Vesicular Acetylcholine Transport Proteins
Acetylcholine
Choline O-Acetyltransferase
Membrane Transport Proteins
Vesicular Biogenic Amine Transport Proteins
Vesicular Transport Proteins
Neuromuscular Depolarizing Agents
Carrier Proteins
Vesicular Monoamine Transport Proteins
Neuromuscular Junction Diseases
PC12 Cells
Receptors, Cholinergic
Fatty Acid Transport Proteins
Synaptophysin
Synaptic Vesicles
Distribution of cholinergic contacts on Renshaw cells in the rat spinal cord: a light microscopic study. (1/181)
1. Cholinergic terminals in the rat spinal cord were revealed by immunohistochemical detection of the vesicular acetycholine transporter (VAChT). In order to determine the relationships of these terminals to Renshaw cells, we used dual immunolabelling with antibodies against gephyrin or calbindin D28k to provide immunohistochemical identification of Renshaw cells in lamina VII of the ventral horn. 2. A total of 50 Renshaw cells were analysed quantitatively using a computer-aided reconstruction system to provide accurate localization of contact sites and determination of somatic and dendritic surface area. Dendrites could be traced for up to 413 microm from the soma in calbindin D28k-identified Renshaw cells and up to 184 microm in gephyrin-identified cells. 3. A total of 3330 cholinergic terminals were observed on 50 Renshaw cells, with a range of 21-138 terminal appositions per cell (mean 66.6 +/- 25.56 contacts per cell). The vast majority (83.5 %) of the terminals were apposed to dendrites rather than the soma. The overall density of cholinergic contacts increased from a little above 1 per 100 microm2 on the soma and initial 25 microm of proximal dendrites to 4-5 per 100 microm2 on the surface of dendritic segments located 50-250 microm from the soma. Single presynaptic fibres frequently formed multiple contacts with the soma and/or dendrites of individual Renshaw cells. 4. VAChT-immunoreactive terminals apposed to Renshaw cells varied in size from 0.6 to 6.9 microm in diameter (mean 2.26 +/- 0.94; n = 986) and were on average smaller than the cholinergic C-terminals apposed to motoneurones, but larger than VAChT-immunoreactive terminals contacting other ventral horn interneurones. 5. The high density and relatively large size of many cholinergic terminals on Renshaw cells presumably correlates with the strong synaptic connection between motoneurones and Renshaw cells. The fact that the majority of contacts are distributed over the dendrites makes the motoneurone axon collateral input susceptible to inhibition by the prominent glycinergic inhibitory synapses located on the soma and proximal dendrites. The relative positions and structural features of the excitatory cholinergic and inhibitory glycinergic synapses may explain why Renshaw cells, although capable of firing at very high frequency following motor axon stimulation, appear to fire at relatively low rates during locomotor activity. (+info)A nerve growth factor mimetic TrkA antagonist causes withdrawal of cortical cholinergic boutons in the adult rat. (2/181)
Cholinergic neurons respond to the administration of nerve growth factor (NGF) in vivo with a prominent and selective increase of choline acetyl transferase activity. This suggests the possible involvement of endogenous NGF, acting through its receptor TrkA, in the maintenance of central nervous system cholinergic synapses in the adult rat brain. To test this hypothesis, a small peptide, C(92-96), that blocks NGF-TrkA interactions was delivered stereotactically into the rat cortex over a 2-week period, and its effect and potency were compared with those of an anti-NGF monoclonal antibody (mAb NGF30). Two presynaptic antigenic sites were studied by immunoreactivity, and the number of presynaptic sites was counted by using an image analysis system. Synaptophysin was used as a marker for overall cortical synapses, and the vesicular acetylcholine transporter was used as a marker for cortical cholinergic presynaptic sites. No significant variations in the number of synaptophysin-immunoreactive sites were observed. However, both mAb NGF30 and the TrkA antagonist C(92-96) provoked a significant decrease in the number and size of vesicular acetylcholine transporter-IR sites, with the losses being more marked in the C(92-96) treated rats. These observations support the notion that endogenously produced NGF acting through TrkA receptors is involved in the maintenance of the cholinergic phenotype in the normal, adult rat brain and supports the idea that NGF normally plays a role in the continual remodeling of neural circuits during adulthood. The development of neurotrophin mimetics with antagonistic and eventually agonist action may contribute to therapeutic strategies for central nervous system degeneration and trauma. (+info)Empty synaptic vesicles recycle and undergo exocytosis at vesamicol-treated motor nerve terminals. (3/181)
We investigated whether recycled cholinergic synaptic vesicles, which were not refilled with ACh, would join other synaptic vesicles in the readily releasable store near active zones, dock, and continue to undergo exocytosis during prolonged stimulation. Snake nerve-muscle preparations were treated with 5 microM vesamicol to inhibit the vesicular ACh transporter and then were exposed to an elevated potassium solution, 35 mM potassium propionate (35 KP), to release all preformed quanta of ACh. At vesamicol-treated endplates, miniature endplate current (MEPC) frequency increased initially from 0.4 to >300 s-1 in 35 KP but then declined to <1 s-1 by 90 min. The decrease in frequency was not accompanied by a decrease in MEPC average amplitude. Nerve terminals accumulated the activity-dependent dye FM1-43 when exposed to the dye for the final 6 min of a 120-min exposure to 35 KP. Thus synaptic membrane endocytosis continued at a high rate, although MEPCs occurred infrequently. After a 120-min exposure in 35 KP, nerve terminals accumulated FM1-43 and then destained, confirming that exocytosis also still occurred at a high rate. These results demonstrate that recycled cholinergic synaptic vesicles that were not refilled with ACh continued to dock and undergo exocytosis after membrane retrieval. Thus transport of ACh into recycled cholinergic vesicles is not a requirement for repeated cycles of exocytosis and retrieval of synaptic vesicle membrane during prolonged stimulation of motor nerve terminals. (+info)NO synthase in cholinergic nerves and NO-induced relaxation in the rat isolated corpus cavernosum. (4/181)
1. In the rat corpus cavernosum (CC), the distribution of immunoreactivity for neuronal and endothelial NO synthase (nNOS and eNOS), and the pattern of NOS-immunoreactive (-IR) nerves in relation to some other nerve populations, were investigated. Cholinergic nerves were specifically immunolabelled with antibodies to the vesicular acetylcholine transporter protein (VAChT). 2. In the smooth muscle septa surrounding the cavernous spaces, and around the central and helicine arteries, the numbers of PGP- and tyrosine hydroxylase (TH)-IR terminals were large, whereas neuropeptide Y (NPY)-, VAChT-, nNOS-, and vasoactive intestinal polypeptide (VIP)-IR terminals were found in few to moderate numbers. 3. Double immunolabelling revealed that VAChT- and nNOS-IR terminals, VAChT- and VIP-IR terminals, nNOS-IR and VIP-IR terminals, and TH- and NPY-IR terminals showed coinciding profiles, and co-existence was verified by confocal laser scanning microscopy. TH immunoreactivity was not found in VAChT-, nNOS-, or VIP-IR nerve fibres or terminals. 4. An isolated strip preparation of the rat CC was developed, and characterized. In this preparation, cumulative addition of NO to noradrenaline (NA)-contracted strips, produced concentration-dependent, rapid, and almost complete relaxations. Electrical field stimulation of endothelin-1-contracted preparations produced frequency-dependent responses: a contractile twitch followed by a fast relaxant response. After cessation of stimulation, there was a slow relaxant phase. Inhibition of NO synthesis, or blockade of guanylate cyclase, abolished the first relaxant phase, whereas the second relaxation was unaffected. 5. The results suggest that in the rat CC, nNOS, VAChT- and VIP-immunoreactivities can be found in the same parasympathetic cholinergic neurons. Inhibitory neurotransmission involves activation of the NO-system, and the release of other, as yet unknown, transmitters. (+info)Activation of TrkA by nerve growth factor upregulates expression of the cholinergic gene locus but attenuates the response to ciliary neurotrophic growth factor. (5/181)
Nerve growth factor (NGF) stimulates the expression of the cholinergic gene locus, which encodes choline acetyltransferase (ChAT) and vesicular acetylcholine transporter (VAChT), the proteins necessary for the synthesis and storage of the neurotransmitter acetylcholine (ACh). To determine whether this action of NGF is mediated by the p140TrkA NGF receptor (a member of the Trk tyrosine kinase family) we used a murine basal forebrain cholinergic cell line, SN56, stably transfected with rat trkA cDNA. Treatment of these transfectants with NGF activated mitogen-activated protein kinase and increased cytosolic free calcium concentrations, confirming the reconstitution of TrkA-mediated signalling pathways. The expression of ChAT and VAChT mRNA, as well as ACh content, were coordinately up-regulated by NGF in SN56-trkA transfectants. None of these responses occurred in the parental SN56 cells, which do not express endogenous TrkA, indicating that these actions of NGF required TrkA. We previously reported that ciliary neurotrophic factor (CNTF) upregulates the expression of ChAT and VAChT, as well as ACh production, in SN56 cells. The combined treatment of SN56-trkA cells with CNTF and NGF revealed a complex interaction of these factors in the regulation of cholinergic gene locus expression. At low concentrations of CNTF (<1 ng/ml), the upregulation of ACh synthesis evoked by these factors was additive. However, at higher concentrations of CNTF (>1 ng/ml), NGF attenuated the stimulatory effect of CNTF on ChAT and VAChT mRNA and ACh content. This attenuation was not due to interference with early steps of CNTF receptor signalling, as pre-treatment of SN56-trkA cells with NGF did not affect the nuclear translocation of the transcription factor, Stat3, evoked by CNTF. (+info)The Phox2 homeodomain proteins are sufficient to promote the development of sympathetic neurons. (6/181)
The development of sympathetic neurons is controlled by a network of transcriptional regulators, including the paired homeodomain proteins Phox2a and Phox2b. To understand the role of Phox2 proteins in more detail, the effect of Phox2 overexpression was analysed in the avian peripheral nervous system. Phox2a expression in neural crest cultures elicited a strong increase in the number of sympathoadrenergic cells. Expression of Phox2a in the chick embryo promoted the generation of additional neurons expressing the noradrenergic marker genes DBH and TH, pan-neuronal genes SCG10 and NF160 and cholinergic genes ChAT and VAChT. Phox2a-induced neurons were found in ectopic locations such as dorsal root ganglia and peripheral nerve. Sympathoadrenergic development could be elicited in cultures of E5 dorsal root ganglia, demonstrating the presence of Phox2a-responsive cells in non-autonomic peripheral ganglia. Phox2b induced ectopic neurons in the chick embryo in the same way as Phox2a. These results show that Phox2 proteins are sufficient to promote sympathetic neuron generation and control, directly or indirectly, the expression of a large number of genes characteristic for sympathetic neurons. (+info)Protein kinase A regulates cholinergic gene expression in PC12 cells: REST4 silences the silencing activity of neuron-restrictive silencer factor/REST. (7/181)
The role of protein kinase A in regulating transcription of the cholinergic gene locus, which contains both the vesicular acetylcholine transporter gene and the choline acetyltransferase gene, was investigated in PC12 cells and a protein kinase A-deficient PC12 mutant, A126.1B2, in which transcription of the gene is reduced. The site of action of protein kinase A was localized to a neuron-restrictive silencer element/repressor element 1 (NRSE/RE-1) sequence within the cholinergic gene. Neuron-restrictive silencer factor (NRSF)/RE-1-silencing transcription factor (REST), the transcription factor which binds to NRSE/RE-1, was expressed at similar levels in both PC12 and A126.1B2 cells. Although nuclear extracts containing NRSF/REST from A126.1B2 exhibited binding to NRSE/RE-1, nuclear extracts from PC12 cells did not. The NRSF/REST isoform REST4 was expressed in PC12 cells but not in A126.1B2. REST4 inhibited binding of NRSF/REST to NRSE/RE-1 as determined by gel mobility shift assays. Coimmunoprecipitation was used to demonstrate interaction between NRSF/REST and REST4. Expression of recombinant REST4 in A126.1B2 was sufficient to transcriptionally activate the cholinergic gene locus. Thus, in PC12 cells, protein kinase A promotes the production of REST4, which inhibits repression of the cholinergic gene locus by NRSF/REST. (+info)Vitamin D3-induced proliferative lesions in the rat adrenal medulla. (8/181)
Adrenal medullary hyperplasia and pheochromocytomas are induced in rats by a variety of non-genotoxic agents, and we have hypothesized that these agents induce lesions indirectly by stimulating chromaffin cell proliferation. Vitamin D3, which has not been previously associated with adrenal medullary proliferative lesions, is the most potent in vivo stimulus to chromaffin cell proliferation yet identified. The present investigation utilized the vitamin D3 model to prospectively test the relationship between mitogenicity and focal proliferative lesions in the adrenal medulla and to determine early events in the pathogenesis of these lesions. Charles River Crl:CD BR rats were treated with 0; 5000; 10,000; or 20,000 IU/kg/day of vitamin D3 in corn oil (5 ml/kg) by oral intubation. Rats were killed after 4, 8, 12, or 26 weeks of treatment, following a final week of labeling with bromodeoxyuridine (BrdU) using a mini-pump. Adrenal sections were double-stained for BrdU and phenylethanolamine-N-methyl transferase (PNMT) to discriminate epinephrine (E) from norepinephrine (NE) cells or for vesicular acetylcholine transporter (VAchT) to identify cholinergic nerve endings. Vitamin D3 caused a 4-5-fold increase in BrdU labeling at week 4, diminishing to a 2-fold increase by week 26. An initial preponderance of labeled E cells gave way to a preponderance of labeled NE cells. By week 26, 17/19 (89%) animals receiving the 2 highest doses of vitamin D3 had focal adrenal medullary proliferative lesions, in contrast to an absence of lesions in control rats. The lesions encompassed a spectrum including BrdU-labeled "hot spots" not readily visible on H and E sections, hyperplastic nodules, and pheochromocytomas. Lesions were usually multicentric, bilateral, and peripheral in location, and almost all were PNMT-negative. The lesions were not cholinergically innervated, suggesting autonomous proliferation. Hot spots, hyperplastic nodules, and pheochromocytomas appear to represent a continuum rather than separate entities. Their development might involve selective responses of chromaffin cell subsets to mitogenic signals, influenced by both innervation and corticomedullary interactions. A number of non-genotoxic compounds that induce pheochromocytomas in rats are known to affect calcium homeostasis. The results of this study provide further evidence to support the hypothesis that altered calcium homeostasis is indirectly involved in the pathogenesis of pheochromocytomas, via effects on chromaffin cell proliferation. (+info)Vesicular Acetylcholine Transport Proteins (VAChT) are specialized integral membrane proteins that play a crucial role in the storage and release of the neurotransmitter acetylcholine (ACh) within synaptic vesicles. These transport proteins are located in the membranes of synaptic vesicles, which are small, membrane-bound organelles found in nerve terminals.
VAChT is responsible for actively transporting ACh from the cytosol (the fluid inside the cell) into these synaptic vesicles. The protein uses the energy derived from the hydrolysis of ATP to move ACh against its concentration gradient, accumulating it within the vesicles to high concentrations. This allows for the efficient and rapid release of ACh into the synapse upon stimulation of the nerve terminal, facilitating neurotransmission between neurons.
Defects in VAChT function or expression have been implicated in several neurological disorders, including certain forms of epilepsy and mental retardation, highlighting its importance in maintaining normal neural communication.
Acetylcholine is a neurotransmitter, a type of chemical messenger that transmits signals across a chemical synapse from one neuron (nerve cell) to another "target" neuron, muscle cell, or gland cell. It is involved in both peripheral and central nervous system functions.
In the peripheral nervous system, acetylcholine acts as a neurotransmitter at the neuromuscular junction, where it transmits signals from motor neurons to activate muscles. Acetylcholine also acts as a neurotransmitter in the autonomic nervous system, where it is involved in both the sympathetic and parasympathetic systems.
In the central nervous system, acetylcholine plays a role in learning, memory, attention, and arousal. Disruptions in cholinergic neurotransmission have been implicated in several neurological disorders, including Alzheimer's disease, Parkinson's disease, and myasthenia gravis.
Acetylcholine is synthesized from choline and acetyl-CoA by the enzyme choline acetyltransferase and is stored in vesicles at the presynaptic terminal of the neuron. When a nerve impulse arrives, the vesicles fuse with the presynaptic membrane, releasing acetylcholine into the synapse. The acetylcholine then binds to receptors on the postsynaptic membrane, triggering a response in the target cell. Acetylcholine is subsequently degraded by the enzyme acetylcholinesterase, which terminates its action and allows for signal transduction to be repeated.
Choline O-Acetyltransferase (COAT, ChAT) is an enzyme that plays a crucial role in the synthesis of the neurotransmitter acetylcholine. It catalyzes the transfer of an acetyl group from acetyl CoA to choline, resulting in the formation of acetylcholine. Acetylcholine is a vital neurotransmitter involved in various physiological processes such as memory, cognition, and muscle contraction. COAT is primarily located in cholinergic neurons, which are nerve cells that use acetylcholine to transmit signals to other neurons or muscles. Inhibition of ChAT can lead to a decrease in acetylcholine levels and may contribute to neurological disorders such as Alzheimer's disease and myasthenia gravis.
Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.
Vesicular biogenic amine transport proteins (VMATs) are a type of transmembrane protein that play a crucial role in the packaging and transport of biogenic amines, such as serotonin, dopamine, norepinephrine, and histamine, into synaptic vesicles within neurons. These proteins are located on the membranes of neurosecretory vesicles and function to regulate the concentration of these neurotransmitters in the cytoplasm and maintain their storage in vesicles until they are released into the synapse during neurotransmission. VMATs are members of the solute carrier family 18 (SLC18) and consist of two isoforms, VMAT1 and VMAT2, which differ in their distribution and substrate specificity. VMAT1 is primarily found in non-neuronal cells, such as endocrine and neuroendocrine cells, while VMAT2 is predominantly expressed in neurons. Dysregulation of VMATs has been implicated in several neurological and psychiatric disorders, including Parkinson's disease, depression, and attention deficit hyperactivity disorder (ADHD).
Vesicular transport proteins are specialized proteins that play a crucial role in the intracellular trafficking and transportation of various biomolecules, such as proteins and lipids, within eukaryotic cells. These proteins facilitate the formation, movement, and fusion of membrane-bound vesicles, which are small, spherical structures that carry cargo between different cellular compartments or organelles.
There are several types of vesicular transport proteins involved in this process:
1. Coat Proteins (COPs): These proteins form a coat around the vesicle membrane and help shape it into its spherical form during the budding process. They also participate in selecting and sorting cargo for transportation. Two main types of COPs exist: COPI, which is involved in transport between the Golgi apparatus and the endoplasmic reticulum (ER), and COPII, which mediates transport from the ER to the Golgi apparatus.
2. SNARE Proteins: These proteins are responsible for the specific recognition and docking of vesicles with their target membranes. They form complexes that bring the vesicle and target membranes close together, allowing for fusion and the release of cargo into the target organelle. There are two types of SNARE proteins: v-SNAREs (vesicle SNAREs) and t-SNAREs (target SNAREs), which interact to form a stable complex during membrane fusion.
3. Rab GTPases: These proteins act as molecular switches that regulate the recruitment of coat proteins, motor proteins, and SNAREs during vesicle transport. They cycle between an active GTP-bound state and an inactive GDP-bound state, controlling the various stages of vesicular trafficking, such as budding, transport, tethering, and fusion.
4. Tethering Proteins: These proteins help to bridge the gap between vesicles and their target membranes before SNARE-mediated fusion occurs. They play a role in ensuring specificity during vesicle docking and may also contribute to regulating the timing of membrane fusion events.
5. Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNAREs): These proteins are involved in intracellular transport, particularly in the trafficking of vesicles between organelles. They consist of a family of coiled-coil domain-containing proteins that form complexes to mediate membrane fusion events.
Overall, these various classes of proteins work together to ensure the specificity and efficiency of vesicular transport in eukaryotic cells. Dysregulation or mutation of these proteins can lead to various diseases, including neurodegenerative disorders and cancer.
Cholinergic fibers are nerve cell extensions (neurons) that release the neurotransmitter acetylcholine at their synapses, which are the junctions where they transmit signals to other neurons or effector cells such as muscles and glands. These fibers are a part of the cholinergic system, which plays crucial roles in various physiological processes including learning and memory, attention, arousal, sleep, and muscle contraction.
Cholinergic fibers can be found in both the central nervous system (CNS) and the peripheral nervous system (PNS). In the CNS, cholinergic neurons are primarily located in the basal forebrain and brainstem, and their projections innervate various regions of the cerebral cortex, hippocampus, thalamus, and other brain areas. In the PNS, cholinergic fibers are responsible for activating skeletal muscles through neuromuscular junctions, as well as regulating functions in smooth muscles, cardiac muscles, and glands via the autonomic nervous system.
Dysfunction of the cholinergic system has been implicated in several neurological disorders, such as Alzheimer's disease, Parkinson's disease, and myasthenia gravis.
Piperidines are not a medical term per se, but they are a class of organic compounds that have important applications in the pharmaceutical industry. Medically relevant piperidines include various drugs such as some antihistamines, antidepressants, and muscle relaxants.
A piperidine is a heterocyclic amine with a six-membered ring containing five carbon atoms and one nitrogen atom. The structure can be described as a cyclic secondary amine. Piperidines are found in some natural alkaloids, such as those derived from the pepper plant (Piper nigrum), which gives piperidines their name.
In a medical context, it is more common to encounter specific drugs that belong to the class of piperidines rather than the term itself.
Neuromuscular depolarizing agents are a type of muscle relaxant used in anesthesia and critical care medicine. These drugs work by causing depolarization of the post-synaptic membrane at the neuromuscular junction, which is the site where nerve impulses are transmitted to muscles. This results in the binding of the drug to the receptor and the activation of ion channels, leading to muscle contraction.
The most commonly used depolarizing agent is suxamethonium (also known as succinylcholine), which has a rapid onset and short duration of action. It is often used during rapid sequence intubation, where there is a need for immediate muscle relaxation to facilitate endotracheal intubation.
However, the use of depolarizing agents can also lead to several side effects, including increased potassium levels in the blood (hyperkalemia), muscle fasciculations, and an increase in intracranial and intraocular pressure. Therefore, these drugs should be used with caution and only under the close supervision of a trained healthcare provider.
Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).
Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.
Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.
Cholinergic neurons are specialized types of nerve cells (neurons) that release the neurotransmitter acetylcholine to transmit signals to other neurons or effector cells, such as muscle cells. These neurons play important roles in various physiological functions, including modulation of motor control, cognition, memory, arousal, and sensory perception. Cholinergic neurons are widely distributed throughout the nervous system, with significant concentrations found in the basal forebrain, brainstem, and spinal cord. Dysfunction or degeneration of cholinergic neurons has been implicated in several neurological disorders, such as Alzheimer's disease, Parkinson's disease, and various forms of dementia.
Vesicular Monoamine Transporter Proteins (VMATs) are a type of transmembrane protein that play a crucial role in the packaging and transport of monoamines, such as serotonin, dopamine, and norepinephrine, into synaptic vesicles within neurons. There are two main isoforms of VMATs, VMAT1 and VMAT2, which differ in their distribution and function.
VMAT1 (also known as SLC18A1) is primarily found in neuroendocrine cells and is responsible for transporting monoamines into large dense-core vesicles. VMAT2 (also known as SLC18A2), on the other hand, is mainly expressed in presynaptic neurons and is involved in the transport of monoamines into small synaptic vesicles.
Both VMAT1 and VMAT2 are integral membrane proteins that utilize a proton gradient to drive the uptake of monoamines against their concentration gradient, allowing for their storage and subsequent release during neurotransmission. Dysregulation of VMAT function has been implicated in several neurological and psychiatric disorders, including Parkinson's disease and depression.
Neuromuscular junction diseases are a group of disorders that affect the functioning of the neuromuscular junction, which is the site where nerve impulses are transmitted to muscles. These diseases are characterized by muscle weakness and fatigue, and can be caused by various factors such as autoimmune disorders, genetic mutations, or toxins.
Examples of neuromuscular junction diseases include myasthenia gravis, Lambert-Eaton myasthenic syndrome (LEMS), congenital myasthenic syndromes (CMS), and botulism. Myasthenia gravis is an autoimmune disorder that causes the immune system to attack the receptors in the neuromuscular junction, leading to muscle weakness and fatigue. LEMS is a rare autoimmune disorder that affects the nerve endings at the neuromuscular junction, causing muscle weakness and decreased reflexes.
Congenital myasthenic syndromes are genetic disorders that affect the functioning of the neuromuscular junction from birth, leading to muscle weakness and fatigue. Botulism is a rare but serious condition caused by the ingestion of botulinum toxin, which can lead to paralysis of the muscles due to interference with nerve impulse transmission at the neuromuscular junction.
Treatment for neuromuscular junction diseases may include medications such as cholinesterase inhibitors, immunosuppressive drugs, or plasma exchange therapy, depending on the specific diagnosis and severity of the condition.
PC12 cells are a type of rat pheochromocytoma cell line, which are commonly used in scientific research. Pheochromocytomas are tumors that develop from the chromaffin cells of the adrenal gland, and PC12 cells are a subtype of these cells.
PC12 cells have several characteristics that make them useful for research purposes. They can be grown in culture and can be differentiated into a neuron-like phenotype when treated with nerve growth factor (NGF). This makes them a popular choice for studies involving neuroscience, neurotoxicity, and neurodegenerative disorders.
PC12 cells are also known to express various neurotransmitter receptors, ion channels, and other proteins that are relevant to neuronal function, making them useful for studying the mechanisms of drug action and toxicity. Additionally, PC12 cells can be used to study the regulation of cell growth and differentiation, as well as the molecular basis of cancer.
Cholinergic receptors are a type of receptor in the body that are activated by the neurotransmitter acetylcholine. Acetylcholine is a chemical that nerve cells use to communicate with each other and with muscles. There are two main types of cholinergic receptors: muscarinic and nicotinic.
Muscarinic receptors are found in the heart, smooth muscle, glands, and the central nervous system. They are activated by muscarine, a type of alkaloid found in certain mushrooms. When muscarinic receptors are activated, they can cause changes in heart rate, blood pressure, and other bodily functions.
Nicotinic receptors are found in the nervous system and at the junction between nerves and muscles (the neuromuscular junction). They are activated by nicotine, a type of alkaloid found in tobacco plants. When nicotinic receptors are activated, they can cause the release of neurotransmitters and the contraction of muscles.
Cholinergic receptors play an important role in many physiological processes, including learning, memory, and movement. They are also targets for drugs used to treat a variety of medical conditions, such as Alzheimer's disease, Parkinson's disease, and myasthenia gravis (a disorder that causes muscle weakness).
Fatty acid transport proteins (FATPs) are a group of membrane-bound proteins that play a crucial role in the uptake and transport of long-chain fatty acids across the plasma membrane of cells. They are widely expressed in various tissues, including the heart, muscle, adipose tissue, and liver.
FATPs have several domains that enable them to perform their functions, including a cytoplasmic domain that binds to fatty acids, a transmembrane domain that spans the plasma membrane, and an ATP-binding cassette (ABC) domain that hydrolyzes ATP to provide energy for fatty acid transport.
FATPs also play a role in the regulation of intracellular lipid metabolism by modulating the activity of enzymes involved in fatty acid activation, desaturation, and elongation. Mutations in FATP genes have been associated with various metabolic disorders, including congenital deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), a rare autosomal recessive disorder that affects fatty acid oxidation.
In summary, fatty acid transport proteins are essential for the uptake and metabolism of long-chain fatty acids in cells and have implications in various metabolic disorders.
Synaptophysin is a protein found in the presynaptic vesicles of neurons, which are involved in the release of neurotransmitters during synaptic transmission. It is often used as a marker for neuronal differentiation and is widely expressed in neuroendocrine cells and tumors. Synaptophysin plays a role in the regulation of neurotransmitter release and has been implicated in various neurological disorders, including Alzheimer's disease and synaptic dysfunction-related conditions.
Synaptic vesicles are tiny membrane-enclosed sacs within the presynaptic terminal of a neuron, containing neurotransmitters. They play a crucial role in the process of neurotransmission, which is the transmission of signals between nerve cells. When an action potential reaches the presynaptic terminal, it triggers the fusion of synaptic vesicles with the plasma membrane, releasing neurotransmitters into the synaptic cleft. These neurotransmitters can then bind to receptors on the postsynaptic neuron and trigger a response. After release, synaptic vesicles are recycled through endocytosis, allowing them to be refilled with neurotransmitters and used again in subsequent rounds of neurotransmission.
Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.
Passive transport does not require the input of energy and includes:
1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.
Active transport requires the input of energy (in the form of ATP) and includes:
1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.
Vesicular monoamine transporter
Vesicular monoamine transporter 1
Choline transporter
Solute carrier family
Synaptic vesicle
Vesicular acetylcholine transporter
Amino acid transporter
SLC22A2
History of catecholamine research
Neurotoxin
Reuptake inhibitor
Neurotransmitter transporter
List of MeSH codes (D12.776.157)
List of MeSH codes (D12.776.543)
Norepinephrine
Taipoxin
Cell signaling
Neurotransmission
Soluble NSF attachment protein
Vesicular monoamine transporter 2
End-plate potential
SLC22A3
Cocaine intoxication
BBSome
Index of biology articles
ARF1
Adrenaline
Latrotoxin
Choline acetyltransferase
Adderall
Vesicular monoamine transporter - Wikipedia
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Unique age-related transcriptional signature in the nervous system of the long-lived red sea urchin Mesocentrotus franciscanus ...
Transporter12
- The vesicular monoamine transporter (VMAT) is a transport protein integrated into the membranes of synaptic vesicles of presynaptic neurons. (wikipedia.org)
- The first H+ efflux generates a transporter conformation associated with a high-affinity amine-binding site in the cytosolic phase, and the second H+ efflux is coupled with a second large conformational change that leads to amine transport from the cytosolic side into the vesicle, reducing amine-binding affinity. (wikipedia.org)
- Purpose: The vesicular acetylcholine transporter (VAChT) is a specific biomarker for imaging presynaptic cholinergic neurons. (wustl.edu)
- The genes encoding choline acetyltransferase (ChAT) and its vesicular transporter (VAChT), CHAT and SLC18A3 respectively, map to the linked region of chromosome 10 and are therefore both positional and obvious functional candidate genes for late-onset AD. (ox.ac.uk)
- Vesicular acetylcholine transporter (VaCht), or Solute Carrier Family 18 Member A3 is encoded by the gene Slc18a3 and is a member of the vesicular amine transporter family. (antibodiesinc.com)
- Mesembrine also boosts the activity of vesicular monoamine transporter 2, or VMAT2. (grass-routes.org)
- In rats, double-labeling immunocytochemistry revealed that combinations of fibers immunoreactive for substance P (SP) and dopamine-beta-hydroxylase (DbetaH), SP and vesicular acetylcholine transporter (VAChT), as well as DbetaH and VAChT occurred only around blood vessels in the lower dermis. (ulaval.ca)
- Allele-specific suppression in Caenorhabditis elegans reveals details of EMS mutagenesis and a possible moonlighting interaction between the vesicular acetylcholine transporter and ERD2 receptors. (ouhsc.edu)
- The mammalian vesicular glutamate transporter VGLUT2 and Drosophila ortholog dVGLUT have been implicated as modulators of DA neuron resilience. (umassmed.edu)
- Moreover, we show that overexpression of the vesicular acetylcholine transporter (VAChT), which mediates the packaging of acetylcholine into synaptic vesicles for exocytotic release, causes a reduction in lifespan and a decline in ACh-linked behaviors during aging. (unito.it)
- The dopamine transporter ( DAT ) also ( sodium-dependent dopamine transporter ) is a membrane-spanning protein coded for in the human by the SLC6A3 gene , (also known as DAT1 ), that pumps the neurotransmitter dopamine out of the synaptic cleft back into cytosol . (cloudfront.net)
- Studies using electrophysiology and radioactive-labeled dopamine have confirmed that the dopamine transporter is similar to other monoamine transporters in that one molecule of neurotransmitter can be transported across the membrane with one or two sodium ions. (cloudfront.net)
VAChT1
- VaCht transports acetylcholine into secretory vesicles for release into the extracellular space. (antibodiesinc.com)
Presynaptic1
- Our lab focuses on the molecular events that govern vesicular trafficking within presynaptic nerve terminals and neurosecretory cells. (edu.au)
Receptors3
- Many G protein-coupled receptors have a relatively high affinity for their peptide and monoamine ligands, but the small amounts of ligand that actually impinge on receptors are not likely to saturate binding. (johnshopkins.edu)
- The research focuses on the cellular and molecular mechanisms of desensitization of hormone response mediated by the activation of G protein-coupled receptors (GPCR). (cas.cz)
- G protein-coupled receptors are plasma membrane integral proteins that serve as transducers of extracellular signals across the plasma membrane bilayer to the cell interior. (cas.cz)
Secretory vesicles1
- This novel trafficking/chaperoning pathway underpins neurotransmission, as secretory vesicles rely on the zippering of SNARE proteins such as syntaxin-1 to undergo fusion with the plasma membrane. (edu.au)
Mammalian1
- 100% sequence homology with Mouse, Rat, Canine, Equine and all other mammalian proteins examined. (novusbio.com)
Beta-amyloid1
- What these failed trials do suggest, however, is that compounds whose mechanism of action is to solely target the beta-amyloid protein, and hence which can be considered to be "classical approaches" ( Masters and Beyreuther, 2006 ), may not represent the optimal approach to the treatment of AD. (frontiersin.org)
Amine1
- Studies indicate that the amino acid residue His419, located on the domain between TMDs X and XI of rat VMAT1, plays a role in energy coupling to the amine transport by assisting the first proton-dependent conformational change. (wikipedia.org)
Glutamate1
- It has been less clear whether changes in vesicle filling with classical transmitters such as acetylcholine, GABA and glutamate make a difference in the postsynaptic response. (johnshopkins.edu)
Intracellular5
- Two well-defined pathological hallmarks of AD have been described: the formation of extracellular amyloid plaques and the development of intracellular neurofibrillary tangles (NFTs) formed by aggregated hyperphosphorylated TAU protein [ 4 ]. (biomedcentral.com)
- For successful transgene expression, viruses administered into muscle must undergo a series of processes, including host cell interaction and internalization, intracellular sorting, long-range retrograde axonal transport, endosomal liberation, and nuclear import. (frontiersin.org)
- Metal chaperones (or metallochaperones) are compounds that function to shuttle metal ions to specific intracellular target proteins. (frontiersin.org)
- Importins, molecular motors and RNA binding proteins function in a bidirectional mechanism of intracellular communication, consisting of anterograde RNA transport, local translation at axon tips, and retrograde transport of the resulting proteins, for neuron length sensing and growth control. (unito.it)
- Once dopamine binds, the protein undergoes a conformational change, which allows both sodium and dopamine to unbind on the intracellular side of the membrane. (cloudfront.net)
Metabolism2
- Age-related gene expression profiles of the short-lived model animals Caenorhabditis elegans and Drosophila melanogaster share a common adult-onset expression program of genes involved in mitochondrial metabolism, DNA repair, catabolism, peptidolysis and cellular transport 3 . (nature.com)
- MRS and immunoblotting techniques were used to measure the neurochemical metabolism levels and cholinergic-related proteins, respectively. (biomedcentral.com)
Cholinergic2
- In this study, we demonstrate that BoNT/A is transported to facial motoneurons, released, and internalized preferentially into cholinergic terminals impinging onto the motoneurons. (jneurosci.org)
- The aim of the project is to determine how disruption of cholinergic activation of striatal GABAergic interneurons alters striatal signalling and striatum-based behaviour by using a mouse model with deletion of the β2 nicotinic acetylcholine receptor subunit in striatal GABAergic interneurons. (cas.cz)
Neurotransmitters3
- It transports monoamine neurotransmitters - such as dopamine, serotonin, norepinephrine, epinephrine, and histamine - into the vesicles, which release the neurotransmitters into synapses as chemical messages to postsynaptic neurons. (wikipedia.org)
- Vesicle packing requires a large energy source to store large quantities of neurotransmitters into a small vesicular space at high concentrations. (wikipedia.org)
- This protein helps transport various neurotransmitters out of cells to have an effect on the brain and body. (grass-routes.org)
Concentrations1
- At the same time, vesicular transport is generally slow, and may limit refilling if vesicles recycle quickly, even at concentrations of cytosolic transmitter that saturate the transport mechanism. (johnshopkins.edu)
Precursor protein4
- Additionally, we detected increased levels of active glycogen synthase kinase 3 β, a physiological kinase of TAU, in neurons derived from AD iPSCs, as well as significant upregulation of amyloid precursor protein (APP) synthesis and APP carboxy-terminal fragment cleavage. (biomedcentral.com)
- Most cases of early-onset AD are linked to autosomal dominant inherited mutations in the genes encoding amyloid precursor protein ( APP ), presenilin 1 ( PSEN1 ), and presenilin 2 ( PSEN2 ). (biomedcentral.com)
- Secreted amyloid-ß precursor protein functions as a GABABR1a ligand to modulate synaptic transmission. (ouhsc.edu)
- BDNF cDNA encodes a 247 amino acid residue precursor protein with a signal peptide and a proprotein that are cleaved to yield the 119 amino acid residue mature BDNF. (novusbio.com)
Encodes2
- chb-3 encodes a novel protein, with a zf-MYND motif and ankyrin repeats, that is highly conserved from worm to human. (stanford.edu)
- The gene that encodes the DAT protein is located on chromosome 5 , consists of 15 coding exons , and is roughly 64 kbp long. (cloudfront.net)
Pathogenesis1
- the majority of which target one or both of the primary aggregating proteins implicated in the pathogenesis of AD. (frontiersin.org)
Plasma membrane1
- We demonstrated that the protein Munc18-1 was responsible for the transport of syntaxin-1 to the plasma membrane. (edu.au)
Extracellular1
- For this purpose, WIN 55,212-2 was injected in pregnant wistar rats from gestation day 5 to 20 and a detailed analysis of the levels of the neurotrophin brain-derived neurotrophic factor (BDNF) as well as of the signaling molecules extracellular signal-regulated kinase (ERK)1/2 and alpha-calcium/calmodulin-dependent protein kinase II (alpha-CaMKII) was carried out in adult offspring. (researchgate.net)
Release2
- It is important to note that the mechanism of vesicular release poses several inherent problems. (johnshopkins.edu)
- It is generally accepted to consider this contact only as a specialized morpho-functional structure, where chemical transmission (via release of the acetylcholine (ACh)) of electrical signal from motor neuron to muscle fiber occurs, ultimately causing the muscle to contract. (intechopen.com)
Hyperphosphorylation1
- To our knowledge, this is the first study in which the hyperphosphorylation of TAU protein has been compared in fAD and sAD iPSC-derived neurons. (biomedcentral.com)
Mechanism3
- VMATs use the same transport mechanism for all types of monoamines, and transport them from the cytosol into high-concentration storage vesicles. (wikipedia.org)
- Transgenic Mice Overexpressing Serum Retinol-Binding Protein Develop Progressive Retinal Degeneration through a Retinoid-Independent Mechanism. (ouhsc.edu)
- The adaptor protein GULP promotes Jedi-1-mediated phagocytosis through a clathrin-dependent mechanism. (academictree.org)
Aggregation1
- Neuroinflammation and oxidative stress, mitochondrial dysfunction, dysregulation of the expression of histone deacetylases, and aggregation of pathogenic forms of proteins are among the most common and significant pathological features of neurodegenerative diseases. (actanaturae.ru)
Deletion1
- Deletion of DJ-1 in rats affects protein abundance and mitochondrial function at the synapse. (ouhsc.edu)
Sodium3
- These studies have also shown that transport rate and direction is totally dependent on the sodium gradient. (cloudfront.net)
- Because of the tight coupling of the membrane potential and the sodium gradient, activity-induced changes in membrane polarity can dramatically influence transport rates. (cloudfront.net)
- Lyophilized from a 0.2 μm filtered solution in Sodium Citrate and NaCl with BSA as a carrier protein. (novusbio.com)
Neurons2
- Transport vesicles are released into the space between neurons, called the synaptic cleft, where they convey a chemical message to the next neuron. (wikipedia.org)
- Neurons from patients with fAD and patients with sAD showed increased phosphorylation of TAU protein at all investigated phosphorylation sites. (biomedcentral.com)
Integral1
- DAT is an integral membrane protein that removes dopamine from the synaptic cleft and deposits it into surrounding cells, thus terminating the signal of the neurotransmitter. (cloudfront.net)
Function6
- There was also an upregulation in expression of positive regulators and key components of the AMPK pathway, autophagy, proteasome function, and the unfolded protein response. (nature.com)
- This facilitation of metal transport is distinct from metal chelators or buffers, which function to exclude or deplete metals from discrete cellular compartments to thereby limit biological interactions of key metal ions. (frontiersin.org)
- Engulfment of cellular material and proteins is a key function for microglia, a resident macrophage of the central nervous system (CNS). (umassmed.edu)
- DAT function requires the sequential binding and co-transport of two Na + ions and one Cl − ion with the dopamine substrate. (cloudfront.net)
- The integrity of hydrophobic lipid environment of PM is an important factor affecting function of membrane proteins. (cas.cz)
- This indicates that current intake (and RDA) values for vitamin K are too low to support proper function of extra-hepatic Gla-proteins. (vitamindwiki.com)
Synaptic transmission2
- Hearing depends on faithful synaptic transmission at the inner hair cell (IHC) ribbon synapse, which is orchestrated by active zone proteins. (uni-goettingen.de)
- BoNT/A acts by cleaving synaptosomal-associated protein of 25 kDa (SNAP-25) at the neuromuscular junction, thus blocking synaptic transmission and weakening overactive muscles. (jneurosci.org)
Synapse1
- Synapse-Assembly Proteins Maintain Synaptic Vesicle Cluster Stability and Regulate Synaptic Vesicle Transport in Caenorhabditis elegans. (ouhsc.edu)
Cleavage1
- It blocks neurotransmission via the specific cleavage of the synaptic protein SNAP-25 (synaptosomal-associated protein of 25 kDa). (jneurosci.org)
Affinity1
- Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography and conjugation of purified mAb. (antibodiesinc.com)
Amino1
- In mammals, the charm of L-arginine occurs through a one's own flesh of cationic amino acid transporters known as CATs (cationic amino acid transporters), the properties of which earmarks of that of the y + amino acid transport system. (fosite.ru)
Nuclear1
- We also found that postnatal γ-MNs are also distinguished by low expression of the neuronal nuclear protein (NeuN). (biomedcentral.com)
Complex1
- Using Argonaute CLIP-seq data, Dr. Rigoutsos and colleagues showed that similar percentages of the two sets of microRNAs were in complex with Argonaute proteins. (pharmaceuticalintelligence.com)
Plays a role1
- It also slows the breakdown of acetylcholine, which plays a role in memory and learning. (grass-routes.org)
Molecular Weight1
- Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. (novusbio.com)
Family1
- The neurotrophin family is comprised of at least four proteins including NGF, BDNF, NT-3, and NT-4/5. (novusbio.com)
Small1
- Previous analyses suggest that lack of normal cilia causes the small-body phenotype through the activation of a signaling pathway which consists of the EGL-4 cGMP-dependent protein kinase and the GCY-12 receptor-type guanylyl cyclase. (stanford.edu)
Biological7
- This is particularly evident in disorders such as Alzheimer's disease (AD), where the use of metal chaperones (that transport metals), as opposed to chelators (which exclude metals from biological interactions), may prove to be the first truly disease modifying approach for this condition. (frontiersin.org)
- Or to be more precise, at least some portions of non-protein-coding DNA are thought to serve important biological functions. (pharmaceuticalintelligence.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human G Protein Coupled Estrogen Receptor 1 (GPER) in serum, plasma, tissue homogenates and other biological fluids. (allelisakits.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human G Protein Coupled Estrogen Receptor 1 (GPER) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (allelisakits.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Tumor Protein, Translationally Controlled 1 (TPT1) in tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (allelisakits.com)
- Description: A competitive ELISA for quantitative measurement of Human Translationally controlled tumor protein(TPT1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (allelisakits.com)
- The biological part of this project will involve making transgenic mice with test non-coding DNA linked to reporter constructs such as green fluorescent protein (GFP). (edu.au)
Cells1
- Each new lot of antibody is quality control tested on cells overexpressing target protein and confirmed to give the expected staining pattern. (antibodiesinc.com)
Human1
- One of the unexpected findings of the Human Genome Project was that over 98% of the human genome does not encode for proteins. (pharmaceuticalintelligence.com)
Show1
- Here, we show that catalytically active BoNT/A is transported to the facial nucleus (FN) after injection into the nasolabial musculature of rats and mice. (jneurosci.org)
Target1
- Many drugs that target VMATs act as inhibitors and alter the kinetics of the protein. (wikipedia.org)
Memory1
- However, the internal relationships between the acetylcholine (Ach) cycle and memory decline during the early stages of AD currently remain unknown. (biomedcentral.com)