates in neurodegeneration?". Mol Neurodegener. 9: 43. doi:10.1186/1750-1326-9-43. PMC 4230508 . ... Tauopathies are often overlapped with synucleinopathies, possibly due to interaction between the synuclein and tau proteins. ... "Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons". Cell. 154 (1): 103-17. doi:10.1016/j.cell. ...
"Alpha-synuclein and tau: teammates in neurodegeneration?". Mol Neurodegener. doi:10.1186/1750-1326-9-43. PMC 4230508 . PMID ... are neurodegenerative diseases characterised by the abnormal accumulation of aggregates of alpha-synuclein protein in neurons, ... Jun 2015). "α-Synuclein strains cause distinct synucleinopathies after local and systemic administration". Nature. advance ... Other rare disorders, such as various neuroaxonal dystrophies, also have α-synuclein pathologies. Because each of the ...
Kawahara K, Hashimoto M, Bar-On P, Ho GJ, Crews L, Mizuno H, Rockenstein E, Imam SZ, Masliah E (March 2008). "alpha-Synuclein ... Parkin might promote aggregation of alpha-synuclein and synphilin-1 into Lewy bodies, which are conjugated to Lys63-linked poly ... Another parkin substrate, synphilin-1 (encoded by SNCAIP), is an alpha-synuclein interacting protein that is enriched in the ... Parkin (ligase) has been shown to interact with: Alpha-synuclein, CASK, CUL1, FBXW7 and GPR37, HSPA1A, HSPA8, Multisynthetase ...
Lee FJ, Liu F, Pristupa ZB, Niznik HB (2001). "Direct binding and functional coupling of alpha-synuclein to the dopamine ... Dopamine transporter has been shown to interact with: Alpha-synuclein, PICK1, and TGFB1I1. Apart from these innate protein- ... Wersinger C, Sidhu A (2003). "Attenuation of dopamine transporter activity by alpha-synuclein". Neurosci. Lett. 340 (3): 189-92 ...
Chandra S, Gallardo G, Fernández-Chacón R, Schlüter OM, Südhof TC (November 2005). "Alpha-synuclein cooperates with CSPalpha in ... 2005). "Characterization of the G alpha(s) regulator cysteine string protein". J. Biol. Chem. 280 (34): 30236-41. doi:10.1074/ ... "The synaptic vesicle protein CSP alpha prevents presynaptic degeneration". Neuron. 42 (2): 237-51. doi:10.1016/S0896-6273(04) ... encoding cysteine-string protein alpha, cause autosomal-dominant adult-onset neuronal ceroid lipofuscinosis". American Journal ...
"Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein". The Journal of Biological Chemistry. 275 ( ... Pronin AN, Morris AJ, Surguchov A, Benovic JL (Aug 2000). "Synucleins are a novel class of substrates for G protein-coupled ... Zhou H, Yan F, Tai HH (Sep 2001). "Phosphorylation and desensitization of the human thromboxane receptor-alpha by G protein- ...
... the primary structural component of which is alpha-synuclein. Cortical Lewy bodies are also composed of alpha-synuclein fibrils ... Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM (February 2004). "Aggresomes formed by alpha-synuclein and synphilin- ... A Lewy body is composed of the protein alpha-synuclein associated with other proteins, such as ubiquitin, neurofilament protein ... Engelender S (April 2008). "Ubiquitination of alpha-synuclein and autophagy in Parkinson's disease". Autophagy. 4 (3): 372-4. ...
Esteves, AR; Arduíno, DM; Silva, DF; Oliveira, CR; Cardoso, SM (2011). "Mitochondrial Dysfunction: The Road to Alpha-Synuclein ... Parkinson's disease is characterized by inclusions of a protein called alpha-synuclien (Lewy bodies) in affected neurons that ...
... stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha ... "Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)". Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (June ... Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM (2004). "Aggresomes formed by alpha-synuclein and synphilin-1 are ... The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic ...
"Comparison of kindreds with parkinsonism and alpha-synuclein genomic multiplications". Ann Neurol. 55 (2): 174-9. doi:10.1002/ ...
It inhibits PTK2B/RAFTK activity and regulates alpha-synuclein phosphorylation. It interacts with Signal-regulatory protein ... and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein ... RA receptor alpha in acute promyelocytic leukemia cells". The Journal of Biological Chemistry. 276 (25): 22375-81. doi:10.1074/ ... alpha and directs integrin-activated cytoskeletal reorganization in macrophages. GRCh38: Ensembl release 89: ENSG00000005020 - ...
Esteves, AR; Arduíno, DM; Silva, DF; Oliveira, CR; Cardoso, SM (2011). "Mitochondrial Dysfunction: The Road to Alpha-Synuclein ... Additionally, in the microenvironment of cancer cells, there is an increase in hypoxia-inducible transcription factor 1-alpha ( ...
Chen, M.; Margittai, M.; Chen, J.; Langen, R. (2007). "Investigation of alpha-Synuclein Fibril Structure by Site-directed Spin ... to understand the structure of amyloid fibrils and the structure of membrane bound Parkinson's disease protein alpha-synuclein ...
Alpha-synuclein is the primary structural component of Lewy body fibrils. In addition, an alpha-synuclein fragment, known as ... Membrane damage by alpha-synuclein could be another Parkinson's disease mechanism. The main known risk factor is age. ... alpha-synuclein: can aggregate to form insoluble fibrils in pathological conditions characterized by Lewy bodies, such as ... The latest research on pathogenesis of disease has shown that the death of dopaminergic neurons by alpha-synuclein is due to a ...
A study in 2018 suggests a post-translationally modified form of the protein called alpha-synuclein may be a causal agent for ... Arima K, Uéda K, Sunohara N, Arakawa K, Hirai S, Nakamura M, Tonozuka-Uehara H, Kawai M (November 1998). "NACP/alpha-synuclein ... Recent studies have shown that the major filamentous component of glial and neuronal cytoplasmic inclusions is alpha-synuclein. ... "Genetic variants of the alpha-synuclein gene SNCA are associated with multiple system atrophy". PLoS ONE. 4 (9): e7114. Bibcode ...
Singleton AB (2005). "Altered alpha-synuclein homeostasis causing Parkinson's disease: the potential roles of dardarin". Trends ... "Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of α-synuclein ...
Elkon H, Don J, Melamed E, Ziv I, Shirvan A, Offen D (June 2002). "Mutant and wild-type alpha-synuclein interact with ...
Vallenius T، Luukko K، Mäkelä TP (2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4 ... binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells.". ...
... indicating that alpha-synuclein antagonizes SNARE function. Ykt6 reversed alpha-synuclein inhibition much more effectively than ... Finally, soluble alpha-synuclein A53T directly bound ER/Golgi SNAREs and inhibited SNARE complex assembly, providing a ... Overexpression of wild type or the familial disease-associated A53T mutant alpha-synuclein delayed transport by up to 50%; ... We tested elements of this hypothesis by expressing human alpha-synuclein in mammalian kidney and neuroendocrine cells and ...
Multiple System Atrophy Workup: Approach Considerations, MRI, PET ScanningUbiquitin positive, alpha-B-crystallin (synuclein) positive, alpha- and beta-tubulin positive, tau-protein positive ... Ubiquitin positive, alpha-B-crystallin (synuclein) positive, alpha- and beta-tubulin positive, tau-protein positive ... The role of alpha-synuclein in the pathogenesis of multiple system atrophy. Acta Neuropathol. 2005. 109:129-40. [Medline]. ... GCIs are ubiquitin-positive, tau-positive, and alpha-synuclein ̶ positive oligodendroglial inclusions. They are different from ...
Multiple System Atrophy / MSA | ColumbiaDoctorsThe cause of MSA is unknown, but it seems related to the build-up of a protein (alpha-synuclein) in glial cells that protect ...
Multiple system atrophy - Your.MDThe brain cells of a person with multiple system atrophy contain misfolded alpha-synuclein protein (of which there is lots of ... Its thought that a build-up of abnormal alpha-synuclein is responsible for the loss of brain cells. ...
... is a neurodegenerative disease with glial cytoplasmatic inclusion organic structures incorporating alpha synuclein protein. ...
Therefore, NACP is now referred to as human alpha-synuclein. Alpha-synuclein is a synuclein protein of unknown function ... which contain rich cytosolic alpha-synuclein but very low levels of mitochondrial alpha-synuclein. It has been shown that alpha ... The human alpha-synuclein protein is made of 140 amino acids and is encoded by the SNCA gene. An alpha-synuclein fragment, ... Other isoforms are alpha-synuclein-126, which lacks residues 41-54 due to loss of exon 3; and alpha-synuclein-112, which lacks ...
alpha-synuclein"Cellular milieu imparts distinct pathological {alpha}-synuclein strains in {alpha}-synucleinopathies," by Chao Peng, Ronald J. ... A. "[alpha]-synuclein interacts with PrPC to induce cognitive impairment through mGluR5 and NMDAR2B," by Diana G Ferreira, ... C. "{alpha}-Synuclein binds and sequesters PIKE-L into Lewy bodies, triggering dopaminergic cell death via AMPK hyperactivation ... "alpha}-Synuclein promotes dilation of the exocytotic fusion pore," by Todd Logan, Jacob Bendor, Chantal Toupin, Kurt Thorn & ...
The behavior of alpha-synuclein in neurons. - PubMed - NCBIThe behavior of alpha-synuclein in neurons.. Fortin DL1, Nemani VM, Nakamura K, Edwards RH. ... alpha-Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with ... To address the dynamics of the protein in live cells, we have used photobleaching and found that alpha-synuclein exhibits high ... In addition to the presumed role of alpha-synuclein dynamics in synaptic function, changes in its physiological behavior may ...
Dominantly inherited mutations in alpha-synuclein cause Parkinsons disease, but the physiological role of alpha-synuclein ... Alpha-synuclein and cysteine-string protein-alpha (CSPalpha) are abundant synaptic vesicle proteins independently linked to ... transgenic alpha-synuclein ameliorates this inhibition. In preventing neurodegeneration in CSPalpha-deficient mice, alpha- ... Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration.. Chandra S1, Gallardo G, Fernández-Chacón R, Schlüter ...
... by modulation of glial function following activation by soluble or insoluble modified alpha-synuclein (alpha-syn), a chief ... Nitrated alpha-synuclein-activated microglial profiling for Parkinsons disease.. Reynolds AD1, Glanzer JG, Kadiu I, Ricardo- ... alpha-Syn is nitrated during oxidative stress responses and in its aggregated form, induces inflammatory microglial functions. ... To this end, PD-associated inflammation was modeled by stimulation of microglia with aggregated and nitrated alpha-syn. These ...
The rationale for this project is that a therapeutic antibody against alpha-synuclein will be able to block its harmful effects ... Project Description: Antibodies binding to alpha-synuclein have been selected in cell models. One of them has shown positive ... By antibody engineering we will learn about the importance of the strength of antibody binding to alpha-synuclein, and ... Relevance to Diagnosis/Treatment of Parkinsons Disease: Immunotherapy targeting alpha-synuclein is a new way of treating PD. ...
Rabbit polyclonal Alpha-synuclein antibody validated for ICC/IF and tested in Human and Rat. Referenced in 4 publications. ... Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine ... Synthetic peptide corresponding to Human Alpha-synuclein aa 111-131 (C terminal).. Sequence: GILEDMPVDPDNEAYEMPSEE ... A 6.4 Mb duplication of the a-synuclein locus causing frontotemporal dementia and Parkinsonism: phenotype-genotype correlations ...
Chicken polyclonal Alpha-synuclein antibody. Validated in WB, IHC, ICC/IF and tested in Mouse, Rat, Horse, Chicken, Cow, Human ... Protein - Recombinant Human Alpha-synuclein protein aggregate (Active) (ab218819) WB, Functional Studies, SDS-PAGE ... Anti-Alpha-synuclein antibody (ab190376) at 1/2000 dilution + Rat brain crude extract. Predicted band size: 14 kDa. ... Ab190376 staining alpha-synuclein in rat cerebellum tissue sections at 1/3000 dilution (red) and co-stained with rabbit ...
Alpha-synuclein Expression Lowering therapeutics: Hit Confirmation. MJFF Research Grant, 2011. Objective/Rationale:. Simply ... To rid brains of Parkinsons patients of alpha-synuclein toxicity one can attempt to clear the protein from the brain, block ... Brains of most patients with Parkinsons are littered with intracellular accumulations of alpha-synuclein, a small 140 amino- ... or ameliorate the consequences of alpha-synuclein toxicity. We hypothesize, that the most direct and acute solution, however, ...
Oligomeric Alpha-synuclein in Multiple System Atrophy - Full Text View - ClinicalTrials.govTotal alpha-synuclein concentration in CSF and oligomeric/total alpha-synuclein ratio in CSF [ Time Frame: Day 0 ]. *Oligomeric ... The oligomeric alpha-synuclein seems to be particularly involved in abnormal protein aggregation in alpha-synucleinopathies. ... and total alpha-synuclein concentration in plasma and oligomeric/total alpha-synuclein ratio in plasma [ Time Frame: Day 0 ]. ... Oligomeric Alpha-synuclein in Multiple System Atrophy (BIOAMS). The safety and scientific validity of this study is the ...
Gastrointestinal Biopsies for the Diagnosis of Alpha-Synuclein Pathology in Parkinson's DiseaseA major component of these inclusions is phosphorylated alpha-synuclein (,i,α,/i,-SYN) protein. There is evidence that ,i,α,/i ... A major component of these inclusions is phosphorylated alpha-synuclein (α-SYN) protein. There is evidence that α-SYN pathology ... K. M. Shannon, A. Keshavarzian, H. B. Dodiya, S. Jakate, and J. H. Kordower, "Is alpha-synuclein in the colon a biomarker for ... M. G. Cersosimo, C. Perandones, F. E. Micheli et al., "Alpha-synuclein immunoreactivity in minor salivary gland biopsies of ...
TSRI - News & View, Scientists 'Watch' as Individual Alpha-Synuclein Proteins Change ShapeTo comply with the National Institutes of Health (NIH) Public Access Policy, a PubMed Central reference number (PMCID) is required in NIH grant applications, proposals, and progress reports for any paper "authored by you or [arising] from your NIH funds (even if you are not an author)" (see http://publicaccess.nih.gov/FAQ.htm#c8).. One way to find the PMCID number is to use PubMed Centrals PMID: PMCID Converter available at http://www.ncbi.nlm.nih.gov/sites/pmctopmid. If you already have the PMID from a PubMed search (it may appear as the Accession Number in your EndNote library), the above converter will provide you with the corresponding PMCID to include in your grant. If you do not have the PMID number, you can look up a PMCID in PubMed. It will be listed in the lower right corner of the AbstractPlus view. A PMCID number will be assigned as soon as an article has successfully been submitted to PMC (see http://publicaccess.nih.gov/FAQ.htm#c9). If you have questions about the NIH Public Access ...
SNCA - Alpha-synuclein - Papio anubis (Olive baboon) - SNCA gene & proteinAlpha-synucleinUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... tr,A0A2I3N0Z9,A0A2I3N0Z9_PAPAN Alpha-synuclein OS=Papio anubis OX=9555 GN=SNCA PE=3 SV=1 ... Belongs to the synuclein family.UniRule annotation. Automatic assertion according to rulesi ...
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading | PNAS2009) Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J Neurochem ... Templated seeding of alpha-synuclein aggregation. Marija Iljina, Gonzalo A. Garcia, Mathew H. Horrocks, Laura Tosatto, Minee L. ... Templated seeding of alpha-synuclein aggregation. Marija Iljina, Gonzalo A. Garcia, Mathew H. Horrocks, Laura Tosatto, Minee L. ... 2008) alpha-Synuclein gene duplication is present in sporadic Parkinson disease. Neurology 70(1):43-49. ...
Blood Plasma of Patients with Parkinsons Disease Increases Alpha-Synuclein Aggregation and Neurotoxicity. Peng Wang,1,2 Xin Li ... This has been attributed to the spread of α-synuclein (α-syn) aggregates, which involves release of α-syn from a neuron and its ...
Mutant Alpha-Synuclein Causes Age-Dependent Neuropathology in Monkey Brain | Journal of Neuroscience2002) Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein. Neuron 34:521 ... 2003) Alpha-synuclein pathology affecting Bergmann glia of the cerebellum in patients with alpha-synucleinopathies. Acta ... Mutant Alpha-Synuclein Causes Age-Dependent Neuropathology in Monkey Brain. Weili Yang, Guohao Wang, Chuan-En Wang, Xiangyu Guo ... Mutant Alpha-Synuclein Causes Age-Dependent Neuropathology in Monkey Brain. Weili Yang, Guohao Wang, Chuan-En Wang, Xiangyu Guo ...
Alpha-Synuclein Detection. Synuclein family members (alpha-, beta-, and gamma-synuclein) are expressed at high levels in adult ... Alpha-synuclein (C‑terminus). 18671A, B. IHC. WB. Human. (S122). Rabbit IgG. Cross‑reacts with mouse and rat alpha-synuclein. ... ELISAs for Alpha-Synuclein Detection. The human alpha-synuclein assay kit (Cat. # 27740A) is a solid-phase sandwich ELISA using ... Antibodies for Alpha-Synuclein Detection. Anti-human alpha-synuclein antibody (Cat. # 18671A, B) is an affinity-purified IgG ...
Medical Xpress - alpha synucleinTargeting alpha-synuclein in the gut may slow down Parkinsons disease. Aggregates of the protein alpha-synuclein arising in ... is caused by the buildup of alpha-synuclein proteins in the brain. The biological function of alpha-synuclein is still not ... ... Research by University at Buffalo biologists is providing new insights into alpha-synuclein, a small acidic protein associated ... are associated with the accumulation of alpha-synuclein proteins in the brain. Researchers at the German Center for ...
alpha Synuclein Antibody (710110)
Invitrogen Anti-alpha Synuclein Recombinant Polyclonal (14HCLC), Catalog # 710110. Tested in Western Blot (WB), ... Mutation of the alpha-synuclein gene is associated with familial forms of PD. Alpha-Synuclein is known to reduce the ... Alpha-Synuclein is involved in the formation of SNARE complexes, and most significantly, aggregated alpha-synuclein is one of ... Alpha-Synuclein belongs to the Synuclein family, which includes beta and gamma Synuclein, and is predominantly expressed in ...
Pathology Outlines - Alpha-synucleinMember of the synuclein family of soluble proteins (alpha-synuclein, beta-synuclein and gamma-synuclein) that are commonly ... Alpha-synuclein. Author: Meenakshi Vij Gupta, M.D. (see Authors page). Revised: 23 May 2016, last major update May 2016. ... Both the sporadic and the familial form of Alzheimer disease also demonstrate alpha-synuclein protein * In recent years, ... several studies have shown that alpha-synuclein aggregation can also be detected outside the central nervous system, ...
- The brain cells of a person with multiple system atrophy contain misfolded alpha-synuclein protein (of which there is lots of in the brain). (your.md)
- Ykt6 reversed alpha-synuclein inhibition much more effectively than sec22b, suggesting a possible neuroprotective role for the enigmatic high expression of ykt6 in neurons. (umt.edu)
- (columbiadoctors.org)
- The secretory delay occurred at low expression levels and was not accompanied by insoluble alpha-synuclein aggregates or mistargeting of transport machinery, suggesting a direct action of soluble alpha-synuclein on trafficking proteins. (umt.edu)
- It's thought that a build-up of abnormal alpha-synuclein is responsible for the loss of brain cells. (your.md)
- Toxicity of human alpha-synuclein when expressed in simple organisms can be suppressed by overexpression of endoplasmic reticulum (ER)-to-Golgi transport machinery, suggesting that inhibition of constitutive secretion represents a fundamental cause of the toxicity. (umt.edu)
- We tested elements of this hypothesis by expressing human alpha-synuclein in mammalian kidney and neuroendocrine cells and assessing ER-to-Golgi transport. (umt.edu)
- In in vitro reconstitutions, purified alpha-synuclein A53T protein specifically inhibited COPII vesicle docking and fusion at a pre-Golgi step. (umt.edu)
- Multiple system wasting ( MSA ) is a neurodegenerative disease with glial cytoplasmatic inclusion organic structures incorporating alpha synuclein protein. (hcamatcollegepark.com)
