Proprotein Convertase 1
Proprotein Convertase 2
Pituitary Gland, Anterior
Molecular Sequence Data
Cutting edge: peripheral neuropeptides attract immature and arrest mature blood-derived dendritic cells. (1/46)Dendritic cells (DC) are highly motile and play a key role in mediating immune responses in various tissues and lymphatic organs. We investigated locomotion of mononuclear cell-derived DC at different maturation stages toward gradients of sensory neuropeptides in vitro. Calcitonin gene-related peptide, vasoactive intestinal polypeptide, secretin, and secretoneurin induced immature DC chemotaxis comparable to the potency of RANTES, whereas substance P and macrophage-inflammatory protein-3beta stimulated immature cell migration only slightly. Checkerboard analyses revealed a true chemotactic response induced by neuropeptides. Upon maturation of DC, neuropeptides inhibited spontaneous, macrophage-inflammatory protein-3beta- and 6Ckine-induced cell migration. Maturation-dependent changes in migratory behavior coincided with distinct neuropeptide-induced signal transduction in DC. Peripheral neuropeptides might guide immature DC to peripheral nerve fibers where high concentrations of these peptides can arrest the meanwhile matured cells. It seems that one function of sensory nerves is to fasten DC at sites of inflammation. (+info)
Secretoneurin and neurogenic inflammation. (2/46)AIM: Review of evidence that the 33-amino-acid polypeptide secretoneurin, which is generated by proteolytic cleavage of secretogranin II, plays a role in neurogenic inflammation. METHODS: Survey of the literature using a MEDLINE search database. RESULTS: Secretoneurin is synthesized in spinal ganglia, transported through the dorsal roots and stored in the axon terminals of primary afferent neurons. Investigations using capsaicin suggest that secretoneurin functions as an excitatory transmitter. Secretoneurin specifically activates various cell functions including the chemotactic migration of monocytes, eosinophils, fibroblasts, smooth muscle cells, and endothelial cells, which suggests that the peptide may modulate inflammatory reactions. Secretoneurin receptors have been functionally characterized. They are G-proteins linked and effects are abrogated by inhibition of protein kinase C. CONCLUSION: With actions as diverse as those seen with other mediators such as tachykinins, secretoneurin may be considered another sensory neuropeptide with modulatory potential in neurogenic inflammation. (+info)
Pituitary adenylate cyclase-activating polypeptide stimulates secretoneurin release and secretogranin II gene transcription in bovine adrenochromaffin cells through multiple signaling pathways and increased binding of pre-existing activator protein-1-like transcription factors. (3/46)Secretoneurin (SN) is a novel bioactive peptide that derives from the neuroendocrine protein secretogranin II (SgII) by proteolytic processing and participates in neuro-immune communication. The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP-38) dose-dependently stimulates (EC(50) approximately 3 nM) SN release (up to 4-fold) and SgII gene expression (up to 60-fold) in cultured bovine adrenochromaffin cells. The effect of PACAP on both SN secretion and SgII mRNA levels is rapid and long lasting. We analyzed in this neuroendocrine cell model the transduction pathways involved in both SN secretion and SgII gene transcription in response to PACAP. The cytosolic calcium chelator BAPTA-AM and the nonselective calcium channel antagonist NiCl(2) equally inhibited both secretion of the peptide and transcription of the SgII gene, indicating a major contribution of calcium influx in PACAP-induced SN biosynthesis and release in chromaffin cells. Inhibition of protein kinase A (PKA) or C (PKC) also reduced PACAP-evoked SN release but did not alter the stimulatory effect of PACAP on SgII mRNA levels. Conversely, application of mitogen-activated protein kinase inhibitors suppressed PACAP-induced SgII gene expression. The effect of PACAP on SgII mRNA levels, like the effect of the PKC stimulator 12-O-tetradecanoylphorbol-13-acetate (TPA), was not affected by cycloheximide, whereas the effects of the PKA stimulator forskolin or cell-depolarization by high K(+) were significantly reduced by the protein synthesis inhibitor. PACAP and TPA both increased the binding activity of the SgII cAMP response element to trans-acting factors present in chromaffin cell nuclear extracts, which are recognized by antibodies to activator protein-1-related proteins. These data indicate that SN biosynthesis is regulated by PACAP in chromaffin cells through complex signaling cascades, suggesting that SN may play a function during trans-synaptic stimulation of the adrenal medulla. (+info)
Inhibitory effect of certain neuropeptides on the proliferation of human retinal pigment epithelial cells. (4/46)AIMS: To define the effect of the neuropeptides substance P, calcitonin gene related peptide, vasoactive intestinal polypeptide, neuropeptide Y, and secretoneurin on the proliferation of human retinal pigment epithelial (RPE) cells. METHODS: ARPE-19 cells were used. The cells were cultured in Dulbecco's modified Eagle's medium. 1000 and 2000 cells were incubated with the peptides for 3 and 5 days, and the effect of the peptides was evaluated by an ATP lite assay dose dependently. Furthermore, specific antagonists at 10(-6) M were used to find out whether the effect would be reversed. RESULTS: In brief, each of the peptides tested had an inhibiting effect. This inhibiting effect was weak but highly significant, averaging 10% to 15%, and was most pronouncedly seen at concentrations between 10(-10) M and 10(-14) M. Each antagonist reversed the inhibiting effect fully. CONCLUSIONS: These results clearly indicate that RPE cells are under neural control and the low effective concentration of the peptides may be the one physiologically acting on these cells. The results are of important relevance both physiologically and pathophysiologically: physiologically, the inhibitory effect may mean that these peptides cause the cells to remain in a differentiated condition. Pathophysiologically, the findings are relevant in proliferative vitreoretinopathy where RPE cells proliferate in excess. The authors hypothesise that the inhibiting effect diminishes when these cells are swept out and actively migrate from their physiological location and thus, dedifferentiate and begin to proliferate. This hypothesis improves the knowledge of the initial processes in the pathogenesis of the disease as there seems to be a discrepancy between facilitatory and inhibitory influences favouring the former in proliferative vitreoretinopathy. Furthermore, these neuropeptides constitute the first endogenous inhibitors of RPE cell proliferation. (+info)
The neuropeptide secretoneurin acts as a direct angiogenic cytokine in vitro and in vivo. (5/46)BACKGROUND: Secretoneurin is an abundant neuropeptide of the central, peripheral, and autonomic nervous systems, located in nerve fibers characterized by a close interaction with blood vessels and known to stimulate endothelial cell migration. METHODS AND RESULTS: We hypothesized that secretoneurin might act as an angiogenic cytokine and tested for these effects in vivo using a mouse cornea neovascularization model and in vitro by assessing capillary tube formation in a matrigel assay. In vivo, secretoneurin-induced neovasculature is characterized by a distinct pattern of arterial and venous vessels of large diameter and length. Immunohistochemical staining for CD-31 revealed endothelial lining of the inner surface of these vessels, and recruitment of alpha-smooth muscle actin-positive perivascular cells suggests vessel maturation. In vitro, secretoneurin-induced capillary tube formation was dose dependent and specific, confirming that effects of secretoneurin occur directly on endothelial cells. Secretoneurin also stimulated proliferation and exerted antiapoptotic effects on endothelial cells and activated intracellular phosphatidylinositol 3' kinase/Akt and mitogen-activated protein kinase pathways, as demonstrated by increased phosphorylation of Akt and extracellular signal-regulated kinase. CONCLUSIONS: These data show that secretoneurin represents a novel direct angiogenic cytokine and reiterate the coordinated relationship between nervous and vascular systems. (+info)
The immune modulator FTY720 targets sphingosine-kinase-dependent migration of human monocytes in response to amyloid beta-protein and its precursor. (6/46)Accumulation of inflammatory mononuclear phagocytes in Alzheimer's senile plaques, a hallmark of the innate immune response to beta-amyloid fibrils, can initiate and propagate neurodegeneration characteristic of Alzheimer's disease. Phagocytes migrate toward amyloid beta-protein involving formyl peptide receptor like-1-dependent signaling. Using human peripheral blood monocytes in Boyden chamber micropore filter assays, we show that the amyloid beta-protein- and amyloid beta-precursor protein-induced migration was abrogated by dimethylsphingosine, a sphingosine kinase inhibitor. Amyloid beta-protein stimulated in monocytes the gene expression for sphingosine-1-phosphate receptors 2 and 5, but not 1, 3, and 4. FTY720 that acts as a sphingosine-1-phosphate receptor agonist after endogenous phosphorylation by sphingosine kinase, as well as various neuropeptides that are known to be monocyte chemoattractants, dose-dependently inhibited amyloid beta-protein-induced migration. These data demonstrate that the migratory effects of beta-amyloid in human monocytes involve spingosine-1-phosphate signaling. Whereas endogenous neuropeptides may arrest and activate monocytes at sites of high beta-amyloid concentrations, interference with the amyloid beta-protein-dependent sphingosine-1-phosphate pathway in monocytes by FTY720, a novel immunomodulatory drug, suggests that FTY720 may be efficacious in beta-amyloid-related inflammatory diseases. (+info)
Secretoneurin, an angiogenic neuropeptide, induces postnatal vasculogenesis. (7/46)BACKGROUND: Induction of postnatal vasculogenesis, the mobilization of bone marrow-derived endothelial progenitor cells and incorporation of these cells into sites of blood vessel formation, is a well-known feature of angiogenic cytokines such as vascular endothelial growth factor. We hypothesized that the angiogenic neuropeptide secretoneurin induces this kind of neovascularization. METHODS AND RESULTS: Secretoneurin induced mobilization of endothelial progenitor cells to sites of vasculogenesis in vivo in the cornea neovascularization assay. Progenitor cells were incorporated into vascular structures or were located adjacent to them. Systemic injection of secretoneurin led to increase of circulating stem cells and endothelial progenitor cells. In vitro secretoneurin induced migration, exerted antiapoptotic effects, and increased the number of these cells. Furthermore, secretoneurin stimulated the mitogen-activated protein kinase system, as shown by phosphorylation of extracellular signal-regulated kinase, and activated the protein kinase B/Akt pathway. Activation of mitogen-activated protein kinase was necessary for increase of cell number and migration, whereas Akt seemed to play a role in migration of endothelial progenitor cells. CONCLUSIONS: These data show that the angiogenic neuropeptide secretoneurin stimulates postnatal vasculogenesis by mobilization, migration, and incorporation of endothelial progenitor cells. (+info)
Secretoneurin in the peripheral ocular innervation. (8/46)PURPOSE: To evaluate whether secretoneurin represents a sensory neuropeptide innervating the anterior segment of the eye. METHODS: The presence and distribution of secretoneurin was investigated in human eyes by radioimmunoassay and immunofluorescence and compared with that of the rat eye. The source of secretoneurin-positive nerves in the eye was established by measuring the concentration in eye tissues, the trigeminal and superior cervical ganglia both in control rats and in rats treated with capsaicin, and by performing immunofluorescence in one rat subjected to sympathectomy. In the rat trigeminal ganglion, the corresponding mRNA was verified by in situ hybridization and the processing of secretogranin II into secretoneurin by gel filtration chromatography. RESULTS: In human eyes, the highest levels of the peptide were found in the choroid. Nerve fibers were visualized in both species in the upper corneal and limbal stroma; in the trabecular meshwork; in the ciliary muscle, the ciliary body stroma, and processes; and in clear association with the dilator muscle, which disappeared after sympathetic denervation in rats; and also innervating the sphincter muscle in the iris and the choroidal stroma and surrounding blood vessels. Significant amounts of secretoneurin were present in the rat trigeminal ganglion and rat eye tissues. Capsaicin pretreatment led to a 57.0% +/- 4.3% and 59.1% +/- 11.9% decrease of the concentration in the trigeminal ganglion and the iris/ciliary body complex, respectively. Despite high levels in the rat superior cervical ganglion, sympathetic denervation failed to lower the concentration in eye tissues. The secretogranin II probe labeled numerous small-sized ganglion cells within the rat trigeminal ganglion, and the precursor of the peptide was found to become completely processed into secretoneurin. CONCLUSIONS: Apart from the sympathetically innervated dilator muscle, there is unequivocal evidence that secretoneurin represents a constituent of capsaicin-sensitive sensory neurons in the rat trigeminal ganglion and of unmyelinated C-fibers in the rat iris/ciliary body complex, which indicates a participation of this peptide in the ocular irritative response, a model for neurogenic inflammation in lower mammals. Because of the association of nerves with blood vessels and potent angiogenic properties, secretoneurin may be involved in neovascularization processes. (+info)
Secretogranin II, also known as chromogranin A-like immunoreactivity or secretoneurin precursor, is a protein that belongs to the granin family. Granins are involved in neuroendocrine differentiation and are commonly used as markers for neuroendocrine tumors.
Secretogranin II is a 59 kDa protein that is synthesized as part of larger precursors, which undergo proteolytic processing to generate smaller bioactive peptides. These peptides have various functions, including modulation of neurotransmitter release and regulation of blood pressure.
Secretogranin II is primarily localized in secretory vesicles of neurons and endocrine cells, where it plays a role in the packaging, transport, and exocytosis of neurosecretory granules. It has been identified as a major component of dense-core vesicles, which store and release hormones and neuropeptides.
In summary, Secretogranin II is a protein involved in the biogenesis and secretion of neurosecretory granules in neurons and endocrine cells.
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.
Chromogranin B is a protein that is primarily found in the secretory granules of neuroendocrine cells, including neurons and endocrine cells. These granules are specialized organelles where hormones and neurotransmitters are stored before being released into the extracellular space. Chromogranin B is co-synthesized and packaged with these secretory products and is therefore often used as a marker for neuroendocrine differentiation.
Chromogranin B is a member of the chromogranin/secretogranin family of proteins, which are characterized by their ability to form large aggregates in the acidic environment of secretory granules. These aggregates play a role in the sorting and processing of secretory products, as well as in the regulation of granule biogenesis and exocytosis.
Chromogranin B has been shown to have various biological activities, including inhibition of protein kinase C, stimulation of calmodulin-dependent processes, and modulation of ion channel activity. However, its precise physiological functions remain to be fully elucidated. Dysregulation of chromogranin B expression and processing has been implicated in several pathological conditions, including neurodegenerative diseases and neoplasia.
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.
Proprotein convertase 1 (PCSK1) is a protein-coding gene that encodes for the prohormone convertase 1/3 (PC1/3), also known as PCsk1 or PCSK1. This enzyme belongs to the family of subtilisin-like proprotein convertases, which play crucial roles in processing and activating various peptide hormones and neuropeptides by cleaving their precursor proteins.
PC1/3 is primarily expressed in neuroendocrine cells, neurons, and enteroendocrine cells of the gastrointestinal tract. It is involved in the maturation of several bioactive peptides, such as:
1. Proinsulin: PC1/3 processes proinsulin into insulin and C-peptide.
2. Proglucagon: PC1/3 cleaves proglucagon to generate glucagon-like peptide-1 (GLP-1), glucagon-like peptide-2 (GLP-2), glicentin, and oxyntomodulin.
3. Proopiomelanocortin (POMC): PC1/3 processes POMC to generate adrenocorticotropic hormone (ACTH), β-lipotropin, β-endorphin, and melanocyte-stimulating hormones (MSH).
4. Prohormone convertase 2 (PCSK2) precursor: PC1/3 cleaves the PCSK2 precursor into its mature form.
5. Neuropeptide YY (NPY): PC1/3 processes NPY precursors to generate NPY and peptide YY (PYY).
6. Proghrelin: PC1/3 converts proghrelin into acylated ghrelin, which stimulates appetite, and desacyl ghrelin, which has no known function.
Defects in the PCSK1 gene can lead to various endocrine disorders, such as monogenic forms of diabetes (MODY), obesity, and short stature.
Proprotein convertase 2 (PCSK2) is a type of enzyme known as a proprotein convertase. It plays a role in the activation of other proteins by cleaving off specific peptide sequences and allowing them to become biologically active. PCSK2 is primarily involved in the processing of hormones and neurotransmitters, including insulin, prolactin, and members of the bombesin family.
Defects in the gene that encodes PCSK2 have been associated with certain medical conditions, such as congenital hyperinsulinism, a disorder characterized by low blood sugar levels due to excessive insulin secretion. However, more research is needed to fully understand the relationship between PCSK2 and these conditions.
Promethazine is an antihistamine and phenothiazine derivative, which is commonly used for its sedative, anti-emetic (prevents vomiting), and anti-allergic properties. It works by blocking the action of histamine, a substance in the body that causes allergic symptoms, and by blocking the action of dopamine, a neurotransmitter in the brain that helps transmit signals.
Promethazine is used to treat various conditions such as allergies, motion sickness, nausea and vomiting, and as a sedative before and after surgery or medical procedures. It may also be used for its calming effects in children with certain behavioral disorders.
Like all medications, promethazine can have side effects, including drowsiness, dry mouth, blurred vision, and dizziness. More serious side effects may include seizures, irregular heartbeat, and difficulty breathing. It is important to follow the instructions of a healthcare provider when taking promethazine and to report any unusual symptoms or side effects promptly.
Secretory vesicles are membrane-bound organelles found within cells that store and transport secretory proteins and other molecules to the plasma membrane for exocytosis. Exocytosis is the process by which these molecules are released from the cell, allowing them to perform various functions, such as communication with other cells or participation in biochemical reactions. Secretory vesicles can be found in a variety of cell types, including endocrine cells, exocrine cells, and neurons. The proteins and molecules contained within secretory vesicles are synthesized in the rough endoplasmic reticulum and then transported to the Golgi apparatus, where they are processed, modified, and packaged into the vesicles for subsequent release.
Neuropeptides are small protein-like molecules that are used by neurons to communicate with each other and with other cells in the body. They are produced in the cell body of a neuron, processed from larger precursor proteins, and then transported to the nerve terminal where they are stored in secretory vesicles. When the neuron is stimulated, the vesicles fuse with the cell membrane and release their contents into the extracellular space.
Neuropeptides can act as neurotransmitters or neuromodulators, depending on their target receptors and the duration of their effects. They play important roles in a variety of physiological processes, including pain perception, appetite regulation, stress response, and social behavior. Some neuropeptides also have hormonal functions, such as oxytocin and vasopressin, which are produced in the hypothalamus and released into the bloodstream to regulate reproductive and cardiovascular function, respectively.
There are hundreds of different neuropeptides that have been identified in the nervous system, and many of them have multiple functions and interact with other signaling molecules to modulate neural activity. Dysregulation of neuropeptide systems has been implicated in various neurological and psychiatric disorders, such as chronic pain, addiction, depression, and anxiety.
Cytoplasmic granules are small, membrane-bound organelles or inclusions found within the cytoplasm of cells. They contain various substances such as proteins, lipids, carbohydrates, and genetic material. Cytoplasmic granules have diverse functions depending on their specific composition and cellular location. Some examples include:
1. Secretory granules: These are found in secretory cells and store hormones, neurotransmitters, or enzymes before they are released by exocytosis.
2. Lysosomes: These are membrane-bound organelles that contain hydrolytic enzymes for intracellular digestion of waste materials, foreign substances, and damaged organelles.
3. Melanosomes: Found in melanocytes, these granules produce and store the pigment melanin, which is responsible for skin, hair, and eye color.
4. Weibel-Palade bodies: These are found in endothelial cells and store von Willebrand factor and P-selectin, which play roles in hemostasis and inflammation.
5. Peroxisomes: These are single-membrane organelles that contain enzymes for various metabolic processes, such as β-oxidation of fatty acids and detoxification of harmful substances.
6. Lipid bodies (also called lipid droplets): These are cytoplasmic granules that store neutral lipids, such as triglycerides and cholesteryl esters. They play a role in energy metabolism and intracellular signaling.
7. Glycogen granules: These are cytoplasmic inclusions that store glycogen, a polysaccharide used for energy storage in animals.
8. Protein bodies: Found in plants, these granules store excess proteins and help regulate protein homeostasis within the cell.
9. Electron-dense granules: These are found in certain immune cells, such as mast cells and basophils, and release mediators like histamine during an allergic response.
10. Granules of unknown composition or function may also be present in various cell types.
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.
Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.
The adrenal medulla is the inner part of the adrenal gland, which is located on top of the kidneys. It is responsible for producing and releasing hormones such as epinephrine (also known as adrenaline) and norepinephrine (also known as noradrenaline). These hormones play a crucial role in the body's "fight or flight" response, preparing the body for immediate action in response to stress.
Epinephrine increases heart rate, blood pressure, and respiratory rate, while also increasing blood flow to muscles and decreasing blood flow to the skin and digestive system. Norepinephrine has similar effects but is generally less potent than epinephrine. Together, these hormones help to prepare the body for physical activity and increase alertness and focus.
Disorders of the adrenal medulla can lead to a variety of symptoms, including high blood pressure, rapid heart rate, anxiety, and tremors. Some conditions that affect the adrenal medulla include pheochromocytoma, a tumor that causes excessive production of epinephrine and norepinephrine, and neuroblastoma, a cancerous tumor that arises from immature nerve cells in the adrenal gland.
The anterior pituitary, also known as the adenohypophysis, is the front portion of the pituitary gland. It is responsible for producing and secreting several important hormones that regulate various bodily functions. These hormones include:
* Growth hormone (GH), which stimulates growth and cell reproduction in bones and other tissues.
* Thyroid-stimulating hormone (TSH), which regulates the production of thyroid hormones by the thyroid gland.
* Adrenocorticotropic hormone (ACTH), which stimulates the adrenal glands to produce cortisol and other steroid hormones.
* Follicle-stimulating hormone (FSH) and luteinizing hormone (LH), which regulate reproductive function in both males and females by controlling the development and release of eggs or sperm.
* Prolactin, which stimulates milk production in pregnant and nursing women.
* Melanocyte-stimulating hormone (MSH), which regulates skin pigmentation and appetite.
The anterior pituitary gland is controlled by the hypothalamus, a small region of the brain located just above it. The hypothalamus produces releasing and inhibiting hormones that regulate the secretion of hormones from the anterior pituitary. These hormones are released into a network of blood vessels called the portal system, which carries them directly to the anterior pituitary gland.
Damage or disease of the anterior pituitary can lead to hormonal imbalances and various medical conditions, such as growth disorders, thyroid dysfunction, adrenal insufficiency, reproductive problems, and diabetes insipidus.
The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.
The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.
The Golgi apparatus performs several essential functions in the cell:
1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.
In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.
Carboxypeptidase H is also known as carboxypeptidase E or CPE. It is an enzyme that plays a role in the processing and activation of neuropeptides, which are small protein-like molecules that function as chemical messengers within the nervous system. Carboxypeptidase H/E is responsible for removing certain amino acids from the end of newly synthesized neuropeptides, allowing them to become biologically active. It is widely expressed in the brain and other tissues throughout the body.
Neuroblastoma is defined as a type of cancer that develops from immature nerve cells found in the fetal or early postnatal period, called neuroblasts. It typically occurs in infants and young children, with around 90% of cases diagnosed before age five. The tumors often originate in the adrenal glands but can also arise in the neck, chest, abdomen, or spine. Neuroblastoma is characterized by its ability to spread (metastasize) to other parts of the body, including bones, bone marrow, lymph nodes, and skin. The severity and prognosis of neuroblastoma can vary widely, depending on factors such as the patient's age at diagnosis, stage of the disease, and specific genetic features of the tumor.
Endocrine glands are ductless glands in the human body that release hormones directly into the bloodstream, which then carry the hormones to various tissues and organs in the body. These glands play a crucial role in regulating many of the body's functions, including metabolism, growth and development, tissue function, sexual function, reproduction, sleep, and mood.
Examples of endocrine glands include the pituitary gland, thyroid gland, parathyroid glands, adrenal glands, pineal gland, pancreas, ovaries, and testes. Each of these glands produces specific hormones that have unique effects on various target tissues in the body.
The endocrine system works closely with the nervous system to regulate many bodily functions through a complex network of feedback mechanisms. Disorders of the endocrine system can result in a wide range of symptoms and health problems, including diabetes, thyroid disease, growth disorders, and sexual dysfunction.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Inflammatory demyelinating diseases of the central nervous system
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An ancestral variant of Secretogranin II confers regulation by PHOX2 transcription factors and association with hypertension. -...
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- Granin (chromogranin and secretogranin) is a protein family of regulated secretory proteins ubiquitously found in the cores of amine and peptide hormone and neurotransmitter dense-core secretory vesicles. (wikipedia.org)
- chromogranin A (CgA) chromogranin B (CgB) secretogranin II (SgII) (see also secretoneurin) secretogranin III (SgIII) secretogranin V (SgV) Some other proteins are also proposed to belong to the granins based on their physico-chemical properties. (wikipedia.org)
- Chromogranins (Cgs) constitute a family of acidic glycopro- teins encompassing chromogranin A (CgA), chromogranin B (CgB) and secretograninII (SgII) that arewidely distributedin neuroendocrine tissues where they are packaged in secretory gran- ules. (123dok.net)
- Secretoneurin, self-regulates a pornographic catalog description read from secretogranin II( chromogranin C, CHGC). (bbandservices.com)
- It belongs to the family of granins that includes chromogranin B, chromogranin C, and secretogranin II. (medscape.com)
- Chromogranin A contains multiple cleavage sites, which undergo a tissue-specific proteolytic process, leading to the production of many biologically active peptides including vasostatin I, vasostatin II, pancreastatin, catestatin, parastatin, and serpinin. (medscape.com)
- We identified CS modifications of chromogranin-A (CgA), islet amyloid polypeptide, secretogranin-1 and secretogranin-2, immunoglobulin superfamily member 10, and protein AMBP. (scilifelab.se)
- Secretoneurin is a 33-amino acid neuropeptide produced by the endoproteolytic cleavage of chromogranin/secretogranin proteins. (biovendor.com)
- Description: The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. (postgenomeconsortium.com)
- To investigate the events involved in regulation of the secretogranin II (SgII) gene, luciferase reporter constructs were transfected into gonadotrope-derived, αT3-1 cells. (elsevierpure.com)
- Aims: Inflammation has been linked to the development of diabetic retinopathy (DR). Chromogranins A, B (CgA, CgB) and secretogranin II (SgII), are prohormones overexpressed in inflammatory diseases. (unisr.it)
- Other markers that can be helpful but are of more limited use include neuron-specific enolase, proconvertases PC1/PC3 and PC2, bombesin and/or gastrin-releasing peptide (GRP), CD57 (Leu-7/HNK-1), synaptic vesicle protein 2, PGP9.5, and others ( 11 ). (basicmedicalkey.com)
- Expression of the desmosomal protein Desmoglein-2 was reduced in pediatric dilated cardiomyopathy pediatric patients. (cusabio.com)
- Additional HS sites were found on syndecan-1, syndecan-4, nerurexin-2, protein NDNF and testican-1. (scilifelab.se)
- 001 medial aspect on sexual dimorphisms in protein degradation of secretogranins. (notinovedades.com)
- also known as ASH1), neurogenic differentiation factor 1 (NeuroD1), yes-associated protein 1 (YAP1) and POU class 2 homeobox 3 (POU2F3). (cancerindex.org)
- microfibril associated protein 2 [Sou. (gsea-msigdb.org)
- Granins (chromogranins or secretogranins) are acidic proteins and are present in the secretory granules of a wide variety of endocrine and neuro-endocrine cells. (wikipedia.org)
- The aim of this study was to comprehensively identify proteins that are enriched in amyloid plaques using unbiased proteomics in two subtypes of early onset AD: sporadic early onset AD (EOAD) and Down Syndrome (DS) with AD. (researchsquare.com)
- Proteins from the vasopressin prohormone along with secretogranin-2 are usually related to magnocellular nerves, although neurokinin A, peptide L, along with neurokinin B are attributed to classy hippocampal neurons. (mrt67307inhibitor.com)
- At least two mutations in the GNAS gene have been identified in people with primary macronodular adrenal hyperplasia (PMAH), a disorder that causes multiple lumps (nodules) to form in the adrenal glands, which are small hormone-producing glands located on top of each kidney. (medlineplus.gov)
- For a small subset of genes, however, only one of the two gene copies is active. (medlineplus.gov)
- However, the close proximity (14 kb) of two oppositely expressed promoter regions is unusual. (thermofisher.com)
- Description: A competitive inhibition quantitative ELISA assay kit for detection of Rabbit Angiotensin II (AngII) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (allelisakits.com)
- angiotensin II receptor type 1 [Sourc. (gsea-msigdb.org)
- Additionally, we identified two HS-modified prohormones (CgA and secretogranin-1), which was surprising, as prohormones are not typically regarded as HSPGs. (scilifelab.se)
- Wehavepreviouslydemonstratedthatmeasurementoftissuecon- centration of the novel secretogranin II-derived peptide EM66 may help to discriminate between benign and malignant pheo- chromocytomas.Theaimofthepresentstudywastocharacterize EM66inplasmaandurineofhealthyvolunteersandpheochromo- cytomapatients,inordertofurtherevaluatetheusefulnessofthis peptide as a circulating marker for the management of the tumors. (123dok.net)
- Cumulative evidences suggest that CgA's derived peptides are involved in a wide range of activities, like regulation of blood pressure (catestatin), glucose metabolism (pancreastatin, catestatin), neuroprotection (serpinin), and tumor angiogenesis (vasostatin I, vasostatin II). (medscape.com)
- An ancestral variant of Secretogranin II confers regulation by PHOX2 transcription factors and association with hypertension. (aravindachakravartilab.org)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human C-Type Lectin Domain Family 2, Member C (CLEC2C) in samples from serum, plasma, tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (allelisakits.com)
- The homozygous desmoglein 2 variant c.1003A;G co-segregated with Arrhythmogenic right ventricular cardiomyopathy, indicating autosomal recessive inheritance and complete penetrance. (cusabio.com)
- The Quantification comes a list of secretogranin II including number Figures 154 to 186. (bbandservices.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human C-Type Lectin Domain Family 2, Member C (CLEC2C) in serum, plasma, tissue homogenates, cell lysates and other biological fluids. (allelisakits.com)
- Description: A sandwich ELISA kit for detection of C-Type Lectin Domain Family 2, Member C from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (allelisakits.com)
- Two of the putative interactors, EBP and OSBPL2/ORP2, have sterol substrates. (bvsalud.org)
- collagen type I alpha 2 chain [Source. (gsea-msigdb.org)
- To further investigate the molecular basis of this notion, we use two methods to inhibit E-cadherin function that distinguish between E-cadherin's cell-cell adhesion and intracellular signaling functions. (gsea-msigdb.org)
- The highest theory folks think saved in the full tiger, required by s error and chronic vital Blueprint( 2- to well-and-good lower universities in smokeless % rituals was). (bbandservices.com)
- Molecular and Cellular Endocrinology , 199 (1-2), 29-36. (elsevierpure.com)
- Whole cell lysates (30 µg lysate) of Jurkat (Lane 1), ACHN (Lane 2), A549 (Lane 3), MCF7 (Lane 4), MDA-MB-231 (Lane 5), OVCAR-3 (Lane 6), HepG2 (Lane 7), tissue lysates (30 µg lysate) of Mouse Brain (Lane 8), Mouse Adipose (Lane 9) and Rat Brain (Lane 10) were electrophoresed using NuPAGE® 10 % Bis-Tris gel (Product # NP0302BOX). (thermofisher.com)
- this region includes two cysteine residues involved in a disulfide bond. (wikipedia.org)
- Medicine (Baltimore).1996;75(2):53-63. (asean-endocrinejournal.org)
- Short term: Store at 2-8°C. Long term: Aliquot and store at -20°C. Avoid freeze/thaw cycles. (lsbio.com)
- Store at 4°C if entire vial will be used within 2-4 weeks. (angioproteomie.com)
- Store the complete kit at 2-8°C. Under these conditions, the kit is stable until the expiration date (see label on the box). (biovendor.com)
- adrenoceptor beta 2 [Source:HGNC Symb. (gsea-msigdb.org)
- Necrolytic migratory erythema associated with glucagonoma: A report of 2 cases. (asean-endocrinejournal.org)
- Feyrter ( 2 ) considered the clear cells of the gastrointestinal tract to be peripheral endocrine or paracrine cells. (basicmedicalkey.com)