Caveolae
Caveolin 1
Caveolins
Caveolin 2
Caveolin 3
beta-Cyclodextrins
Membrane Microdomains
Cell Membrane
Cyclodextrins
Endocytosis
Membrane Proteins
Cholesterol
Microscopy, Immunoelectron
Nystatin
Signal Transduction
Cells, Cultured
Cell Compartmentation
Clathrin
Endothelium, Vascular
Endothelial Cells
Microscopy, Electron
Protein Transport
Coated Vesicles
Long QT Syndrome
Electrocardiography
Congenital Disorders of Glycosylation
Ether-A-Go-Go Potassium Channels
Syncope
Arrhythmias, Cardiac
Manganese Poisoning
Schools, Veterinary
Manganese
alpha-Synuclein
Veterinary Medicine
Presence of oxidized cholesterol in caveolae uncouples active platelet-derived growth factor receptors from tyrosine kinase substrates. (1/744)
Platelet-derived growth factor receptor beta (PDGFRbeta) in fibroblasts is concentrated in caveolae where it controls the tyrosine phosphorylation of multiple proteins. Caveolae are enriched in cholesterol and sphingolipids, but the role of these lipids in PDGFR signal transduction is unknown. We report that introduction of cholest-4-en-3-one into caveolae membranes uncouples PDGFR autophosphorylation from tyrosine phosphorylation of neighboring proteins. Cholest-4-en-3-one appears to interfere with the normal interaction between PDGFR and its partners. The results suggest that tightly packed caveolae lipids form a membrane platform that functions as a lipid scaffold for organizing the molecular interactions of multiple signaling pathways. (+info)Agonist-modulated targeting of the EDG-1 receptor to plasmalemmal caveolae. eNOS activation by sphingosine 1-phosphate and the role of caveolin-1 in sphingolipid signal transduction. (2/744)
Plasmalemmal caveolae are membrane microdomains that are specifically enriched in sphingolipids and contain a wide array of signaling proteins, including the endothelial isoform of nitric-oxide synthase (eNOS). EDG-1 is a G protein-coupled receptor for sphingosine 1-phosphate (S1P) that is expressed in endothelial cells and has been implicated in diverse vascular signal transduction pathways. We analyzed the subcellular distribution of EDG-1 in COS-7 cells transiently transfected with cDNA constructs encoding epitope-tagged EDG-1. Subcellular fractionation of cell lysates resolved by ultracentrifugation in discontinuous sucrose gradients revealed that approximately 55% of the EDG-1 protein was recovered in fractions enriched in caveolin-1, a resident protein of caveolae. Co-immunoprecipitation experiments showed that EDG-1 could be specifically precipitated by antibodies directed against caveolin-1 and vice versa. The targeting of EDG-1 to caveolae-enriched fractions was markedly increased (from 51 +/- 11% to 93 +/- 14%) by treatment of transfected cells with S1P (5 microm, 60 min). In co-transfection experiments expressing EDG-1 and eNOS cDNAs in COS-7 cells, we found that S1P treatment significantly and specifically increased nitric-oxide synthase activity, with an EC(50) of 30 nm S1P. Overexpression of transfected caveolin-1 cDNA together with EDG-1 and eNOS markedly diminished S1P-mediated eNOS activation; caveolin overexpression also attenuated agonist-induced phosphorylation of EDG-1 receptor by >90%. These results suggest that the interaction of the EDG-1 receptor with caveolin may serve to inhibit signaling through the S1P pathway, even as the targeting of EDG-1 to caveolae facilitates the interactions of this receptor with ligands and effectors that are also targeted to caveolae. The agonist-modulated targeting of EDG-1 to caveolae and its dynamic inhibitory interactions with caveolin identify new points for regulation of sphingolipid-dependent signaling in the vascular wall. (+info)Scavenger receptor BI transfers major lipoprotein-associated phospholipids into the cells. (3/744)
The phospholipids of lipoproteins can be transferred to cells by an endocytosis-independent uptake pathway. We analyzed the role of scavenger receptor BI (SR-BI) for the selective cellular phospholipid import. Human monocytes rapidly acquired the pyrene (py)-labeled phospholipids sphingomyelin (SM), phosphatidylcholine, and phosphatidylethanolamine from different donors (low and high density lipoproteins (LDL, HDL), lipid vesicles). The anti-SR-BI antibody directed against the extracellular loop of the membrane protein lowered the cellular import of the phospholipids by 40-80%. The phospholipid transfer from the lipid vesicles into the monocytes was suppressed by LDL, HDL, and apoprotein AI. Transfection of BHK cells with the cDNA for human SR-BI enhanced the cellular import of the vesicle-derived py-phospholipids by 5-6-fold. In the case of the LDL donors, transfer of py-SM to the transfected cells was stimulated to a greater extent than the uptake of the other py-phospholipids. Similar differences were not observed when the vesicles and HDL were used as phospholipid donors. The concentration of LDL required for the half-maximal phospholipid import was close to the previously reported apparent dissociation constant for LDL binding to SR-BI. The low activation energy of the SR-BI-mediated py-phospholipid import indicated that the transfer occurs entirely in a hydrophobic environment. Disruption of cell membrane caveolae by cyclodextrin treatment reduced the SR-BI-catalyzed incorporation of py-SM, suggesting that intact caveolae are necessary for the phospholipid uptake. In conclusion, SR-BI mediates the selective import of the major lipoprotein-associated phospholipids into the cells, the transfer efficiency being dependent on the structure of the donor lipoprotein. (+info)Isoforms of caveolin-1 and caveolar structure. (4/744)
The relationship between caveolin-1 isoforms alpha and beta and caveolar ultrastructure was studied. By immunofluorescence microscopy of human fibroblasts, caveolae were observed as dots positive for caveolin-1, but many dots labeled by an antibody recognizing both isoforms (anti-alphabeta) were not labeled by another antibody specific for the alpha isoform (anti-alpha). Immunogold electron microscopy of freeze-fracture replicas revealed caveolae of different depths, and indicated that anti-alpha labeled deep caveolae preferentially over shallow ones, whereas anti-alphabeta labeled both forms with an equivalent frequency and intensity. The presence of the beta isoform in deep caveolae was confirmed by labeling epitope-tagged beta-caveolin. When made to be expressed in HepG2 cells lacking endogenous caveolins, the alpha isoform formed caveolar depressions efficiently, but the beta isoform hardly did so. Caveolae were also formed in cells expressing the two isoforms, but their frequency was variable among cells of the same clone. Coexpression of caveolin-1 and caveolin-2 caused more efficient formation of deep caveolae than caveolin-1 alone. The result indicates that the two isoforms of caveolin-1 have a different potential for forming caveolae structure, and more importantly, that deep and shallow caveolae may be diversified in their molecular composition. (+info)Ultrastructural and histochemical characterization of special muscle cells in the monkey small intestine. (5/744)
The ultrastructure, three-dimensional arrangement, and histochemical features of special muscle cells in the monkey small intestine were investigated. The cells formed a special layer separated from the main part by a connective tissue space along the submucosal surface of the circular muscle coat. Scanning electron microscopy using alkali maceration demonstrated this inner sublayer to be a continuous thin sheet consisting of irregularly-shaped muscle cells equipped with many cytoplasmic projections and caveolae. Other ultrastructural features included direct contact with interstitial cells, due to their close association with nerve fibers of the deep muscular plexus. Histochemical examination revealed significant alkaline phosphatase activity and immunoreactivity for vascular smooth muscle alpha actin in these muscle cells, whereas the ordinary circular muscle cells were immunopositive for enteric smooth muscle gamma actin. These findings suggest that the special muscle cells play an important role in regulating the radial stretch of the monkey small intestinal wall. (+info)Bradykinin activates the Janus-activated kinase/signal transducers and activators of transcription (JAK/STAT) pathway in vascular endothelial cells: localization of JAK/STAT signalling proteins in plasmalemmal caveolae. (6/744)
Bradykinin (BK) is an important physiological regulator of endothelial cell function. In the present study, we have examined the role of the Janus-activated kinase (JAK)/signal transducers and activators of transcription (STAT) pathway in endothelial signal transduction through the BK B2 receptor (B2R). In cultured bovine aortic endothelial cells (BAECs), BK activates Tyk2 of the JAK family of tyrosine kinases. Activation results in the tyrosine phosphorylation and subsequent nuclear translocation of STAT3. BK also activates the mitogen-activated p44 and p42 protein kinases, resulting in STAT3 serine phosphorylation. Furthermore, Tyk2 and STAT3 form a complex with the B2R in response to BK stimulation. Under basal conditions, Tyk2, STAT3 and the B2R are localized either partially or entirely in endothelial plasmalemmal caveolae. Following BK stimulation of BAECs, however, the B2R and STAT3 are translocated out of caveolae. Taken together, these data suggest that BK activates the JAK/STAT pathway in endothelial cells and that JAK/STAT signalling proteins are localized in endothelial caveolae. Moreover, caveolar localization of the B2R and STAT3 appears to be regulated in an agonist-dependent manner. (+info)Differential targeting of beta -adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the cAMP signaling pathway. (7/744)
Differential modes for beta(1)- and beta(2)-adrenergic receptor (AR) regulation of adenylyl cyclase in cardiomyocytes is most consistent with spatial regulation in microdomains of the plasma membrane. This study examines whether caveolae represent specialized subdomains that concentrate and organize these moieties in cardiomyocytes. Caveolae from quiescent rat ventricular cardiomyocytes are highly enriched in beta(2)-ARs, Galpha(i), protein kinase A RIIalpha subunits, caveolin-3, and flotillins (caveolin functional homologues); beta(1)-ARs, m(2)-muscarinic cholinergic receptors, Galpha(s), and cardiac types V/VI adenylyl cyclase distribute between caveolae and other cell fractions, whereas protein kinase A RIalpha subunits, G protein-coupled receptor kinase-2, and clathrin are largely excluded from caveolae. Cell surface beta(2)-ARs localize to caveolae in cardiomyocytes and cardiac fibroblasts (with markedly different beta(2)-AR expression levels), indicating that the fidelity of beta(2)-AR targeting to caveolae is maintained over a physiologic range of beta(2)-AR expression. In cardiomyocytes, agonist stimulation leads to a marked decline in the abundance of beta(2)-ARs (but not beta(1)-ARs) in caveolae. Other studies show co-immunoprecipitation of cardiomyocytes adenylyl cyclase V/VI and caveolin-3, suggesting their in vivo association. However, caveolin is not required for adenylyl cyclase targeting to low density membranes, since adenylyl cyclase targets to low buoyant density membrane fractions of HEK cells that lack prototypical caveolins. Nevertheless, cholesterol depletion with cyclodextrin augments agonist-stimulated cAMP accumulation, indicating that caveolae function as negative regulators of cAMP accumulation. The inhibitory interaction between caveolae and the cAMP signaling pathway as well as domain-specific differences in the stoichiometry of individual elements in the beta-AR signaling cascade represent important modifiers of cAMP-dependent signaling in the heart. (+info)Downmodulation of caveolin-1 expression in human ovarian carcinoma is directly related to alpha-folate receptor overexpression. (8/744)
Caveolin (cav-1) and the GPI-anchored alpha-folate receptor (alphaFR) are membrane proteins both found associated to caveolar structures. Several studies in tumor cells independently reported cav-1 downregulation and alphaFR overexpression. Here we analysed the expression of the two molecules in normal and tumor ovarian samples derived from fresh specimens and from cultured cell lines. Whereas normal ovary surface epithelial cells displayed only cav-1 expression, ovarian tumor surgical samples and cell lines (COR, IGROV1, OVCAR3 and OVCA432) displayed high alphaFR and low-level or no cav-1 expression, except those cell lines (SKOV3 and SW626) with the lower alphaFR expression. SKOV3, but not two alphaFR-negative non-ovarian cell lines, exhibited down-regulation of cav-1 expression following stable alphaFR cDNA transfection. Conversely, cav-1 transfection in IGROV1 cells led to downregulated alphaFR expression, together with formation of caveolar structures and reduction of growth capability. Moreover, cav-1 expression was induced in IGROV1 cells by transfection with intracellular anti-alphaFR antibodies to downmodulate alphaFR expression. In cav-1 transfected cells, transcriptional activity of the alphaFR-specific promoter P1 was reduced by 70% and an additional specific DNA-protein complex was identified by gel-shift assay, indicating that cav-1 expression influences alphaFR gene transcription. Together these results support the notion that alphaFR and cav-1 protein expression is reciprocally regulated in ovary cancer cells. (+info)Caveolin 1 is a protein that is primarily found in the plasma membrane of cells. It is a structural protein that helps to form small, flask-shaped invaginations in the membrane called caveolae. Caveolae are involved in a variety of cellular processes, including signal transduction, cholesterol homeostasis, and endocytosis. Caveolin 1 is also involved in the development and progression of certain diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. In some cases, changes in the expression or function of caveolin 1 can contribute to the development of these diseases. For example, some studies have suggested that increased levels of caveolin 1 may be associated with an increased risk of cancer, while decreased levels may be associated with cardiovascular disease. Overall, caveolin 1 is an important protein that plays a role in many cellular processes and is involved in the development and progression of certain diseases.
Caveolins are a family of proteins that are primarily found in the plasma membrane of cells. They are involved in the formation of specialized structures called caveolae, which are small invaginations in the plasma membrane that are involved in a variety of cellular processes, including signal transduction, endocytosis, and cholesterol homeostasis. There are three known caveolin genes in humans, which encode for three different caveolin proteins: caveolin-1, caveolin-2, and caveolin-3. Caveolin-1 is the most widely expressed of the three and is found in many different cell types, including epithelial cells, endothelial cells, and muscle cells. Caveolin-2 is primarily expressed in epithelial cells and muscle cells, while caveolin-3 is primarily expressed in muscle cells. Caveolins have been implicated in a variety of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, mutations in the caveolin-1 gene have been associated with certain types of cancer, while changes in the expression of caveolin-2 have been linked to the development of atherosclerosis. Additionally, caveolins have been shown to play a role in the pathogenesis of Huntington's disease and other neurodegenerative disorders.
Caveolin 2 is a protein that is found in the plasma membrane of cells. It is a component of caveolae, which are small, flask-shaped invaginations of the plasma membrane that are involved in a variety of cellular processes, including signal transduction, cholesterol homeostasis, and endocytosis. Caveolin 2 is encoded by the "CAV2" gene and is expressed in many different types of cells, including epithelial cells, endothelial cells, and smooth muscle cells. It plays a role in the regulation of intracellular signaling pathways and has been implicated in a number of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.
Caveolin 3 is a protein that is primarily expressed in skeletal muscle cells. It is a component of caveolae, which are small, flask-shaped invaginations of the plasma membrane that are involved in various cellular processes, including signal transduction, cholesterol homeostasis, and endocytosis. In the medical field, caveolin 3 is often studied in the context of muscle diseases, particularly those that affect skeletal muscle. Mutations in the caveolin 3 gene have been associated with a number of muscle disorders, including limb-girdle muscular dystrophy type 2A (LGMD2A), which is a progressive muscle wasting disorder that primarily affects the muscles of the shoulders and hips. Caveolin 3 is also involved in the development and function of muscle fibers, and changes in its expression or function have been linked to various other muscle disorders, as well as to cancer and other diseases.
Beta-cyclodextrins (β-CD) are a type of cyclic oligosaccharide composed of seven glucose units linked by α-1,4-glycosidic bonds. They are commonly used in the medical field as a drug delivery system to improve the solubility, stability, and bioavailability of poorly water-soluble drugs. β-CD forms inclusion complexes with a wide range of hydrophobic molecules, including drugs, by encapsulating them within the hydrophobic cavity of the cyclodextrin molecule. This results in an increase in the solubility of the drug and a reduction in its toxicity. β-CD can also enhance the stability of drugs by protecting them from degradation and improving their shelf life. In addition to their use as drug delivery agents, β-CDs have also been used in medical imaging, as contrast agents for magnetic resonance imaging (MRI) and computed tomography (CT) scans. They have also been used in the treatment of certain medical conditions, such as inflammatory bowel disease and irritable bowel syndrome. Overall, β-CDs have a wide range of applications in the medical field, and their use is expected to continue to grow as researchers discover new ways to harness their unique properties.
Cyclodextrins are a group of cyclic oligosaccharides that are commonly used in the medical field as pharmaceutical excipients. They are composed of glucose units linked by α-1,4-glycosidic bonds to form a torus-shaped molecule with a hydrophobic central cavity and hydrophilic outer surface. Cyclodextrins have the ability to form inclusion complexes with a wide range of hydrophobic molecules, including drugs, lipids, and other bioactive compounds. By encapsulating these molecules within the hydrophobic cavity of the cyclodextrin, they can improve their solubility, stability, and bioavailability. In the medical field, cyclodextrins are used as solubilizing agents, stabilizers, and permeation enhancers in various pharmaceutical formulations, such as tablets, capsules, and topical creams. They are also used as carriers for drug delivery systems, such as nanoparticles and liposomes, to improve the targeted delivery of drugs to specific tissues or organs. Cyclodextrins have also been studied for their potential therapeutic applications, such as in the treatment of cancer, diabetes, and infectious diseases. They have been shown to have anti-inflammatory, anti-cancer, and anti-viral properties, and are being investigated as potential adjuvants for vaccines and immunotherapies.
Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.
Cholesterol is a waxy, fat-like substance that is produced by the liver and is also found in some foods. It is an essential component of cell membranes and is necessary for the production of hormones, bile acids, and vitamin D. However, high levels of cholesterol in the blood can increase the risk of developing heart disease and stroke. There are two main types of cholesterol: low-density lipoprotein (LDL) cholesterol, which is often referred to as "bad" cholesterol because it can build up in the walls of arteries and lead to plaque formation, and high-density lipoprotein (HDL) cholesterol, which is often referred to as "good" cholesterol because it helps remove excess cholesterol from the bloodstream and transport it back to the liver for processing.
Nystatin is an antifungal medication that is used to treat a variety of fungal infections, including candidiasis (a yeast infection that can affect the mouth, throat, esophagus, vagina, and skin), dermatophytosis (a fungal infection of the skin caused by dermatophytes), and oropharyngeal candidiasis (a yeast infection of the mouth and throat). It works by inhibiting the growth of fungi and is available in various forms, including creams, ointments, tablets, and suspensions. Nystatin is generally considered safe and well-tolerated, but it can cause side effects such as nausea, vomiting, and diarrhea. It is important to follow the instructions of a healthcare provider when using nystatin and to complete the full course of treatment, even if symptoms improve before the medication is finished.
Clathrin is a protein that plays a crucial role in the process of endocytosis, which is the process by which cells take in substances from their environment. Clathrin forms a lattice-like structure that surrounds and helps to shape the plasma membrane as it buds inward to form a vesicle. This vesicle then pinches off from the plasma membrane and is transported into the cell, where it can be processed and used by the cell. Clathrin is also involved in the transport of certain molecules within the cell, such as the transport of proteins from the Golgi apparatus to the plasma membrane. In the medical field, clathrin is often studied in relation to diseases such as cancer, where it has been implicated in the formation of abnormal blood vessels and the spread of cancer cells.
Long QT Syndrome (LQTS) is a rare genetic disorder that affects the heart's electrical activity, specifically the time it takes for the heart to recharge between beats. In individuals with LQTS, the QT interval on an electrocardiogram (ECG) is prolonged, which can lead to abnormal heart rhythms and potentially life-threatening arrhythmias, such as torsades de pointes. LQTS is caused by mutations in genes that regulate the flow of ions across the heart's cell membranes. These mutations can disrupt the normal balance of ions, leading to abnormal electrical activity in the heart. The severity of LQTS can vary widely, with some individuals experiencing only mild symptoms and others experiencing severe symptoms or even sudden cardiac death. Treatment for LQTS typically involves medications to slow the heart rate and prevent abnormal heart rhythms, as well as lifestyle changes such as avoiding certain triggers that can worsen symptoms. In some cases, individuals with LQTS may require an implantable cardioverter-defibrillator (ICD) to detect and treat life-threatening arrhythmias.
KCNQ1 potassium channel is a type of ion channel that is responsible for regulating the flow of potassium ions across cell membranes. It is encoded by the KCNQ1 gene and is expressed in various tissues throughout the body, including the heart, brain, and skeletal muscle. In the heart, KCNQ1 potassium channels play a critical role in the regulation of heart rate and rhythm. They help to maintain the resting membrane potential of cardiac cells and are involved in the repolarization phase of the cardiac action potential. Mutations in the KCNQ1 gene can lead to long QT syndrome, a disorder characterized by abnormal heart rhythms and an increased risk of sudden cardiac death. In the brain, KCNQ1 potassium channels are involved in the regulation of neuronal excitability and the transmission of nerve impulses. They are also thought to play a role in the development and function of the nervous system. In skeletal muscle, KCNQ1 potassium channels are involved in the regulation of muscle contraction and relaxation. Mutations in the KCNQ1 gene can lead to myotonia, a disorder characterized by muscle stiffness and difficulty relaxing. Overall, KCNQ1 potassium channels play a critical role in the regulation of various physiological processes throughout the body and are an important target for the development of new treatments for a range of diseases and disorders.
Congenital Disorders of Glycosylation (CDG) are a group of rare genetic disorders that affect the way that sugars (called glycans) are attached to proteins in the body. These disorders can affect various organs and systems in the body, including the brain, liver, and nervous system. CDGs are caused by mutations in genes that are involved in the process of glycosylation, which is the addition of sugars to proteins. These mutations can result in the production of abnormal proteins that are not properly glycosylated, leading to a wide range of symptoms and complications. The symptoms of CDGs can vary widely depending on the specific type of disorder and the severity of the condition. Some common symptoms include developmental delays, intellectual disability, seizures, hypotonia (low muscle tone), and problems with feeding and growth. CDGs are typically diagnosed through a combination of clinical evaluation, genetic testing, and laboratory tests that measure the levels of specific sugars in the body. Treatment for CDGs may involve a range of interventions, including dietary modifications, medications, and supportive therapies to manage symptoms and complications.
Ether-a-go-go potassium channels, also known as KCNH channels, are a family of ion channels that are important for regulating the electrical activity of cells, particularly in the heart and nervous system. These channels are named after the fact that they were first identified in the African clawed frog (Xenopus laevis) and were found to be activated by the volatile anesthetic ether. There are several different subtypes of ether-a-go-go potassium channels, each with its own unique properties and functions. Some of the most well-known subtypes include the ether-a-go-go potassium channel 1 (KCNH1) and the ether-a-go-go potassium channel 2 (KCNH2), which are both expressed in the heart and play important roles in regulating the electrical activity of cardiac cells. In the heart, ether-a-go-go potassium channels help to maintain the normal rhythm of electrical activity by allowing potassium ions to flow out of cardiac cells. This helps to repolarize the cell membrane and restore it to its resting state, which is necessary for the heart to contract and pump blood effectively. In the nervous system, ether-a-go-go potassium channels are thought to play a role in regulating the excitability of neurons and may be involved in the development and progression of certain neurological disorders. For example, mutations in the KCNH2 gene, which encodes the ether-a-go-go potassium channel 2, have been linked to long QT syndrome, a disorder that can cause abnormal heart rhythms and an increased risk of sudden cardiac death. Overall, ether-a-go-go potassium channels are an important class of ion channels that play a critical role in regulating the electrical activity of cells in the heart and nervous system.
Syncope is a medical condition characterized by a temporary loss of consciousness due to a lack of blood flow to the brain. It is also known as fainting or passing out. Syncope can be caused by a variety of factors, including low blood pressure, heart problems, anemia, dehydration, or certain medications. Symptoms of syncope may include dizziness, lightheadedness, weakness, and loss of consciousness. Treatment for syncope depends on the underlying cause and may include lifestyle changes, medications, or medical procedures.
Arrhythmias, cardiac refer to abnormal heart rhythms that are not synchronized with the electrical signals that control the heartbeat. These abnormal rhythms can be caused by a variety of factors, including structural abnormalities of the heart, damage to the heart muscle, or problems with the electrical conduction system of the heart. Arrhythmias can range from relatively harmless to life-threatening. Some common types of cardiac arrhythmias include atrial fibrillation, ventricular tachycardia, and atrial flutter. Symptoms of arrhythmias may include palpitations, shortness of breath, dizziness, or fainting. Treatment for arrhythmias may involve medications, lifestyle changes, or medical procedures such as catheter ablation or implantation of a pacemaker or defibrillator.
Manganese poisoning is a condition that occurs when a person is exposed to high levels of manganese over a prolonged period of time. Manganese is a naturally occurring element that is essential for human health in small amounts, but exposure to high levels of manganese can be harmful. Manganese poisoning can occur through inhalation of manganese dust or fumes, ingestion of contaminated water or food, or through skin absorption. Symptoms of manganese poisoning can include tremors, muscle weakness, memory loss, and difficulty with coordination and balance. In severe cases, manganese poisoning can lead to neurological damage and even death. Treatment for manganese poisoning typically involves removing the person from the source of exposure and providing supportive care to manage symptoms. In some cases, medications may be used to help manage symptoms or to speed up the elimination of manganese from the body. It is important to prevent manganese poisoning by taking steps to minimize exposure to high levels of this element.
Manganese is a chemical element with the symbol Mn and atomic number 25. It is a trace element that is essential for human health, but only in small amounts. In the medical field, manganese is primarily used to treat manganese toxicity, which is a condition that occurs when the body is exposed to high levels of manganese. Symptoms of manganese toxicity can include tremors, muscle weakness, and cognitive impairment. Treatment typically involves removing the source of exposure and providing supportive care to manage symptoms. Manganese is also used in some medical treatments, such as in the treatment of osteoporosis and in the production of certain medications.
Alpha-Synuclein is a protein that is found in nerve cells in the brain and spinal cord. It is involved in the normal functioning of these cells, and it is also a key component of Lewy bodies, which are abnormal protein aggregates that are found in the brains of people with Parkinson's disease and other neurodegenerative disorders. Alpha-Synuclein is thought to play a role in the development of these disorders by disrupting the normal functioning of nerve cells and leading to the formation of Lewy bodies.
In the medical field, metals are materials that are commonly used in medical devices, implants, and other medical applications. These metals can include stainless steel, titanium, cobalt-chromium alloys, and other materials that are known for their strength, durability, and biocompatibility. Metals are often used in medical devices because they can withstand the rigors of the human body and provide long-lasting support and stability. For example, metal implants are commonly used in orthopedic surgery to replace damaged or diseased joints, while metal stents are used to keep blood vessels open and prevent blockages. However, metals can also have potential risks and complications. For example, some people may be allergic to certain metals, which can cause skin irritation, inflammation, or other adverse reactions. Additionally, metal implants can sometimes cause tissue damage or infection, which may require additional medical treatment. Overall, the use of metals in the medical field is a complex and multifaceted issue that requires careful consideration of the benefits and risks involved.
Caveolae
Endocytosis
Robert Parton
Plasma membrane Ca2+ ATPase
Congenital generalized lipodystrophy
Major capsid protein VP1
Potocytosis
Pinocytosis
SDPR
Caveolin
Caveolin 3
FLOT1
Caveolin 1
ENTPD1
PTRF
Lipid raft
PACSIN2
DNA vaccine
EN1 (gene)
Alain Prochiantz
EN2 (gene)
Endothelial NOS
Channelosome
MAP3K2
Low-density lipoprotein receptor-related protein 8
Phospholipase D1
List of diminutives by language
Romano-Ward syndrome
Marilyn Farquhar
Polystyrene (drug delivery)
MedlinePlus: Genes: C
cavea - Wiktionary, the free dictionary
RANGRF RAN guanine nucleotide release factor [Homo sapiens (human)] - Gene - NCBI
Vauthey Research Group - Group Members
Caveolin-1 Polyclonal Antibody (600-401-J62)
Beth BRAGDON | Assistant professor | PhD | Boston University, MA | BU | Department of Orthopaedic Surgery | Research profile
Long QT Syndrome: Practice Essentials, Background, Etiopathophysiology
Identification of Caveolin Sequences involved in Anchorage-dependence of cell growth | ICASADEG | Project | Fact sheet | FP6 |...
Frontiers | Involvement of TGF-β and Autophagy Pathways in Pathogenesis of Diabetes: A Comprehensive Review on Biological and...
WikiGenes - ZANTAC - (E)-N-[2-[[5-(dimethylaminomethyl)-2...
Researchers Explore Link Between Metal Exposure and Parkinson's Symptoms - Neuroscience News
High-throughput, single-particle tracking reveals nested membrane domains that dictate KRasG12D diffusion and trafficking |...
Caveolin-1 in Cardiovascular Disease: A Double-Edged Sword | Diabetes | American Diabetes Association
NIOSHTIC-2 Search Results - Full View
Publications Citing Globals Software - Laboratory for Fluorescence Dynamics
G protein β interacts with the glucocorticoid receptor and suppresses its transcriptional activity in the nucleus | Journal of...
CNIC
Mechanics of development | Royal Society
DeCS - New terms
DeCS - Termos Novos
DeCS - Termos Novos
DeCS - New terms
DeCS - Termos Novos
DeCS - Termos Novos
DeCS - Términos Nuevos
DeCS - New terms
DeCS - Termos Novos
DeCS - New terms
Plasma membrane4
- Caveolin-1 (Cav-1), an anchoring protein in the plasma membrane caveolae in ECs and vascular smooth muscle cells (VSMCs), attenuates endothelial NO production by occupying the calcium/calmodulin (Ca 2+ /CaM) binding site of eNOS ( 4 ) ( Fig. 1 ). (diabetesjournals.org)
- In ECs, Cav-1 anchors eNOS in plasma membrane caveolae, which limits its translocation and phosphorylated activation and thereby reduces its capacity to generate NO ( 7 ) ( Fig. 1 ). (diabetesjournals.org)
- Caveolins can serve as protein markers of caveolae ('little caves'), invaginations in the plasma membrane 50-100 nanometers in diameter. (biomedcentral.com)
- Abstract Caveolin-1, the first member of caveolin family reported, is recognized as the structural component of caveola, a plasma membrane invagination or vesicles that are a subcompartment distinct from clathrin-coated pits. (techscience.com)
Structural component1
- Internalisation of Rac binding sites is mediated by caveolin-1, a structural component of a subtype of rafts termed caveolae. (europa.eu)
Protein1
- On the other hand, an increase in Ca 2+ induces eNOS translocation from the cell membrane to the cytosol or Golgi complex ( 8 ), where it is phosphorylated and fully activated by protein kinases that reside in caveolae, such as p38 mitogen-activated protein kinase, phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt), cAMP-dependent protein kinase A, and 5′ AMP-activated protein kinase ( 7 ). (diabetesjournals.org)
Cell2
- Integrin-mediated retention of phosphorylated caveolin in focal adhesions inhibits raft internalisation, which occurs upon its recruitment to caveolae after cell detachment. (europa.eu)
- Over-represented proteins were involved in the C-jun-amino-terminal kinase pathway, caveolae-mediated endocytosis signaling, cardiovascular-cancer-respiratory pathway, regulation of clathrin-mediated endocytosis, non-small cell lung cancer signaling, pulmonary hypertension, glutamate receptor, immune response and angiogenesis. (cdc.gov)
Lipid rafts3
- 16. Ethanol mimics ligand-mediated activation and endocytosis of IL-1RI/TLR4 receptors via lipid rafts caveolae in astroglial cells. (nih.gov)
- Caveolin-1 is a scaffolding protein of cholesterol-rich caveolae lipid rafts in the plasma membrane. (nih.gov)
- 2003. Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells. . (umass.edu)
Signal transduction1
- In addition to regulating cholesterol transport, caveolin-1 has the ability to bind a diverse array of cell signaling molecules and regulate cell signal transduction in caveolae. (nih.gov)
Endocytosis6
- Endocytosis pathways can be subdivided into four main categories: phagocytosis, macropinocitosis, caveolae-mediated and clathrin-mediated. (medscape.com)
- Entry of tiger frog virus (an Iridovirus) into HepG2 cells via a pH-dependent, atypical, caveola-mediated endocytosis pathway. (bvsalud.org)
- Taken together, our results demonstrated that TFV entry occurs by caveola -mediated endocytosis with a pH -dependent step. (bvsalud.org)
- This atypical caveola -mediated endocytosis is different from the clathrin -mediated endocytosis of frog virus 3 (FV3) by BHK cells , which has been recognized as a model for iridoviruses . (bvsalud.org)
- 12. Caveolae/raft-dependent endocytosis. (nih.gov)
- 15. Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids. (nih.gov)
Receptors2
- LDL receptors, caveolae and cholesterol in endothelial dysfunction: oxLDLs accomplices or victims? (biametrics.com)
- 11) It's #Transcytosis (an active process), through a vesicular pathway involving #caveolae , scavenger receptors ( #SRB1 ) and activin like receptor kinase 1 ( #ALK1 ). (cardiometabolic-ce.com)
Membrane4
- Caveolae are specialized membrane microdomains enriched in cholesterol and sphingolipids which are present in multiple cell types including cardiomyocytes. (nih.gov)
- Studies suggest that cavin-1 plays an essential role in forming and stabilizing caveolae, which are small pouches in the membrane that surrounds cells. (nih.gov)
- Western blot analysis of caveolar membrane fractions isolated by sucrose density centrifugation demonstrated that Hsp27 and Hsp70 were localized in caveolae. (nih.gov)
- 13. Plasma membrane cyclic nucleotide phosphodiesterase 3B (PDE3B) is associated with caveolae in primary adipocytes. (nih.gov)
Caveolin5
- CEES treatment also resulted in increased expression of caveolin-1, the major structural component of caveolae. (nih.gov)
- 10. Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated by targeting to lipid raft/caveolae and in mitotic endothelial cells. (nih.gov)
- Surprisingly, expression of the depolarization mutant in caveolin-1 null cells dramatically impeded caveolae formation. (cdc.gov)
- Furthermore, knockdown of caveolae formation by methyl-beta-cyclodextrin failed to prevent wild-type caveolin-1 rear polarization. (cdc.gov)
- Thus, we have identified a sequence motif that is essential for caveolin-1 rear polarization and caveolae formation. (cdc.gov)
Cholera1
- In addition, TFV virions colocalized with the cholera toxin subunit B , indicating that TFV enters as caveola -internalized cargo into the Golgi complex . (bvsalud.org)
Cholesterol2
- Oxidized LDL (OxLDL) can serve as a cholesterol acceptor (orange circles), thereby disrupting caveolae and eNOS function. (jci.org)
- However, in the presence of OxLDL, HDL maintains the total cholesterol content of caveolae by the provision of cholesterol ester (blue circles), resulting in preservation of the eNOS signaling module ( 29 - 31 ). (jci.org)
Cells1
- Implications of caveolae in testicular and epididymal myoid cells to sperm motility. (hal.science)
Role2
Essential2
- Caveolae are particularly numerous in adipocytes, where they appear to be essential for the normal transport, processing, and storage of fats. (nih.gov)
- 18. Caveolae facilitate but are not essential for platelet-activating factor-mediated calcium mobilization and extracellular signal-regulated kinase activation. (nih.gov)
Open1
- Caveolae assume various shapes from open pits to closed vesicles. (nih.gov)