Synaptophysin
Synaptic Vesicles
Vesicle-Associated Membrane Protein 2
Synaptogyrins
Chromogranins
Carcinoma, Neuroendocrine
Synapsins
Chromogranin A
Nerve Tissue Proteins
Immunohistochemistry
R-SNARE Proteins
Synapses
Phosphopyruvate Hydratase
Neurosecretory Systems
Membrane Proteins
Neurons
GAP-43 Protein
Neurocytoma
Hippocampus
Carcinoid Tumor
Dimethyl Suberimidate
Synaptotagmins
Presynaptic Terminals
Vesicular Glutamate Transport Proteins
Neuroendocrine Cells
Paraganglioma, Extra-Adrenal
Organelles
Nerve terminal damage by beta-bungarotoxin: its clinical significance. (1/724)
We report here original data on the biological basis of prolonged neuromuscular paralysis caused by the toxic phospholipase A2 beta-bungarotoxin. Electron microscopy and immunocytochemical labeling with anti-synaptophysin and anti-neurofilament have been used to show that the early onset of paralysis is associated with the depletion of synaptic vesicles from the motor nerve terminals of skeletal muscle and that this is followed by the destruction of the motor nerve terminal and the degeneration of the cytoskeleton of the intramuscular axons. The postjunctional architecture of the junctions were unaffected and the binding of fluorescein-isothiocyanate-conjugated alpha-bungarotoxin to acetylcholine receptor was not apparently affected by exposure to beta-bungarotoxin. The re-innervation of the muscle fiber was associated by extensive pre- and post-terminal sprouting at 3 to 5 days but was stable by 7 days. Extensive collateral innervation of adjacent muscle fibers was a significant feature of the re-innervated neuromuscular junctions. These findings suggest that the prolonged and severe paralysis seen in victims of envenoming bites by kraits (elapid snakes of the genus Bungarus) and other related snakes of the family Elapidae is caused by the depletion of synaptic vesicles from motor nerve terminals and the degeneration of the motor nerve terminal and intramuscular axons. (+info)A neomorphic syntaxin mutation blocks volatile-anesthetic action in Caenorhabditis elegans. (2/724)
The molecular mechanisms underlying general anesthesia are unknown. For volatile general anesthetics (VAs), indirect evidence for both lipid and protein targets has been found. However, no in vivo data have implicated clearly any particular lipid or protein in the control of sensitivity to clinical concentrations of VAs. Genetics provides one approach toward identifying these mechanisms, but genes strongly regulating sensitivity to clinical concentrations of VAs have not been identified. By screening existing mutants of the nematode Caenorhabditis elegans, we found that a mutation in the neuronal syntaxin gene dominantly conferred resistance to the VAs isoflurane and halothane. By contrast, other mutations in syntaxin and in the syntaxin-binding proteins synaptobrevin and SNAP-25 produced VA hypersensitivity. The syntaxin allelic variation was striking, particularly for isoflurane, where a 33-fold range of sensitivities was seen. Both the resistant and hypersensitive mutations decrease synaptic transmission; thus, the indirect effect of reducing neurotransmission does not explain the VA resistance. As assessed by pharmacological criteria, halothane and isoflurane themselves reduced cholinergic transmission, and the presynaptic anesthetic effect was blocked by the resistant syntaxin mutation. A single gene mutation conferring high-level resistance to VAs is inconsistent with nonspecific membrane-perturbation theories of anesthesia. The genetic and pharmacological data suggest that the resistant syntaxin mutant directly blocks VA binding to or efficacy against presynaptic targets that mediate anesthetic behavioral effects. Syntaxin and syntaxin-binding proteins are candidate anesthetic targets. (+info)The synaptophysin-synaptobrevin complex: a hallmark of synaptic vesicle maturation. (3/724)
Exocytosis of synaptic vesicles requires the formation of a fusion complex consisting of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein, or VAMP) and the plasma membrane proteins syntaxin and soluble synaptosomal-associated protein of 25 kDa (or SNAP 25). In search of mechanisms that regulate the assembly of the fusion complex, it was found that synaptobrevin also binds to the vesicle protein synaptophysin and that synaptophysin-bound synaptobrevin cannot enter the fusion complex. Using a combination of immunoprecipitation, cross-linking, and in vitro interaction experiments, we report here that the synaptophysin-synaptobrevin complex is upregulated during neuronal development. In embryonic rat brain, the complex is not detectable, although synaptophysin and synaptobrevin are expressed and are localized to the same nerve terminals and to the same pool of vesicles. In contrast, the ability of synaptobrevin to participate in the fusion complex is detectable as early as embryonic day 14. The binding of synaptoporin, a closely related homolog of synaptophysin, to synaptobrevin changes in a similar manner during development. Recombinant synaptobrevin binds to synaptophysin derived from adult brain extracts but not to that derived from embryonic brain extracts. Furthermore, the soluble cytosol fraction of adult, but not of embryonic, synaptosomes contains a protein that induces synaptophysin-synaptobrevin complex formation in embryonic vesicle fractions. We conclude that complex formation is regulated during development and is mediated by a posttranslational modification of synaptophysin. Furthermore, we propose that the synaptophysin-synaptobrevin complex is not essential for exocytosis but rather provides a reserve pool of synaptobrevin for exocytosis that can be readily recruited during periods of high synaptic activity. (+info)A nerve growth factor mimetic TrkA antagonist causes withdrawal of cortical cholinergic boutons in the adult rat. (4/724)
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)A case of synchronous double primary lung cancer with neuroendocrine features. (5/724)
We report a case of unique double primary lung cancers with neuroendocrine features in a 63-year-old male smoker. The mass in the left lower lobe (LLL) was a small cell/large cell carcinoma with spindle cell sarcomatous areas and organoid structure. The mass in the left upper lobe (LUL) was a tubular adenocarcinoma with neuroendocrine features including organoid nests showing occasional rosette formation, nuclear palisading in the periphery of the nests and positive immunoreaction for CD56, chromogranin A and synaptophysin. The difference in histological structures between the two masses led us to diagnose double primary lung cancer. The combination of small cell lung carcinoma and spindle cell carcinoma is very uncommon. The relationship between LLL and LUL tumors remains unclear. Multiple lung cancers with neuroendocrine features have only rarely been reported in the literature. The patient in our case died of widespread cancer 2 years and 4 months after the surgery without adjuvant chemotherapy, a longer postoperative survival time than in cases of ordinary extensive small cell lung cancer. Multiple lung cancers with neuroendocrine features are extremely rare and similar cases have not been reported in the literature. Neuroendocrine differentiation has attracted widespread attention and, therefore, examining neuroendocrine features in lung cancers is important. (+info)Expression of human apolipoprotein E3 or E4 in the brains of Apoe-/- mice: isoform-specific effects on neurodegeneration. (6/724)
Apolipoprotein (apo) E isoforms are key determinants of susceptibility to Alzheimer's disease. The apoE4 isoform is the major known genetic risk factor for this disease and is also associated with poor outcome after acute head trauma or stroke. To test the hypothesis that apoE3, but not apoE4, protects against age-related and excitotoxin-induced neurodegeneration, we analyzed apoE knockout (Apoe-/-) mice expressing similar levels of human apoE3 or apoE4 in the brain under control of the neuron-specific enolase promoter. Neuronal apoE expression was widespread in the brains of these mice. Kainic acid-challenged wild-type or Apoe-/- mice had a significant loss of synaptophysin-positive presynaptic terminals and microtubule-associated protein 2-positive neuronal dendrites in the neocortex and hippocampus, and a disruption of neurofilament-positive axons in the hippocampus. Expression of apoE3, but not of apoE4, protected against this excitotoxin-induced neuronal damage. ApoE3, but not apoE4, also protected against the age-dependent neurodegeneration seen in Apoe-/- mice. These differences in the effects of apoE isoforms on neuronal integrity may relate to the increased risk of Alzheimer's disease and to the poor outcome after head trauma and stroke associated with apoE4 in humans. (+info)Impairments in high-frequency transmission, synaptic vesicle docking, and synaptic protein distribution in the hippocampus of BDNF knockout mice. (7/724)
Brain-derived neurotrophic factor (BDNF) promotes long-term potentiation (LTP) at hippocampal CA1 synapses by a presynaptic enhancement of synaptic transmission during high-frequency stimulation (HFS). Here we have investigated the mechanisms of BDNF action using two lines of BDNF knockout mice. Among other presynaptic impairments, the mutant mice exhibited more pronounced synaptic fatigue at CA1 synapses during high-frequency stimulation, compared with wild-type animals. Quantitative analysis of CA1 synapses revealed a significant reduction in the number of vesicles docked at presynaptic active zones in the mutant mice. Synaptosomes prepared from the mutant hippocampus exhibited a marked decrease in the levels of synaptophysin as well as synaptobrevin [vesicle-associated membrane protein (VAMP-2)], a protein known to be involved in vesicle docking and fusion. Treatment of the mutant slices with BDNF reversed the electrophysiological and biochemical deficits in the hippocampal synapses. Taken together, these results suggest a novel role for BDNF in the mobilization and/or docking of synaptic vesicles to presynaptic active zones. (+info)Immunolocalization of mitsugumin29 in developing skeletal muscle and effects of the protein expressed in amphibian embryonic cells. (8/724)
The temporal appearance and subcellular distribution of mitsugumin29 (MG29), a 29-kDa transmembrane protein isolated from the triad junction in skeletal muscle, were examined by immunohistochemistry during the development of rabbit skeletal muscle. MG29 appeared in the sarcoplasmic reticulum (SR) in muscle cells at fetal day 15 before the onset of transverse tubule (T tubule) formation. In muscle cells at fetal day 27, in which T tubule and triad formation is ongoing, both SR and triad were labeled for MG29. In muscle cells at newborn 1 day, the labeling of the SR had become weak and the triads were well developed and clearly labeled for MG29. Specific and clear labeling for MG29 was restricted to the triads in adult skeletal muscle cells. When MG29 was expressed in amphibian embryonic cells by injection of the cRNA, a large quantity of tubular smooth-surfaced endoplasmic reticulum (sER) was formed in the cytoplasm. The tubular sER was 20-40 nm in diameter and appeared straight or reticular in shape. The tubular sER was formed by the fusion of coated vesicles [budded off from the rough-surfaced endoplasmic reticulum (rER)] and vacuoles of rER origin. The present results suggest that MG29 may play important roles both in the formation of the SR and the construction of the triads during the early development of skeletal muscle cells. (+info)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.
Vesicle-Associated Membrane Protein 2 (VAMP-2), also known as Synaptobrevin-2, is a type of SNARE (Soluble N-ethylmaleimide sensitive factor Attachment protein REceptor) protein found in neurons. It is primarily located on the membranes of synaptic vesicles, which are small membrane-bound compartments that store neurotransmitters in the presynaptic terminal.
VAMP-2 plays a crucial role in the process of synaptic vesicle fusion with the presynaptic plasma membrane during neurotransmitter release. This protein interacts with other SNARE proteins, such as syntaxin and SNAP-25, to form a stable complex that brings the vesicle and plasma membranes into close proximity, allowing for the fusion of the two membranes and subsequent release of neurotransmitters into the synaptic cleft.
Mutations in the VAMP-2 gene have been associated with certain neurological disorders, such as autism spectrum disorder and epilepsy, highlighting its importance in normal neuronal function.
Synaptogyrins are a family of proteins that are primarily located in the presynaptic active zones of neurons. They are involved in the regulation and organization of neurotransmitter release at synapses. Specifically, they play a role in the clustering of calcium channels and vesicle fusion proteins, which is critical for the rapid and efficient release of neurotransmitters in response to action potentials. Synaptogyrin-1 is the most well-studied member of this family and has been shown to interact with a number of other synaptic proteins, including neurexins, bassoon, and piccolo. Mutations in synaptogyrin genes have been associated with various neurological disorders, highlighting their importance in normal brain function.
Chromogranins are a group of proteins that are stored in the secretory vesicles of neuroendocrine cells, including neurons and endocrine cells. These proteins are co-released with neurotransmitters and hormones upon stimulation of the cells. Chromogranin A is the most abundant and best studied member of this protein family.
Chromogranins have several functions in the body. They play a role in the biogenesis, processing, and storage of neuropeptides and neurotransmitters within secretory vesicles. Additionally, chromogranins can be cleaved into smaller peptides, some of which have hormonal or regulatory activities. For example, vasostatin-1, a peptide derived from chromogranin A, has been shown to have vasodilatory and cardioprotective effects.
Measurement of chromogranin levels in blood can be used as a biomarker for the diagnosis and monitoring of neuroendocrine tumors, which are characterized by excessive secretion of chromogranins and other neuroendocrine markers.
Carcinoma, neuroendocrine is a type of cancer that arises from the neuroendocrine cells, which are specialized cells that have both nerve and hormone-producing functions. These cells are found throughout the body, but neuroendocrine tumors (NETs) most commonly occur in the lungs, gastrointestinal tract, pancreas, and thyroid gland.
Neuroendocrine carcinomas can be classified as well-differentiated or poorly differentiated based on how closely they resemble normal neuroendocrine cells under a microscope. Well-differentiated tumors tend to grow more slowly and are less aggressive than poorly differentiated tumors.
Neuroendocrine carcinomas can produce and release hormones and other substances that can cause a variety of symptoms, such as flushing, diarrhea, wheezing, and heart palpitations. Treatment for neuroendocrine carcinoma depends on the location and extent of the tumor, as well as the patient's overall health. Treatment options may include surgery, radiation therapy, chemotherapy, targeted therapy, or a combination of these approaches.
Synapsins are a family of proteins found in the presynaptic terminals of neurons. They play a crucial role in the regulation of neurotransmitter release and synaptic plasticity, which is the ability of synapses to strengthen or weaken over time in response to increases or decreases in their activity.
Synapsins are associated with the cytoskeleton of presynaptic terminals and help to tether vesicles containing neurotransmitters to the cytoskeleton. This allows for the rapid mobilization of vesicles to the active zone of the synapse, where they can be released in response to an action potential.
Synapsins are also involved in the regulation of vesicle pool size and the clustering of calcium channels at the active zone. They have been implicated in various neurological disorders, including epilepsy, fragile X syndrome, and Alzheimer's disease.
Chromogranin A is a protein that is widely used as a marker for neuroendocrine tumors. These are tumors that arise from cells of the neuroendocrine system, which is a network of cells throughout the body that produce hormones and help to regulate various bodily functions. Chromogranin A is stored in secretory granules within these cells and is released into the bloodstream when the cells are stimulated to release their hormones.
Chromogranin A is measured in the blood as a way to help diagnose neuroendocrine tumors, monitor the effectiveness of treatment, and track the progression of the disease. Elevated levels of chromogranin A in the blood may indicate the presence of a neuroendocrine tumor, although other factors can also cause an increase in this protein.
It's important to note that while chromogranin A is a useful marker for neuroendocrine tumors, it is not specific to any one type of tumor and should be used in conjunction with other diagnostic tests and clinical evaluation.
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.
Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.
R-SNARE proteins are a subgroup of SNARE (Soluble N-ethylmaleimide sensitive factor Attachment protein REceptor) proteins that are characterized by the presence of an arginine (R) residue at a specific position in their SNARE motif. The SNARE motif is a conserved region of around 60-70 amino acids that plays a crucial role in mediating membrane fusion events in cells.
R-SNARE proteins are typically located on the target membrane, where they interact with Q-SNARE proteins (which contain a glutamine (Q) residue at the corresponding position) on the vesicle membrane to form a stable complex known as a SNARE complex. The formation of this complex brings the two membranes into close proximity and provides the energy required for their fusion, allowing for the transport of cargo between intracellular compartments or from the outside to the inside of the cell.
R-SNARE proteins are involved in various intracellular trafficking pathways, including endocytosis, exocytosis, and membrane recycling. Mutations in R-SNARE proteins have been implicated in several human diseases, such as neurological disorders and cancer.
A synapse is a structure in the nervous system that allows for the transmission of signals from one neuron (nerve cell) to another. It is the point where the axon terminal of one neuron meets the dendrite or cell body of another, and it is here that neurotransmitters are released and received. The synapse includes both the presynaptic and postsynaptic elements, as well as the cleft between them.
At the presynaptic side, an action potential travels down the axon and triggers the release of neurotransmitters into the synaptic cleft through exocytosis. These neurotransmitters then bind to receptors on the postsynaptic side, which can either excite or inhibit the receiving neuron. The strength of the signal between two neurons is determined by the number and efficiency of these synapses.
Synapses play a crucial role in the functioning of the nervous system, allowing for the integration and processing of information from various sources. They are also dynamic structures that can undergo changes in response to experience or injury, which has important implications for learning, memory, and recovery from neurological disorders.
Phosphopyruvate Hydratase is an enzyme also known as Enolase. It plays a crucial role in the glycolytic pathway, which is a series of reactions that occur in the cell to break down glucose into pyruvate, producing ATP and NADH as energy-rich intermediates.
Specifically, Phosphopyruvate Hydratase catalyzes the conversion of 2-phospho-D-glycerate (2-PG) to phosphoenolpyruvate (PEP), which is the second to last step in the glycolytic pathway. This reaction includes the removal of a water molecule from 2-PG, resulting in the formation of PEP and the release of a molecule of water.
The enzyme requires magnesium ions as a cofactor for its activity, and it is inhibited by fluoride ions. Deficiency or dysfunction of Phosphopyruvate Hydratase can lead to various metabolic disorders, including some forms of muscular dystrophy and neurodegenerative diseases.
Neurosecretory systems are specialized components of the nervous system that produce and release chemical messengers called neurohormones. These neurohormones are released into the bloodstream and can have endocrine effects on various target organs in the body. The cells that make up neurosecretory systems, known as neurosecretory cells, are found in specific regions of the brain, such as the hypothalamus, and in peripheral nerves.
Neurosecretory systems play a critical role in regulating many physiological processes, including fluid and electrolyte balance, stress responses, growth and development, reproductive functions, and behavior. The neurohormones released by these systems can act synergistically or antagonistically to maintain homeostasis and coordinate the body's response to internal and external stimuli.
Neurosecretory cells are characterized by their ability to synthesize and store neurohormones in secretory granules, which are released upon stimulation. The release of neurohormones can be triggered by a variety of signals, including neural impulses, hormonal changes, and other physiological cues. Once released into the bloodstream, neurohormones can travel to distant target organs, where they bind to specific receptors and elicit a range of responses.
Overall, neurosecretory systems are an essential component of the neuroendocrine system, which plays a critical role in regulating many aspects of human physiology and behavior.
Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:
1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction
Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:
1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.
Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).
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.
GAP-43 protein, also known as growth-associated protein 43 or B-50, is a neuronal protein that is highly expressed during development and axonal regeneration. It is involved in the regulation of synaptic plasticity, nerve impulse transmission, and neurite outgrowth. GAP-43 is localized to the growth cones of growing axons and is thought to play a role in the guidance and navigation of axonal growth during development and regeneration. It is a member of the calcium/calmodulin-dependent protein kinase substrate family and undergoes phosphorylation by several protein kinases, including PKC (protein kinase C), which regulates its function. GAP-43 has been implicated in various neurological disorders, such as Alzheimer's disease, Parkinson's disease, and schizophrenia.
Neurocytoma is a rare, typically benign (non-cancerous) intraventricular brain tumor originating from the ventricles of the brain. It mainly affects adults in their third to fifth decade of life and accounts for less than 1% of all primary brain tumors. Histologically, neurocytomas are characterized by uniform round cells with salt-and-pepper chromatin and scant cytoplasm, resembling neurons. They usually arise in the lateral ventricles, particularly around the foramen of Monro, and can cause obstructive hydrocephalus due to their location. Neurocytomas are generally slow-growing tumors, but they can sometimes display more aggressive behavior. Complete surgical resection is the treatment of choice when feasible, although radiation therapy and chemotherapy may also be considered in specific cases.
The hippocampus is a complex, curved formation in the brain that resembles a seahorse (hence its name, from the Greek word "hippos" meaning horse and "kampos" meaning sea monster). It's part of the limbic system and plays crucial roles in the formation of memories, particularly long-term ones.
This region is involved in spatial navigation and cognitive maps, allowing us to recognize locations and remember how to get to them. Additionally, it's one of the first areas affected by Alzheimer's disease, which often results in memory loss as an early symptom.
Anatomically, it consists of two main parts: the Ammon's horn (or cornu ammonis) and the dentate gyrus. These structures are made up of distinct types of neurons that contribute to different aspects of learning and memory.
A carcinoid tumor is a type of slow-growing neuroendocrine tumor that usually originates in the digestive tract, particularly in the small intestine. These tumors can also arise in other areas such as the lungs, appendix, and rarely in other organs. Carcinoid tumors develop from cells of the diffuse endocrine system (also known as the neuroendocrine system) that are capable of producing hormones or biologically active amines.
Carcinoid tumors can produce and release various hormones and bioactive substances, such as serotonin, histamine, bradykinins, prostaglandins, and tachykinins, which can lead to a variety of symptoms. The most common syndrome associated with carcinoid tumors is the carcinoid syndrome, characterized by flushing, diarrhea, abdominal cramping, and wheezing or difficulty breathing.
Carcinoid tumors are typically classified as functional or nonfunctional based on whether they produce and secrete hormones that cause symptoms. Functional carcinoid tumors account for approximately 30% of cases and can lead to the development of carcinoid syndrome, while nonfunctional tumors do not produce significant amounts of hormones and are often asymptomatic until they grow large enough to cause local or distant complications.
Treatment options for carcinoid tumors depend on the location, size, and extent of the tumor, as well as whether it is functional or nonfunctional. Treatment may include surgery, medications (such as somatostatin analogs, chemotherapy, or targeted therapies), and radiation therapy. Regular follow-up with imaging studies and biochemical tests is essential to monitor for recurrence and assess treatment response.
Neoplasms are abnormal growths of cells or tissues in the body that can be benign (non-cancerous) or malignant (cancerous). When referring to "Complex and Mixed Neoplasms," it is typically used in the context of histopathology, where it describes tumors with a mixture of different types of cells or growth patterns.
A complex neoplasm usually contains areas with various architectural patterns, cell types, or both, making its classification challenging. It may require extensive sampling and careful examination to determine its nature and behavior. These neoplasms can be either benign or malignant, depending on the specific characteristics of the tumor cells and their growth pattern.
A mixed neoplasm, on the other hand, is a tumor that contains more than one type of cell or tissue component, often arising from different germ layers (the three primary layers of embryonic development: ectoderm, mesoderm, and endoderm). A common example of a mixed neoplasm is a teratoma, which can contain tissues derived from all three germ layers, such as skin, hair, teeth, bone, and muscle. Mixed neoplasms can also be benign or malignant, depending on the specific components of the tumor.
It's important to note that the classification and behavior of complex and mixed neoplasms can vary significantly based on their location in the body, cellular composition, and other factors. Accurate diagnosis typically requires a thorough examination by an experienced pathologist and may involve additional tests, such as immunohistochemistry or molecular analysis, to determine the appropriate treatment and management strategies.
Dimethyl suberimidate is a homobifunctional cross-linking agent that is used in molecular biology for protein-protein or protein-nucleic acid cross-linking. It is an imidoester with the chemical formula (CH3)2N-CO-[CH2]8-CO-N(CH3)2.
This reagent works by reacting with primary amines (-NH2) on proteins or nucleic acids, forming stable amide bonds between them. The length of the spacer arm (comprising eight methylene groups) provides sufficient distance and flexibility for the cross-linked molecules to maintain their native structures and functions.
Dimethyl suberimidate is used in various applications, such as studying protein-protein interactions, mapping protein domains, and analyzing protein complexes' structures. It is crucial to perform cross-linking reactions under controlled conditions to ensure specificity and minimize non-specific binding.
Synaptotagmins are a family of calcium-binding proteins that are primarily located in the presynaptic terminals of neurons. They play a crucial role in the regulation of synaptic vesicle exocytosis, which is the process by which neurotransmitters are released into the synaptic cleft. Synaptotagmins function as calcium sensors for synaptic vesicle fusion, and they are involved in the rapid synchronization of neurotransmitter release in response to action potentials. There are several isoforms of synaptotagmin, each with distinct biochemical and functional properties, that contribute to the diversity and specificity of synaptic transmission.
Presynaptic terminals, also known as presynaptic boutons or nerve terminals, refer to the specialized structures located at the end of axons in neurons. These terminals contain numerous small vesicles filled with neurotransmitters, which are chemical messengers that transmit signals between neurons.
When an action potential reaches the presynaptic terminal, it triggers the influx of calcium ions into the terminal, leading to the fusion of the vesicles with the presynaptic membrane and the release of neurotransmitters into the synaptic cleft, a small gap between the presynaptic and postsynaptic terminals.
The released neurotransmitters then bind to receptors on the postsynaptic terminal, leading to the generation of an electrical or chemical signal that can either excite or inhibit the postsynaptic neuron. Presynaptic terminals play a crucial role in regulating synaptic transmission and are targets for various drugs and toxins that modulate neuronal communication.
Vesicular Glutamate Transport Proteins (VGLUTs) are a group of proteins that play a crucial role in the packaging and transport of the neurotransmitter glutamate into synaptic vesicles within neurons. Glutamate is the primary excitatory neurotransmitter in the central nervous system, and its release and uptake must be tightly regulated to maintain proper neural communication.
VGLUTs are integral membrane proteins located on the membranes of synaptic vesicles. They facilitate the accumulation of glutamate inside these vesicles through a process called antiport, where they exchange glutamate for protons from the cytoplasm. This results in a high concentration of glutamate within the vesicle, allowing for its regulated release upon neuronal stimulation.
There are three isoforms of VGLUTs (VGLUT1, VGLUT2, and VGLUT3) encoded by different genes (SLC17A7, SLC17A6, and SLC17A8, respectively). These isoforms exhibit distinct expression patterns in the central nervous system and are involved in various neurological functions. Dysregulation of VGLUTs has been implicated in several neurological disorders, including epilepsy, pain perception, and neurodegenerative diseases.
Neuroendocrine cells are specialized cells that are found throughout the body, but primarily in the respiratory and digestive tracts. These cells have characteristics of both neurons and endocrine cells. Like neurons, neuroendocrine cells can receive and transmit signals to other cells using chemical messengers called neurotransmitters. Like endocrine cells, they can produce and secrete hormones into the bloodstream, where they can travel to other parts of the body and affect the function of distant organs.
Neuroendocrine cells are responsible for a variety of physiological functions, including regulating air and blood flow in the lungs, controlling the motility and secretion of the gastrointestinal tract, and modulating immune responses. They can also play a role in the development and progression of certain diseases, such as neuroendocrine tumors, which are rare but aggressive cancers that can arise from these cells.
Anatomically, neuroendocrine cells can be found as scattered individual cells or as clusters of cells called neuroepithelial bodies. They are characterized by the presence of dense-core granules containing hormones and neurotransmitters, which can be released in response to various stimuli. Neuroendocrine cells can also express a variety of receptors, including those for neurotransmitters, hormones, and growth factors, which allow them to respond to signals from other cells and modulate their own activity.
Paraganglioma, extra-adrenal, is a type of rare tumor that develops in the nervous system's paraganglia, which are groups of specialized cells that are responsible for regulating blood pressure and other bodily functions. Unlike adrenal paragangliomas, which form in the adrenal glands located on top of the kidneys, extra-adrenal paragangliomas develop outside of the adrenal glands, in various locations along the sympathetic and parasympathetic nervous systems. These tumors can be functional or nonfunctional, meaning they may or may not produce hormones such as catecholamines (epinephrine, norepinephrine, and dopamine). Functional extra-adrenal paragangliomas can cause symptoms related to excessive hormone production, including hypertension, sweating, headaches, and rapid heartbeat. Treatment typically involves surgical removal of the tumor, along with preoperative preparation to manage potential hormonal imbalances.
Organelles are specialized structures within cells that perform specific functions essential for the cell's survival and proper functioning. They can be thought of as the "organs" of the cell, and they are typically membrane-bound to separate them from the rest of the cellular cytoplasm. Examples of organelles include the nucleus (which contains the genetic material), mitochondria (which generate energy for the cell), ribosomes (which synthesize proteins), endoplasmic reticulum (which is involved in protein and lipid synthesis), Golgi apparatus (which modifies, sorts, and packages proteins and lipids for transport), lysosomes (which break down waste materials and cellular debris), peroxisomes (which detoxify harmful substances and produce certain organic compounds), and vacuoles (which store nutrients and waste products). The specific organelles present in a cell can vary depending on the type of cell and its function.
Exocytosis is the process by which cells release molecules, such as hormones or neurotransmitters, to the extracellular space. This process involves the transport of these molecules inside vesicles (membrane-bound sacs) to the cell membrane, where they fuse and release their contents to the outside of the cell. It is a crucial mechanism for intercellular communication and the regulation of various physiological processes in the body.
Synaptophysin
SYPL1
VAMP2
Ceruminous adenoma
Neuroendocrine differentiation
Parkinson's disease clinical research
Chromogranin A
SIAH1
Nestin (protein)
Neuroendocrine tumor
AP1G1
SIAH2
UBE2L6
UBE2E2
SNAP91
SYNGR1
Lung cancer
Leteprinim
CPLX2
Environmental enrichment
Superior olivary complex
Synapto-pHluorin
Pineoblastoma
Werner Franke
SYNPR
Vesicular transport protein
RE1-silencing transcription factor
CNKSR2
MIA PaCa-2
Hensen's cell
Synaptophysin - Wikipedia
Product Listing - Synaptophysin - Cedarlane
Synaptophysin Monoclonal Antibody (SYP, 3551) (6855-MSM1-P1) ...
Synaptophysin monoclonal antibody (EP10) - ADI-905-782 - Enzo Life Sciences
Synaptophysin - Pathline
Synaptophysin Antibody | Affinity Biosciences
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MARVEL Domain-Containing Proteins - Synaptophysin | CU Experts | CU Boulder
Synaptophysin gene expression in human brain: a quantitative in situ hybridization and immunocytochemical study. - Department...
Synaptophysin I selectively specifies the exocytic pathway of synaptobrevin 2/VAMP2.
Striatal synaptophysin expression and haloperidol-induced synaptic plasticity. - Department of Psychiatry
Synaptophysin Test in Kolkata : Synaptophysin Test At Home @ Best Prices
Serval - Neuron-associated class III beta-tubulin isotype, microtubule-associated protein 2, and synaptophysin in human...
Metastatic Cancer With Unknown Primary Site Medication: Antineoplastic Agents
CB2 cannabinoid receptor agonist ameliorates Alzheimer-like phenotype in AβPP/PS1 mice
Estrogen and insulin transport through the blood-brain barrier
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Synaptophysin and insulin-like growth factor-1 immunostaining in the central nucleus of the inferior colliculus in adult...
Estrogen up-regulates estrogen receptor α and synaptophysin in slice cultures of rat hippocampus<...
Detection and quantification of hippocampal synaptophysin messenger RNA in schizophrenia using autoclaved, formalin-fixed,...
Thieme E-Journals - Arquivos Brasileiros de Neurocirurgia: Brazilian Neurosurgery / Full Text
Neuroendocrine Markers Insulinoma-Associated Protein 1, Chromogranin, Synaptophysin, and CD56 Show Rare Positivity in...
Aberrant intermediate filament and synaptophysin expression is a frequent event in malignant melanoma: An immunohistochemical...
Neonatal prebiotic (BGOS) supplementation increases the levels of synaptophysin, GluN2A-subunits and BDNF proteins in the adult...
Expressions of amyloid precursor protein, synaptophysin and presenilin-1 in the different areas of the developing cerebellum of...
IJMS | Free Full-Text | A Novel Zinc Chelator, 1H10, Ameliorates Experimental Autoimmune Encephalomyelitis by Modulating Zinc...
Ovary | College of American Pathologists
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Chromogranin11
- Diagnostically, it is often used in combination with chromogranin A. Synaptophysin has been shown to interact with AP1G1 and SIAH2. (wikipedia.org)
- Adenocarcinoma ex-goblet cell carcinoid (AdexGCC) was considered a neuroendocrine adenocarcinoma, despite majority of tumor cells being negative for conventional neuroendocrine markers such as chromogranin and synaptophysin. (gastrores.org)
- Recently, insulinoma-associated protein 1 (INSM1) has been identified as a novel neuroendocrine marker that is more sensitive than chromogranin, synaptophysin, and CD56 in pulmonary neuroendocrine tumors. (gastrores.org)
- We studied this marker in conjunction with chromogranin, synaptophysin, and CD56 in 36 appendiceal AdexGCCs (21 primaries, 15 metastatic). (gastrores.org)
- Primary and metastatic AdexGCCs showed no difference in INSM1, chromogranin, synaptophysin, or CD56 staining. (gastrores.org)
- INSM1 exhibits low expression in AdexGCCs and is expressed by a lower proportion of tumor cells compared to chromogranin and synaptophysin. (gastrores.org)
- Conventional neuroendocrine markers, such as chromogranin and synaptophysin, however, are often negative or focally positive in these tumors [ 2 , 3 ]. (gastrores.org)
- Hristov et al previously demonstrated that chromogranin and synaptophysin were only expressed in 37% and 30% of AdexGCCs, respectively [ 2 ]. (gastrores.org)
- In contrast, conventional carcinoids are often diffusely positive for chromogranin and synaptophysin, with abundant electron-dense granules on electron microscopy [ 4 ]. (gastrores.org)
- Available sections were immunostained for keratin (OSCAR and AE1/AE3 antibodies), desmin, neurofilament protein, glial fibrillary acidic protein, synaptophysin, and chromogranin A. Not all cases could be tested for all markers. (elsevierpure.com)
- MCC express both neuroendocrine (neuron-specific enolase, synaptophysin, chromogranin) and cytokeratin markers (cytokeratin 20, as a paranuclear dot, CAM 5.2) and is negative for S100 and the common leukocyte antigen ( 2 ). (ispub.com)
Protein13
- Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the SYP gene. (wikipedia.org)
- The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally. (wikipedia.org)
- Synaptophysin is an integral membrane protein involved in neurotransmitter exocytosis. (enzolifesciences.com)
- Studies have shown Synaptophysin to be a major cholesterol-binding protein in brain synaptic vesicles. (enzolifesciences.com)
- Synaptophysin is a presynaptic vesicle protein. (ox.ac.uk)
- Detection of synaptophysin messenger RNA broadens the range of methods by which synaptic protein gene products can be studied and used as markers of synaptic density and synaptic involvement during physiological and pathological processes in human brain. (ox.ac.uk)
- Protein-protein interaction is not sufficient for the control of VAMP2 sorting, which is mediated by the C-terminal domain of synaptophysin I. Synaptophysin I directs the sorting of VAMP2 to vesicles before surface delivery, without influencing VAMP2 endocytosis. (uninsubria.it)
- Consistent with this, dynamin and a-SNAP (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein) mutants which block trafficking at the plasma membrane do not abrogate the effect of synaptophysin I on VAMP2 sorting. (uninsubria.it)
- Synaptophysin is a presynaptic vesicle protein and a marker of synaptic density. (ox.ac.uk)
- Synaptophysin is a protein that is found in neurons. (flebo.in)
- Neuron-associated class III beta-tubulin isotype, microtubule-associated protein 2, and synaptophysin in human retinoblastomas in situ. (unil.ch)
- This study reveals the expressions of Alzheimer's disease-related amyloid precursor protein, presenilin-1, and a presynaptic marker protein, synaptophysin, in the archi-, paleo- and neocerebellum during the postnatal development of the rat. (northwestern.edu)
- It is concluded that the postnatal expressions of soluble and membrane-bound amyloid precursor protein, synaptophysin and presenilin-1 are regulated differently during the ontogenetical development of the archi-, paleo- and neocerebellum of rat. (northwestern.edu)
Studied synaptophysin messenger1
- We have studied synaptophysin messenger RNA in the neocortex, hippocampus and cerebellum using in situ hybridization histochemistry to see if the encoding transcript can be detected in post mortem human brain and to investigate factors which might influence its abundance. (ox.ac.uk)
Level of synaptophysin3
- The level of synaptophysin messenger RNA expression was uniform in all neocortical areas examined. (ox.ac.uk)
- The level of synaptophysin messenger RNA paralleled that of synaptophysin immunoreactivity, indicating that changes in gene expression contribute to variations in the latter observed in aging and other situations. (ox.ac.uk)
- The level of synaptophysin increases progressively from postnatal day 7 up to 3 weeks in the archi- and paleocerebellum, and up to 6 weeks in the neocerebellum. (northwestern.edu)
Immunoreactivity6
- Synaptophysin immunoreactivity also reduced with age, as well as with duration of formalin fixation but not post mortem interval. (ox.ac.uk)
- Synaptophysin immunoreactivity correlated with the abundance of the messenger RNA in neurons within, and projecting to, each hippocampal subfield. (ox.ac.uk)
- Significantly greater synaptophysin immunoreactivity was seen in the left than the right CA4 and CA1 regions. (ox.ac.uk)
- A similar trend was observed for synaptophysin immunoreactivity. (ox.ac.uk)
- In tissue sections as well as in slice cultures mRNA expression of ERα, ERβ and synaptophysin was higher in CA3 than in CA1, and mRNA expression and immunoreactivity for both ER subtypes were found in both principal cells and interneurons. (elsevierpure.com)
- In slice cultures, supplementation of the medium with 10 -8 M estradiol led to an increase of nuclear immunoreactivity for ERα, but not for ERβ, which was accompanied by a dramatic up-regulation of synaptophysin immunoreactivity in stratum radiatum of CA1. (elsevierpure.com)
Hippocampal synaptophysin2
Presynaptic marker1
- To this end, we studied estrogen-induced expression of both estrogen receptor (ER) subtypes (ERα and ERβ) together with the presynaptic marker synaptophysin in the rat hippocampus. (elsevierpure.com)
Hippocampus3
- Synaptophysin was also measured immunocytochemically in the hippocampus. (ox.ac.uk)
- Neonatal prebiotic (BGOS) supplementation increases the levels of synaptophysin, GluN2A-subunits and BDNF proteins in the adult rat hippocampus. (ox.ac.uk)
- The administration of BGOS significantly elevated GluN2A subunits, synaptophysin and BDNF in the hippocampus of 22 day old rats. (ox.ac.uk)
Synapses1
- It acts as a marker for neuroendocrine tumors, and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses. (wikipedia.org)
Quantification1
- Quantification of synaptophysin mRNA per cell showed that the increase was pronounced in large putatively cholinergic, striatal neurones. (ox.ac.uk)
Synaptic plasticity1
- Striatal synaptophysin expression and haloperidol-induced synaptic plasticity. (ox.ac.uk)
Immunohistochemical1
- Immunohistochemical examination revealed neuronal tumor immunophenotype with diffuse positivity for non-specific enolase, synaptophysin, and focal positivity for S-100. (thieme-connect.com)
Neurons4
- Synaptophysin is a calcium-binding and integral membrane glycoprotein present in presynaptic vesicles in almost all neurons. (thermofisher.com)
- D ) Immunostaining of uninfected primary neurons for endogenous synaptophysin (green) and synapsin (magenta). (elifesciences.org)
- Specifically, neurons are expressing endogenously tagged synaptophysin with a triple HA-tag (top row), SV2A tagged at the N-terminus with nine tandem HA-tags (9x HA) (middle row), and synaptogyrin tagged at the N-terminus with a 9X HA-tag (bottom row). (elifesciences.org)
- Lysates were prepared from neurons infected with lentivirus encoding for synaptophysin conjugated to three HA-tags (3X) or nine HA-tags (9X). (elifesciences.org)
Tumor2
Proteins3
- Ectopically expressed synaptophysin I interacts with VAMP2 and alters its default surface targeting to a prominent vesicular distribution, with no effect on the targeting of other membrane proteins. (uninsubria.it)
- These results indicate that the sorting determinants of synaptic vesicle proteins can operate independently of a neuronal context and implicate the association of VAMP2 with synaptophysin I in the specification of the pathway of synaptic vesicle biogenesis. (uninsubria.it)
- We have tested whether feeding neonatal rats daily (from post-natal days 3-21) with a galacto-oligosaccharide prebiotic (Bimuno®, BGOS) or a control solution, alters the levels of hippocampal N-Methyl-D-Aspartate receptor (NMDAR) subunits (GluN1, GluN2A, GluN2B), synaptic proteins (synaptophysin, MAP2, and GAP43) and brain-derived-neurotrophic factor (BDNF), at post-natal days 22 and 56. (ox.ac.uk)
Monoclonal3
- The following product was used in this experiment: Synaptophysin Monoclonal Antibody (SYP, 3551) from Thermo Fisher Scientific, catalog # 6855-MSM1-P1. (thermofisher.com)
- Product Description google Mouse anti-Synaptophysin Monoclonal Antibody (Unconjugated), suitable for WB, IHC-Frozen, IHC-Paraffin-embedded. (biosensis.com)
- Synaptophysin is a glycoprotein that is a component of the membrane of neuroendocrine secretory granules and is identified by monoclonal antibodies in a number of neuroendocrine tumors. (flebo.in)
Neuroendocrine cells1
- Synaptophysin is a useful marker for the identification of normal neuroendocrine cells and neuroendocrine neoplasms. (biosensis.com)
Vimentin1
- Immunohistochemistry was performed in both tissue and 3D sections for markers including synaptophysin, vimentin, neurofilament and MIB-1. (frontiersin.org)
Endogenous1
- Synaptophysin Antibody detects endogenous levels of total Synaptophysin. (affbiotech.com)
Glycoprotein1
- Scientific Background Synaptophysin is a 38 kDa glycoprotein present in the membranes of neuronal presynaptic vesicles in brain, spinal cord, retina, vesicles of adrenal medulla, neuromuscular junctions and endocrine cells. (biosensis.com)
MRNA1
- A significant increase in synaptophysin mRNA content was observed in the dorsolateral striatum but not in other brain areas compared with control animals. (ox.ac.uk)
Immunohistochemistry2
- Using immunohistochemistry, synaptophysin can be demonstrated in a range of neural and neuroendocrine tissues, including cells of the adrenal medulla and pancreatic islets. (wikipedia.org)
- Synaptophysin Test is the most reliable immunohistochemistry marker for identifying the abnormal tumors causing cancer. (flebo.in)
Formalin2
- A concentration of 1.0-2.0 µg/mL is recommended to detect synaptophysin in formalin/acetone fixed tissues. (biosensis.com)
- To do this, we targeted synaptophysin messenger RNA with a 35S-labelled oligonucleotide probe in autoclaved, formalin-fixed, paraffin wax-embedded sections of the hippocampal formation of 11 schizophrenics and 11 controls. (ox.ac.uk)
Stain1
- A pathological complete response confirmed by a synaptophysin stain was noted at both sites. (ispub.com)
Situ1
- Synaptophysin gene expression in human brain: a quantitative in situ hybridization and immunocytochemical study. (ox.ac.uk)
Synaptobrevin1
- Synaptophysin I selectively specifies the exocytic pathway of synaptobrevin 2/VAMP2. (uninsubria.it)
Tissues1
- As synaptophysin is a maker of these neuroendocrine tissues, it forms a reliable source to test the formation of tumors. (flebo.in)
Detect1
- The Synaptophysin Test is run to detect the neuroendocrine tumors in the cells. (flebo.in)
Human2
- Western blot analysis of MW marker (1) and Human brain extract (2), probed with Synaptophysin mAb (EP10). (enzolifesciences.com)
- These data show that quantitative detection of synaptophysin messenger RNA as well as synaptophysin itself can reliably be carried out in post mortem human brain sections. (ox.ac.uk)
Expression3
- We have seen in consultation a number of malignant melanomas with anomalous expression of keratin, other intermediate filaments, or synaptophysin, and therefore studied a large group of primary and metastatic melanomas to determine the frequency of these events. (elsevierpure.com)
- Anomalous expression of all intermediate filaments and synaptophysin was found in significant subsets of malignant melanoma, representing potentially serious diagnostic pitfalls. (elsevierpure.com)
- Malignant melanoma showing anomalous intermediate filament and synaptophysin expression may easily be mistaken for carcinomas, rhabdomyosarcomas, and neuroendocrine tumors. (elsevierpure.com)
Complex1
- Synaptophysin has four transmembrane domains and it forms a complex with dynamin at high calcium concentrations suggesting an involvement in synaptic vesicle endocytosis. (thermofisher.com)
Found2
- Strong correlations were found for the amount of synaptophysin messenger RNA between individual regions and between homologous areas in the two hemispheres. (ox.ac.uk)
- We found a similar pattern and magnitude of decreased synaptophysin messenger RNA in schizophrenia in the autoclaved sections as we had in the frozen sections, including the selective preservation of synaptophysin messenger RNA in CA1. (ox.ac.uk)
Messenger4
- Synaptophysin messenger RNA declined with increasing age and prolonged post mortem interval. (ox.ac.uk)
- Synaptophysin messenger RNA was readily detected in the autoclaved sections. (ox.ac.uk)
- The reduction of synaptophysin messenger RNA was replicated when six subjects with schizophrenia not included in the earlier study were considered separately. (ox.ac.uk)
- Using this material, we confirmed the finding of decreased synaptophysin messenger RNA in the hippocampal formation in schizophrenia, furthering the evidence for synaptic pathology in this region in the disorder. (ox.ac.uk)
Present2
- There are only two interpretations of the synaptophysin test: either the neuroendocrine tumors are present in the body or they are absent. (flebo.in)
- In a 3-week-old animal, synaptophysin staining is present in all areas of the cerebellar molecular layer and in the internal granule cell layer. (northwestern.edu)
Shown1
- Recent research has shown, however, that elimination of synaptophysin in mice creates behavioral changes such as increased exploratory behavior, impaired object novelty recognition, and reduced spatial learning. (wikipedia.org)