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.
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.
A synuclein that is a major component of LEWY BODIES that plays a role in neurodegeneration and neuroprotection.
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.
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)
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.
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 proteins' are specialized proteins found within the nervous system's biological tissue, including neurofilaments, neuronal cytoskeletal proteins, and neural cell adhesion molecules, which facilitate structural support, intracellular communication, and synaptic connectivity essential for proper neurological function.
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.
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.
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.
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.
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 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.
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.

Axon pathology in Parkinson's disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein. (1/77)

Pathogenic alpha-synuclein (alphaS) gene mutations occur in rare familial Parkinson's disease (PD) kindreds, and wild-type alphaS is a major component of Lewy bodies (LBs) in sporadic PD, dementia with LBs (DLB), and the LB variant of Alzheimer's disease, but beta-synuclein (betaS) and gamma-synuclein (gammaS) have not yet been implicated in neurological disorders. Here we show that in PD and DLB, but not normal brains, antibodies to alphaS and betaS reveal novel presynaptic axon terminal pathology in the hippocampal dentate, hilar, and CA2/3 regions, whereas antibodies to gammaS detect previously unrecognized axonal spheroid-like lesions in the hippocampal dentate molecular layer. The aggregation of other synaptic proteins and synaptic vesicle-like structures in the alphaS- and betaS-labeled hilar dystrophic neurites suggests that synaptic dysfunction may result from these lesions. Our findings broaden the concept of neurodegenerative "synucleinopathies" by implicating betaS and gammaS, in addition to alphaS, in the onset/progression of PD and DLB.  (+info)

Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. (2/77)

alpha-, beta-, and gamma-Synuclein, a novel family of neuronal proteins, has become the focus of research interest because alpha-synuclein has been increasingly implicated in the pathogenesis of Parkinson's and Alzheimer's disease. However, the normal functions of the synucleins are still unknown. For this reason, we characterized alpha-, beta-, and gamma-synuclein expression in primary hippocampal neuronal cultures and showed that the onset of alpha- and beta-synuclein expression was delayed after synaptic development, suggesting that these synucleins may not be essential for synapse formation. In mature cultured primary neurons, alpha- and beta-synuclein colocalized almost exclusively with synaptophysin in the presynaptic terminal, whereas little gamma-synuclein was expressed at all. To assess the function of alpha-synuclein, we suppressed expression of this protein with antisense oligonucleotide technology. Morphometric ultrastructural analysis of the alpha-synuclein antisense oligonucleotide-treated cultures revealed a significant reduction in the distal pool of synaptic vesicles. These data suggest that one function of alpha-synuclein may be to regulate the size of distinct pools of synaptic vesicles in mature neurons.  (+info)

Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. (3/77)

Filamentous inclusions made of alpha-synuclein constitute the defining neuropathological characteristic of Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Rare familial cases of Parkinson's disease are associated with mutations A53T and A30P in alpha-synuclein. We report here the assembly properties and secondary structure characteristics of recombinant alpha-synuclein. Carboxy-terminally truncated human alpha-synuclein (1-87) and (1-120) showed the fastest rates of assembly, followed by human A53T alpha-synuclein, and rat and zebra finch alpha-synuclein. Wild-type human alpha-synuclein and the A30P mutant showed slower rates of assembly. Upon shaking, filaments formed within 48 h at 37 degrees C. The related proteins beta- and gamma-synuclein only assembled after several weeks of incubation. Synthetic human alpha-synuclein filaments were decorated by an antibody directed against the carboxy-terminal 10 amino acids of alpha-synuclein, as were filaments extracted from dementia with Lewy bodies and multiple system atrophy brains. Circular dichroism spectroscopy indicated that alpha-synuclein undergoes a conformational change from random coil to beta-sheet structure during assembly. X-ray diffraction and electron diffraction of the alpha-synuclein assemblies showed a cross-beta conformation characteristic of amyloid.  (+info)

Chaperone-like activity of synucleins. (4/77)

Synucleins are a family of small proteins that are predominantly expressed in neurons. The functions of the synucleins are not entirely understood, but they have been implicated in the pathogenesis of several neurodegenerative diseases. Our data show that alpha-, beta- or gamma-synuclein suppresses the aggregation of thermally denatured alcohol dehydrogenase and chemically denatured insulin. The A53T but not the A30P mutant alpha-synuclein was able to inhibit the aggregation of insulin and the chaperone-like activity of alpha-synuclein was lost upon removal of its C-terminal residues 98-140. These results demonstrate that synucleins with the exception of the A30P mutant possess chaperone-like activity.  (+info)

Properties of NACP/alpha-synuclein and its role in Alzheimer's disease. (5/77)

The precursor of the non-amyloid beta/A4 protein (non-Abeta) component of Alzheimer's disease amyloid (NACP)/alpha-synuclein is the human homologue of alpha-synuclein, a member of a protein family which includes alpha-, beta- and gamma-synuclein. This protein is thought to be involved in neuronal plasticity because of its unique expression, mainly in the telencephalon during maturation. Consequently, disarrangement of NACP/alpha-synuclein might disrupt synaptic activity, resulting in memory disturbance. Previous studies have shown that damage to synaptic terminals is closely associated with global cognitive impairment and is an early event in the pathogenesis of Alzheimer's disease. Although the relationship between synaptic damage and amyloidogenesis is not clear, some proteins at the synaptic site have been implicated in both neuronal alteration and amyloid formation. Indeed, abnormal accumulation of both NACP/alpha-synuclein and Abeta precursor protein occurs at synapses of Alzheimer's patients. Other evidence suggests that NACP/alpha-synuclein is a component of the Lewy bodies found in patients with Parkinson's disease or dementia with Lewy bodies, and that a point mutation in this protein may be the cause of familial Parkinson's disease. Consequently, abnormal transport, metabolism or function of NACP/alpha-synuclein appears to impair synaptic function, which induces, at least in part, neuronal degeneration in several neurodegenerative diseases.  (+info)

Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology. (6/77)

Neurodegeneration with brain iron accumulation, type 1 (NBIA 1), or Hallervorden-Spatz syndrome, is a rare neurodegenerative disorder characterized clinically by Parkinsonism, cognitive impairment, pseudobulbar features, as well as cerebellar ataxia, and neuropathologically by neuronal loss, gliosis, and iron deposition in the globus pallidus, red nucleus, and substantia nigra. The hallmark pathological lesions of NBIA 1 are axonal spheroids, but Lewy body (LB)-like intraneuronal inclusions, glial inclusions, and rare neurofibrillary tangles also occur. Here we show that there is an accumulation of alpha-synuclein (alphaS) in LB-like inclusions, glial inclusions, and spheroids in the brains of three NBIA 1 patients. Further, beta-synuclein (betaS) and gamma-synuclein (gammaS) immunoreactivity was detected in spheroids but not in LB-like or glial inclusions. Western blot analysis demonstrated high-molecular weight alphaS aggregates in the high-salt-soluble and Triton X-100-insoluble/sodium dodecyl sulfate-soluble fraction of the NBIA 1 brain. Significantly, the levels of alphaS were markedly reduced in the Triton X-100-soluble fractions compared to control brain, and unlike other synucleinopathies, insoluble alphaS did not accumulate in the formic acid-soluble fraction. These findings expand the concept of neurodegenerative synucleinopathies by implicating alphaS, betaS, and gammaS in the pathogenesis of NBIA 1.  (+info)

Parkinson's disease-associated alpha-synuclein is more fibrillogenic than beta- and gamma-synuclein and cannot cross-seed its homologs. (7/77)

Parkinson's disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies. Recently, two point mutations in alpha-synuclein were found to be associated with familial PD, but as of yet no mutations have been described in the homologous genes beta- and gamma-synuclein. alpha-Synuclein forms the major fibrillar component of Lewy bodies, but these do not stain for beta- or gamma-synuclein. This result is very surprising, given the extent of sequence conservation and the high similarity in expression and subcellular localization, in particular between alpha- and beta-synuclein. Here we compare in vitro fibrillogenesis of all three purified synucleins. We show that fresh solutions of alpha-, beta-, and gamma- synuclein show the same natively unfolded structure. While over time alpha-synuclein forms the previously described fibrils, no fibrils could be detected for beta- and gamma-synuclein under the same conditions. Most importantly, beta- and gamma-synuclein could not be cross-seeded with alpha-synuclein fibrils. However, under conditions that drastically accelerate aggregation, gamma-synuclein can form fibrils with a lag phase roughly three times longer than alpha-synuclein. These results indicate that beta- and gamma-synuclein are intrinsically less fibrillogenic than alpha-synuclein and cannot form mixed fibrils with alpha-synuclein, which may explain why they do not appear in the pathological hallmarks of PD, although they are closely related to alpha-synuclein and are also abundant in brain.  (+info)

Chicken synucleins: cloning and expression in the developing embryo. (8/77)

Synucleins comprise a family of small intracellular proteins that have recently attracted considerable attention because of their involvement in human diseases. Mutations of alpha-synuclein has been found in several families with hereditary early-onset Parkinson's disease and accumulation of this protein in characteristic cytoplasmic inclusions is a pathohistological hallmark of several neurodegenerative diseases that have been recently classified as 'alpha;-synucleinopathies' (reviewed in Brain Res. Bull. 50 (1999) 465; J. Neurosci. Res. 58 (1999) 120; Philos. Trans. R. Soc. Lond. Biol. Sci. 354 (1999) 1101; Brain Pathol. 9 (1999) 733). Aggregates of beta-synuclein and persyn (gamma-synuclein) also have been found in dystrophic neurites associated with Parkinson's and other neurodegenerative diseases (Proc. Natl. Acad. Sci. USA 96 (1999) 13450; and our unpublished observations). Moreover, persyn has been implicated in malignization of breast tumours (Cancer Res. 57 (1997) 759; Cancer Res. 59 (1999) 742; Hum. Mol. Genet. 7 (1998) 1417). All synucleins have distinct, although overlapping, patterns of expression in the embryonic, postnatal and adult mammalian nervous systems, suggesting important, although still not clear, biological functions in neuronal developing. Chicken embryo is a unique object for developmental studies that allows in vivo manipulations not always possible for mammalian embryos. Studies of synucleins expression in this model system could shed light on their functions in the developing nervous system. We cloned three chicken synucleins from the embryonic neural cDNA libraries and studied their expression in normal chicken embryonic tissues by Northern and in situ hybridization with specific probes. Our results demonstrate that primary structures and expression patterns of synucleins are similar in birds and mammals, suggesting that conserved function of synucleins is important for embryonic development of vertebrates.  (+info)

Gamma-synuclein is a protein that belongs to the synuclein family, which also includes alpha-synuclein and beta-synuclein. These proteins are abundantly expressed in the brain and are involved in various cellular processes such as vesicle trafficking, neurotransmitter release, and maintaining the structure of neurons.

Gamma-synuclein is primarily found in the central nervous system and is expressed at lower levels compared to alpha-synuclein. It has been identified as a component of Lewy bodies, which are intracellular inclusions found in the brains of patients with Parkinson's disease and other synucleinopathies. However, its precise role in these diseases remains unclear.

Like other synucleins, gamma-synuclein can form aggregates under certain conditions, and this property has been suggested to contribute to its pathological role in neurodegenerative disorders. Additionally, gamma-synuclein has been implicated in cancer, where it promotes tumor growth and metastasis.

Overall, further research is needed to fully understand the physiological and pathological functions of gamma-synuclein.

Synucleins are a family of small, heat-stable, water-soluble proteins that are primarily expressed in neurons. They are involved in various cellular processes such as modulating synaptic plasticity, vesicle trafficking, and neurotransmitter release. The most well-known members of this family are alpha-synuclein, beta-synuclein, and gamma-synuclein.

Abnormal accumulation and aggregation of alpha-synuclein into insoluble fibrils called Lewy bodies and Lewy neurites are hallmark features of several neurodegenerative disorders, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. These conditions are collectively referred to as synucleinopathies. The dysfunction and aggregation of alpha-synuclein are thought to contribute to the progressive loss of dopaminergic neurons in the substantia nigra pars compacta, a region of the brain involved in motor control, leading to the characteristic symptoms observed in these disorders.

Alpha-synuclein is a protein that is primarily found in neurons (nerve cells) in the brain. It is encoded by the SNCA gene and is abundantly expressed in presynaptic terminals, where it is believed to play a role in the regulation of neurotransmitter release.

In certain neurological disorders, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, alpha-synuclein can form aggregates known as Lewy bodies and Lewy neurites. These aggregates are a pathological hallmark of these diseases and are believed to contribute to the death of nerve cells, leading to the symptoms associated with these disorders.

The precise function of alpha-synuclein is not fully understood, but it is thought to be involved in various cellular processes such as maintaining the structure of the presynaptic terminal, regulating synaptic vesicle trafficking and neurotransmitter release, and protecting neurons from stress.

Beta-synuclein is a protein that is encoded by the SNCB gene in humans. It is a member of the synuclein family, which also includes alpha-synuclein and gamma-synuclein. Beta-synuclein is primarily found in the brain and is expressed at high levels in neurons.

Like alpha-synuclein, beta-synuclein has been shown to interact with lipids and play a role in the maintenance of synaptic function. However, unlike alpha-synuclein, which can form aggregates that are associated with neurodegenerative diseases such as Parkinson's disease and dementia with Lewy bodies, beta-synuclein does not appear to form aggregates under normal physiological conditions.

Some studies have suggested that beta-synuclein may play a protective role in the brain by inhibiting the aggregation of alpha-synuclein. However, other studies have suggested that beta-synuclein may contribute to neurodegeneration in certain contexts, such as in the presence of mutations or under conditions of cellular stress.

Overall, while the exact functions and regulatory mechanisms of beta-synuclein are still being elucidated, it is clear that this protein plays important roles in neuronal function and may have implications for neurodegenerative diseases.

Parkinson's disease is a progressive neurodegenerative disorder that affects movement. It is characterized by the death of dopamine-producing cells in the brain, specifically in an area called the substantia nigra. The loss of these cells leads to a decrease in dopamine levels, which results in the motor symptoms associated with Parkinson's disease. These symptoms can include tremors at rest, stiffness or rigidity of the limbs and trunk, bradykinesia (slowness of movement), and postural instability (impaired balance and coordination). In addition to these motor symptoms, non-motor symptoms such as cognitive impairment, depression, anxiety, and sleep disturbances are also common in people with Parkinson's disease. The exact cause of Parkinson's disease is unknown, but it is thought to be a combination of genetic and environmental factors. There is currently no cure for Parkinson's disease, but medications and therapies can help manage the symptoms and improve quality of life.

Protein D-aspartate-L-isoaspartate methyltransferase (PCMT or PRMT5) is an enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to the side chain nitrogen atom of a specific aspartate or glutamate residue on protein substrates. This enzyme plays a crucial role in the maintenance of protein structure and function by correcting the spontaneous deamidation of asparagine and isomerization of aspartate to isoaspartate residues, which can lead to protein aggregation and loss of function. PCMT also regulates various cellular processes, including transcription, RNA processing, DNA damage repair, and signal transduction, by modifying the activity or localization of its target proteins.

Lewy bodies are abnormal aggregates of alpha-synuclein protein that develop in nerve cells (neurons) in the brain. They are named after Frederick Lewy, a German-American neurologist who discovered them while working with Dr. Alois Alzheimer. The presence of Lewy bodies is a hallmark feature of Lewy body dementia, which includes both Parkinson's disease dementia and dementia with Lewy bodies.

Lewy bodies can lead to the dysfunction and death of neurons in areas of the brain that control movement, cognition, and behavior. This can result in a range of symptoms, including motor impairments, cognitive decline, visual hallucinations, and mood changes. The exact role of Lewy bodies in the development and progression of these disorders is not fully understood, but they are believed to contribute to the neurodegenerative process that underlies these conditions.

Nerve tissue proteins are specialized proteins found in the nervous system that provide structural and functional support to nerve cells, also known as neurons. These proteins include:

1. Neurofilaments: These are type IV intermediate filaments that provide structural support to neurons and help maintain their shape and size. They are composed of three subunits - NFL (light), NFM (medium), and NFH (heavy).

2. Neuronal Cytoskeletal Proteins: These include tubulins, actins, and spectrins that provide structural support to the neuronal cytoskeleton and help maintain its integrity.

3. Neurotransmitter Receptors: These are specialized proteins located on the postsynaptic membrane of neurons that bind neurotransmitters released by presynaptic neurons, triggering a response in the target cell.

4. Ion Channels: These are transmembrane proteins that regulate the flow of ions across the neuronal membrane and play a crucial role in generating and transmitting electrical signals in neurons.

5. Signaling Proteins: These include enzymes, receptors, and adaptor proteins that mediate intracellular signaling pathways involved in neuronal development, differentiation, survival, and death.

6. Adhesion Proteins: These are cell surface proteins that mediate cell-cell and cell-matrix interactions, playing a crucial role in the formation and maintenance of neural circuits.

7. Extracellular Matrix Proteins: These include proteoglycans, laminins, and collagens that provide structural support to nerve tissue and regulate neuronal migration, differentiation, and survival.

Parkinsonian disorders are a group of neurological conditions characterized by motor symptoms such as bradykinesia (slowness of movement), rigidity, resting tremor, and postural instability. These symptoms are caused by the degeneration of dopamine-producing neurons in the brain, particularly in the substantia nigra pars compacta.

The most common Parkinsonian disorder is Parkinson's disease (PD), which is a progressive neurodegenerative disorder. However, there are also several other secondary Parkinsonian disorders, including:

1. Drug-induced parkinsonism: This is caused by the use of certain medications, such as antipsychotics and metoclopramide.
2. Vascular parkinsonism: This is caused by small vessel disease in the brain, which can lead to similar symptoms as PD.
3. Dementia with Lewy bodies (DLB): This is a type of dementia that shares some features with PD, such as the presence of alpha-synuclein protein clumps called Lewy bodies.
4. Progressive supranuclear palsy (PSP): This is a rare brain disorder that affects movement, gait, and eye movements.
5. Multiple system atrophy (MSA): This is a progressive neurodegenerative disorder that affects multiple systems in the body, including the autonomic nervous system, motor system, and cerebellum.
6. Corticobasal degeneration (CBD): This is a rare neurological disorder that affects both movement and cognition.

It's important to note that while these disorders share some symptoms with PD, they have different underlying causes and may require different treatments.

Impulse Control Disorders (ICDs) are a group of psychiatric conditions characterized by the failure to resist an impulse, drive, or temptation to perform an act that is harmful to oneself or others. This leads to negative consequences such as distress, anxiety, or disruption in social, occupational, or other important areas of functioning.

The Diagnostic and Statistical Manual of Mental Disorders, 5th Edition (DSM-5) recognizes several specific ICDs, including:

1. Kleptomania - the recurrent failure to resist impulses to steal items, even though they are not needed for personal use or financial gain.
2. Pyromania - the deliberate and purposeful fire-setting on more than one occasion.
3. Intermittent Explosive Disorder - recurrent behavioral outbursts representing a failure to control aggressive impulses, resulting in serious assaultive acts or destruction of property.
4. Pathological Gambling - persistent and recurrent maladaptive gambling behavior that disrupts personal, family, or vocational pursuits.
5. Internet Gaming Disorder - the excessive and prolonged use of the internet for gaming, which leads to clinically significant impairment or distress.

These disorders are typically associated with a range of emotional, cognitive, and behavioral symptoms that can vary depending on the specific disorder and individual presentation. Treatment often involves a combination of psychotherapy, medication, and self-help strategies to manage symptoms and improve overall functioning.

Neurodegenerative diseases are a group of disorders characterized by progressive and persistent loss of neuronal structure and function, often leading to cognitive decline, functional impairment, and ultimately death. These conditions are associated with the accumulation of abnormal protein aggregates, mitochondrial dysfunction, oxidative stress, chronic inflammation, and genetic mutations in the brain. Examples of neurodegenerative diseases include Alzheimer's disease, Parkinson's disease, Huntington's disease, Amyotrophic Lateral Sclerosis (ALS), and Spinal Muscular Atrophy (SMA). The underlying causes and mechanisms of these diseases are not fully understood, and there is currently no cure for most neurodegenerative disorders. Treatment typically focuses on managing symptoms and slowing disease progression.

Dopamine is a type of neurotransmitter, which is a chemical messenger that transmits signals in the brain and nervous system. It plays several important roles in the body, including:

* Regulation of movement and coordination
* Modulation of mood and motivation
* Control of the reward and pleasure centers of the brain
* Regulation of muscle tone
* Involvement in memory and attention

Dopamine is produced in several areas of the brain, including the substantia nigra and the ventral tegmental area. It is released by neurons (nerve cells) and binds to specific receptors on other neurons, where it can either excite or inhibit their activity.

Abnormalities in dopamine signaling have been implicated in several neurological and psychiatric conditions, including Parkinson's disease, schizophrenia, and addiction.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

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Bai XC, Yan C, Yang G, Lu P, Ma D, Sun L, Zhou R, Scheres SH, Shi Y (2015). "An atomic structure of human gamma-secretase". ... Alpha-synuclein from Multiple system atrophy and TMEM106B. Scheres has been a member of the Board of Reviewing Editors for ... For example, Xiaochen Bai, currently at UTSW, in his group solved the structure of human Gamma secretase in a collaboration ... "Structures of alpha-synuclein filaments from multiple system atrophy". Nature. 585 (7825): 464-469. Bibcode:2020Natur.585..464S ...
Sharma N, Brandis KA, Herrera SK, Johnson BE, Vaidya T, Shrestha R, Debburman SK (2006). "alpha-Synuclein budding yeast model: ... The expression of the 11S particle is induced by interferon gamma and is responsible, in conjunction with the immunoproteasome ... interferon gamma. The proteasome assembled with these alternative subunits is known as the immunoproteasome, whose substrate ... whose expression is induced by interferon gamma, are the primary producers of peptides which are optimal in size and ...
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Kawahara K, Hashimoto M, Bar-On P, Ho GJ, Crews L, Mizuno H, Rockenstein E, Imam SZ, Masliah E (March 2008). "alpha-Synuclein ... Zhang Z, Zhang R (March 2008). "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation". The ...
Synuclein Mice (with Silke Nuber PhD, Alice Y. Nam BS, Molly M. Rajsombath BS, Haley Cirka Xiaoping Hronowski PhD, Junmin Wang ... he and co-workers identified presenilin as a component of the long-sought-after gamma-secretase, one of the enzymes involved in ... Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies (with John B ...
Ashkar AA, Di Santo JP, Croy BA (July 2000). "Interferon gamma contributes to initiation of uterine vascular modification, ... levels of Natural killer cells are elevated as they degrade alpha-synuclein aggregates, destroy senescent neurons, and ... Depletion of the inflammatory cytokine interferon gamma reversed the effect.[citation needed] Tumor-infiltrating NK cells have ... FC-gamma-RIII = CD16), an activating biochemical receptor that binds the Fc portion of IgG class antibodies. This allows NK ...
This protein is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial ... "Endonuclease G mediates α-synuclein cytotoxicity during Parkinson's disease". The EMBO Journal. 32 (23): 3041-54. doi:10.1038/ ...
Jin YH, Kim YJ, Kim DW, Baek KH, Kang BY, Yeo CY, Lee KY (Apr 2008). "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates ... "Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease". Science. 317 (5837): 516-19. ...
When this gene family is compared to cytochrome C, a slow evolving gene, and fibrinogen gamma chain, a fast evolving gene it is ... and alpha-synuclein". J. Biol. Chem. (39th ed.). 286 (39): 34088-34100. doi:10.1074/jbc.m111.243907. PMC 3190826. PMID 21832049 ...
Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the ... Payton JE, Perrin RJ, Clayton DF, George JM (November 2001). "Protein-protein interactions of alpha-synuclein in brain ... major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There ...
Waking is usually characterized by beta (12-30 Hz) and gamma (25-100 Hz) depending on whether there was a peaceful or stressful ... mainly when they are characterized by abnormal accumulation of alpha-synuclein, such as multiple system atrophy (MSA), ... Hughes JR (July 2008). "Gamma, fast, and ultrafast waves of the brain: their relationships with epilepsy and behavior". ... low amplitude activity and spontaneous occurrence of beta and gamma waves. The best candidates for generation of these fast ...
miR-7 and miR-153 act to reduce alpha-synuclein levels (a hallmark of PD) but are reduced in PD brain. DNA methylation Neurons ... For instance, the differential expression of lncRNA interferon gamma antisense RNA negatively regulates the expression of HLA- ... Histone marks alpha-synuclein, the protein encoded by SNCA, can associate with histones and prevent their acetylation in ... Hallmarks include mutations to the alpha-synuclein gene, SNCA, as well as PARK2, PINK1, UCHL1, DJ1, and LRRK2 genes, and ...
Suh YH; Checler F (September 2002). "Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and ... by gamma secretase (γ-secretase), an enzyme complex within the membrane. The sequential actions of these secretases results in ...
Gamma-synuclein is a protein that in humans is encoded by the SNCG gene. Synuclein-gamma is a member of the synuclein family of ... Gamma-synuclein is the least conserved of the synuclein proteins. Gamma-Synucleins expression in breast tumors is a marker for ... The normal cellular function of gamma-synuclein remains unknown. Gamma-synuclein has been shown to interact with BUB1B. ... Gamma-synuclein is a synuclein protein found primarily in the peripheral nervous system (in primary sensory neurons, ...
BETA- AND GAMMA-SYNUCLEINS MODULATE SYNAPTIC VESICLE-BINDING OF ALPHA-SYNUCLEIN. Kathryn E. Carnazza, View ORCID ProfileLauren ... BETA- AND GAMMA-SYNUCLEINS MODULATE SYNAPTIC VESICLE-BINDING OF ALPHA-SYNUCLEIN Message Subject (Your Name) has forwarded a ...
"α-Synuclein (αS) has been well-documented to play a role in human synucleinopathies such as Parkinsons disease (PD) and ... and gamma-synuclein is invariably associated with inclusion formation and toxicity Tae-Eun Kim 1 , Andrew J Newman 1 , Thibaut ... and gamma-synuclein is invariably associated with inclusion formation and toxicity Tae-Eun Kim et al. Hum Mol Genet. 2021. . ... 1998) Absence of mutation in the beta- and gamma-synuclein genes in familial autosomal dominant Parkinsons disease. DNA Res. ...
Recombinant Human SRPK1 GST (N-Term) Protein. Backed by our 100% Guarantee.
synuclein, gamma. involved_in. IBA. PMID:21873635. GO_Central. PMID:21873635. RGD:13792537. NCBI chr16:9,700,513...9,705,751 ... actin, gamma 1. involved_in. ISO. (MGI:6189485,PMID:27840001). RGD. PMID:27840001. MGI:6189485. NCBI chr10:105,619,738... ... synuclein, beta. involved_in. IBA. ISO. PMID:21873635. (MGI:5605098,PMID:25009269). RGD. PMID:25009269 PMID:21873635. MGI: ... synuclein alpha. involved_in. IBA. ISO. PMID:21873635. (MGI:3850310,PMID:18980610), (MGI:5605098,PMID:25009269). RGD. PMID: ...
Cited in 1 publications. View Mouse Monoclonal anti-TAF15 Antibody (4D71) (NBP1-92685). Validated Applications: WB, ICC/IF, IHC. Validated Species: Human, Mouse, Rat. Sample size available. Range of directly conjugated antibodies available.
Surgucheva, I. G., Sivak, J. M., Fini, M. E., Palazzo, R. E., and Surguchov, A. P. (2003). Effect of gamma-synuclein ... 2019). Class II transactivator (CIITA) mediates IFN-gamma induced eNOS repression by enlisting SUV39H1. Biochim. Biophys. Acta ...
BBSRC Project Grant: "Delineating the regulation and function of gamma-synuclein in adipocyte lipid metabolism". PI: JJ ...
... and α-synuclein (α-Syn of Parkinsons disease) form large fibrils. Evidence is increasing however that much smaller oligomers ... gamma-Synuclein / metabolism* Actions. * Search in PubMed * Search in MeSH * Add to Search ... Here we extend that hypothesis to the superfamily of α, β, and γ-synucleins. Our models of numerous synuclein oligomers, ... Non-Amyloid-β Component of Human α-Synuclein Oligomers Induces Formation of New Aβ Oligomers: Insight into the Mechanisms That ...
2. Synuclein-gamma is closely involved in perineural invasion and distant metastasis in mouse models and is a novel prognostic ... Overexpression of synuclein-gamma in pancreatic adenocarcinoma.. Li Z; Sclabas GM; Peng B; Hess KR; Abbruzzese JL; Evans DB; ...
3. Alternative splicing of synuclein gamma in endometrial cancer: identification of a novel isoform. Schaal K, Hirschfeld M, ...
Gamma-synuclein is an adipocyte-neuron gene coordinately expressed with leptin and increased in human obesity. J Nutr 138(5): ... 2010). Interestingly, the levels of α-synuclein are also relevant to obesity, as increased α-synuclein is reportedly consistent ... Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat ... alpha-Synuclein locus triplication causes Parkinsons disease. Science 302(5646):841. 14593171. . Crossref, Medline, Google ...
Flotillin and gamma-synuclein, proteins which interact with myocilin, were expressed in all samples [41,42]. Rab8 (ras-related ... Surgucheva I, Park BC, Yue BY, Tomarev S, Surguchov A. Interaction of myocilin with gamma-synuclein affects its secretion and ...
Increased striatal dopamine release and hyperdopaminergic-like behaviour in mice lacking both alpha-synuclein and gamma- ... SNCA-OVX mice are devoid of mouse α-synuclein but overexpress human wild-type α-synuclein at disease-relevant levels and show ... mice that express Cre recombinase in DA neurons and the human α-synuclein transgene and are mouse α-synuclein-null; and (2) ... We made this line optogenetic-capable by crossing with Slc6a3IRES-Cre mice which were mouse α-synuclein-null (Slc6a3IRES-Cre+/+ ...
... and gamma-synuclein: implications for fibrillation. Protein Sci. 15, 2795-2804 (2006). ...
The gamma chain subunit of Fc receptors is required for alpha-synuclein-induced pro-inflammatory signaling in microglia. ... IFN-gamma signaling in the central nervous system controls the course of experimental autoimmune encephalomyelitis ...
Synuclein_Gamma,modify,28-APR-06,(null),(null) C30081,T-Cell_Leukemia_Lymphoma_1B_Protein,modify,28-APR-06,(null),(null) C30082 ...
The research work relates to the use of small molecule modulators of human brain gamma-synuclein protein involved in ...
... gamma-Synuclein D12.776.641.860.750 D12.776.631.860.750 gamma-Tocopherol D3.438.150.909.750.500 D3.633.100.150.909.750.500 ... gamma-Lipotropin D12.776.641.650.405.935.518 D12.776.631.650.405.935.518 gamma-MSH D12.776.641.650.405.935.524 D12.776.631.650. ... gamma-Chain T-Cell Antigen Receptor G5.355.330.801.311 G5.344.801.311 G12.425.742.530.311 G12.500.287.311 G12.500.349.530.311 ... alpha-Synuclein D12.776.641.860.500 D12.776.631.860.500 D12.776.637.500 alpha-Tocopherol D3.438.150.909.750.249 D3.633.100.150. ...
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gamma-Synuclein Preferred Concept UI. M0159752. Registry Number. 0. Scope Note. A homolog of ALPHA-SYNUCLEIN that plays a role ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.. Terms. gamma- ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.. Entry Term(s). Persyn ... 2006; GAMMA-SYNUCLEIN was indexed under NERVE TISSUE PROTEINS 1988-2005. History Note. 2006(1988). Date Established. 2006/01/01 ...
gamma-Synuclein Preferred Concept UI. M0159752. Registry Number. 0. Scope Note. A homolog of ALPHA-SYNUCLEIN that plays a role ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.. Terms. gamma- ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.. Entry Term(s). Persyn ... 2006; GAMMA-SYNUCLEIN was indexed under NERVE TISSUE PROTEINS 1988-2005. History Note. 2006(1988). Date Established. 2006/01/01 ...
Description: A sandwich ELISA kit for detection of Synuclein Gamma from Human in samples from blood, serum, plasma, cell ... ELISA kit for Human Gamma-glutamylcysteine synthetase (Gamma-GCS). KTE62527-5platesof96wells Abbkine 5 plates of 96 wells. 2538 ... Human SYNRg(Synergin Gamma) ELISA Kit. Human SYNRg(Synergin Gamma) ELISA Kit. To Order Contact us: michael@lotusbiotechnologies ... Description: A sandwich quantitative ELISA assay kit for detection of Human Synuclein Gamma (SNCg) in samples from serum, ...
Association of alpha-, beta-, and gamma-Synuclein with diffuse lewy body disease. Archives of neurology 2010 Aug 67 (8): 970-5 ... Beta-synuclein gene variants and Parkinsons disease: a preliminary case-control study. Neuroscience letters 2007 Jun 420 (3): ... INDEL Length and Haplotypes in the ?-Synuclein Gene: A Key to Differentiate Dementia with Lewy Bodies? Journal of Alzheimers ...
Human Gamma-Synuclein (breast cancer-specific gene 1) is a soluble protein belonging to the synuclein family. This protein is ... Gamma-Synuclein is also associated with axonal pathology in Parkinsons desease and others neurodegenerative disordes. ... Product Sheet: Rabbit anti-Human Gamma- Synuclein IgG fraction polyclonal antibody. *Catalog # PN-7020a-9 ... 127 of human gamma-synuclein. The IgG fraction was purified using Protein G-Sepharose. ...
gamma-Synuclein - Preferred Concept UI. M0159752. Scope note. A homolog of ALPHA-SYNUCLEIN that plays a role in neurofilament ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1. ... Gamma-Synuclein may also activate SIGNAL TRANSDUCTION PATHWAYS associated with ETS-DOMAIN PROTEIN ELK-1.. ... gamma-sinucleína Scope note:. Homólogo de la ALFA-SINUCLEÍNA que interviene en la integridad de la red de neurofilamentos. Se ...
Gamma-synuclein Protein. S22-30CH. Human. HIS. E.coli. Full Length. NM_003087. ... Alpha Synuclein (A53T) Pre-Formed Fibrils (Type 1). S22-361N. Human. TAG-Free. E.coli. Full Length. NP_000336.1. ... Alpha Synuclein Pre-Formed Fibril (Type 1). S22-381N. Human. TAG-Free. E.coli. Full Length. NP_000336.1. ... Alpha Synuclein Pre-Formed Fibril (Type 1). S22M-381N. Mouse. TAG-Free. E.coli. Full Length. NP_001035916.1. ...
synuclein gamma [Source:HGNC Sym.... SOD2. 6648. SOD2. superoxide dismutase 2 [Source:H.... ...
The aim of the current study was to investigate DNA cloning and the expression of alpha-Synuclein protein in E. coli. Materials ... Identifying the structure and function of alpha-Synuclein protein can lead to the development of appropriate treatments for ... Identification, localization and characterization of the human gamma-synuclein gene. Hum Genet. 1998;103(1):106-12. [Link] [DOI ... Most of alpha-Synuclein expressed from the pET28a-alpha-Synuclein plasmid accumulated in the bacteria as incorporated objects. ...

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