Adaptor Protein Complex alpha Subunits
Coated Pits, Cell-Membrane
Adaptor Proteins, Vesicular Transport
Receptor, IGF Type 2
Electrophoresis, Agar Gel
Monomeric Clathrin Assembly Proteins
Adaptor Protein Complex 2
Adaptor Protein Complex 1
HSC70 Heat-Shock Proteins
Adaptor Protein Complex gamma Subunits
Adaptor Protein Complex beta Subunits
Adaptor Protein Complex mu Subunits
Vesicular Transport Proteins
ADP-Ribosylation Factor 1
Nerve Tissue Proteins
Molecular Sequence Data
Coat Protein Complex I
Adaptor Protein Complex sigma Subunits
Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Recombinant Fusion Proteins
Fluorescent Antibody Technique
HSP70 Heat-Shock Proteins
Centrifugation, Density Gradient
Internalization and sequestration of the human prostacyclin receptor. (1/386)Prostacyclin (PGI(2)), the major product of cyclooxygenase in macrovascular endothelium, mediates its biological effects through its cell surface G protein-coupled receptor, the IP. PKC-mediated phosphorylation of human (h) IP is a critical determinant of agonist-induced desensitization (Smyth, E. M., Hong Li, W., and FitzGerald, G. A. (1998) J. Biol. Chem. 273, 23258-23266). The regulatory events that follow desensitization are unclear. We have examined agonist-induced sequestration of hIP. Human IP, tagged at the N terminus with hemagglutinin (HA) and fused at the C terminus to the green fluorescent protein (GFP), was coupled to increased cAMP (EC(50) = 0.39 +/- 0.09 nm) and inositol phosphate (EC(50) = 86. 6 +/- 18.3 nm) generation when overexpressed in HEK 293 cells. Iloprost-induced sequestration of HAhIP-GFP, followed in real time by confocal microscopy, was partially colocalized to clathrin-coated vesicles. Iloprost induced a time- and concentration-dependent loss of cell surface HA, indicating receptor internalization, which was prevented by inhibitors of clathrin-mediated trafficking and partially reduced by cotransfection of cells with a dynamin dominant negative mutant. Sequestration (EC(50) = 27.6 +/- 5.7 nm) was evident at those concentrations of iloprost that induce PKC-dependent desensitization. Neither the PKC inhibitor GF109203X nor mutation of Ser-328, the site for PKC phosphorylation, altered receptor sequestration indicating that, unlike desensitization, internalization is PKC-independent. Deletion of the C terminus prevented iloprost-induced internalization, demonstrating the critical nature of this region for sequestration. Internalization was unaltered by cotransfection of cells with G protein-coupled receptor kinases (GRK)-2, -3, -5, -6, arrestin-2, or an arrestin-2 dominant negative mutant, indicating that GRKs and arrestins do not play a role in hIP trafficking. The hIP is sequestered in response to agonist activation via a PKC-independent pathway that is distinct from desensitization. Trafficking is dependent on determinants located in the C terminus, is GRK/arrestin-independent, and proceeds in part via a dynamin-dependent clathrin-coated vesicular endocytotic pathway although other dynamin-independent pathways may also be involved. (+info)
Deltorphin II-induced rapid desensitization of delta-opioid receptor requires both phosphorylation and internalization of the receptor. (2/386)Similar to other G protein-coupled receptors, rapid phosphorylation of the delta-opioid receptor in the presence of agonist has been reported. Hence, agonist-induced desensitization of the delta-opioid receptor has been suggested to be via the receptor phosphorylation, arrestin-mediated pathway. However, due to the highly efficient coupling between the delta-opioid receptor and the adenylyl cyclase, the direct correlation between the rates of receptor phosphorylation and receptor desensitization as measured by the adenylyl cyclase activity could not be established. In the current studies, using an ecdysone-inducible expression system to control the delta-opioid receptor levels in HEK293 cells, we could demonstrate that the rate of deltorphin II-induced receptor desensitization is dependent on the receptor level. Only at receptor concentrations +info)
Properties of GST-CALM expressed in E. coli. (3/386)Clathrin-coated vesicles (CCVs) are involved in protein and lipid trafficking between intracellular compartments in eukaryotic cells. CCVs are composed of clathrin and assembly proteins. The clathrin assembly protein lymphoid myeloid leukemia (CALM) gene, encodes a homologoue of the neuronal clathrin assembly protein AP180. In this study, we characterized the properties of the CALM expressed in E. coli. The molecular weight of bacterially expressed GST-CALM fusion protein was approximately 105 kD on SDS-PAGE. The CALM protein could promote clathrin triskelia into clathrin cages and could bind the preformed clathrin cage. However, 33 kD N-terminal domain of CALM could not bind pre-assembled clathrin cages, but assemble clathrin triskelia into clathrin cages. The CALM protein was bound to SH3 domain through N-terminal domain1, in vitro. The CALM protein is proteolyzed by caspase 3, caspase 8 and calpain through C-terminal domain. (+info)
A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins. (4/386)Pep12p is a yeast syntaxin located primarily in late endosomes. Using mutagenesis of a green fluorescent protein chimera we have identified a sorting signal FSDSPEF, which is required for transport of Pep12p from the exocytic pathway to late endosomes, from which it can, when overexpressed, reach the vacuole. When this signal is mutated, Pep12p instead passes to early endosomes, a step that is determined by its transmembrane domain. Surprisingly, Pep12p is then specifically retained in early endosomes and does not go on to late endosomes. By testing appropriate chimeras in mutant strains, we found that FSDSPEF-dependent sorting was abolished in strains lacking Gga1p and Gga2p, Golgi-associated coat proteins with homology to gamma adaptin. In the gga1 gga2 double mutant endogenous Pep12p cofractionated with the early endosome marker Tlg1p, and recycling of Snc1p through early endosomes was defective. Pep12p sorting was also defective in cells lacking the clathrin heavy or light chain. We suggest that specific and direct delivery of proteins to early and late endosomes is required to maintain the functional heterogeneity of the endocytic pathway and that the GGA proteins, probably in association with clathrin, help create vesicles destined for late endosomes. (+info)
The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes. (5/386)The heterotetrameric adaptor protein complex AP-3 has been shown to function in the sorting of proteins to the endosomal/lysosomal system. However, the mechanism of AP-3 recruitment onto membranes is poorly understood, and it is still uncertain whether AP-3 nucleates clathrin-coated vesicles. Using purified components, we show that AP-3 and clathrin are recruited onto protein-free liposomes and Golgi-enriched membranes by a process that requires ADP-ribosylation factor (ARF) and GTP but no other proteins or nucleotides. The efficiency of recruitment onto the two sources of membranes is comparable and independent of the composition of the liposomes. Clathrin binding occurred in a cooperative manner as a function of the membrane concentration of AP-3. Thin-section electron microscopy of liposomes and Golgi-enriched membranes that had been incubated with AP-3, clathrin, and ARF.GTP showed the presence of clathrin-coated buds and vesicles. These results establish that AP-3-containing clathrin-coated vesicles form in vitro and are consistent with AP-3-dependent protein transport being mediated by clathrin-coated vesicles. (+info)
Cellular internalization of cytolethal distending toxin from Haemophilus ducreyi. (6/386)The chancroid bacterium Haemophilus ducreyi produces a toxin (HdCDT) which is a member of the recently discovered family of cytolethal distending toxins (CDTs). These protein toxins prevent the cyclin-dependent kinase cdc2 from being activated, thus blocking the transition of cells from the G(2) phase into mitosis, with the consequent arrest of intoxicated cells in G(2). It is not known whether these toxins act by signaling from the cell surface or intracellularly only. Here we report that HdCDT has to undergo at least internalization before being able to act. Cellular intoxication was inhibited (i) by removal of clathrin coats via K(+) depletion, (ii) by treatment with drugs that inhibit receptor clustering into coated pits, and (iii) in cells genetically manipulated to fail in clathrin-dependent endocytosis. Intoxication was also completely inhibited in cells treated with bafilomycin A1 or nocodazole and in cells incubated at 18 degrees C, i.e., under conditions known to block the fusion of early endosomes with downstream compartments. Moreover, disruption of the Golgi complex by treatment with brefeldin A or ilimaquinone blocked intoxication. In conclusion, our data indicate that HdCDT enters cells via clathrin-coated pits and has to be transported via the Golgi complex in order to intoxicate cells. This is the first member of the family of CDTs for which cellular internalization and some details of the pathway have been demonstrated. (+info)
Impaired membrane traffic in defective ether lipid biosynthesis. (7/386)The first steps of ether lipid biosynthesis are exclusively localized to peroxisomes and hence some peroxisomal disorders are characterized by a severe deficiency of plasmalogens, the main ether lipids in humans. Here we report on gene defects of plasmalogen biosynthesis, chromosomal localization of the corresponding genes and, as a consequence of plasmalogen deficiency, on structural alterations of caveolae, clathrin-coated pits, endoplasmic reticulum and Golgi cisternae, as well as on the reduced rate of transferrin receptor cycling. The data suggest that plasmalogens, analogous to cholesterol, are essential for correct membrane functioning and their deficiency results in impaired membrane trafficking. (+info)
Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo. (8/386)Within the clathrin-coated vesicle (CCV) cycle, coat assembly drives the internalization of receptors from the cell surface and disassembly allows for the processing of internalized ligands. The heat shock cognate protein, hsc70, has been implicated in regulating coat disassembly. We find that in cells overexpressing ATPase-deficient hsc70 mutants, uncoating of CCVs is inhibited in vivo, and the majority of unassembled cytosolic clathrin shifts to an assembled pool that cofractionates with AP1 and AP2. Surprisingly, this assembled pool of coat proteins accumulates in the absence of cargo receptors, suggesting that disruption of hsc70 activity may cause misassembly of empty clathrin cages. The strongest effect of overexpression of hsc70 mutants is a block in transferrin receptor (TfnR) recycling, which cannot be accounted for by the degree of inhibition of uncoating of endocytic CCVs. These results suggest that hsc70 participates in multiple transport and/or sorting events between endosomal compartments. Additionally, the mutant-expressing cells are defective at internalizing transferrin. In the most potent case, the initial rate of uptake is inhibited 10-fold, and TfnR levels double at the cell surface. Our findings demonstrate that hsc70 indeed regulates coat disassembly and also suggest that this chaperone broadly modulates clathrin dynamics throughout the CCV cycle. (+info)
Coated vesicles are small membrane-bound sacs that are involved in the transport of molecules within cells. They are coated with a layer of proteins, called clathrin, which helps to regulate the movement of molecules into and out of the vesicle. Coated vesicles are involved in a variety of cellular processes, including the transport of proteins from the endoplasmic reticulum to the Golgi apparatus, the transport of lipids and other molecules between organelles, and the transport of molecules to the plasma membrane for secretion or uptake. In the medical field, coated vesicles are often studied in the context of diseases such as neurodegenerative disorders, where the abnormal accumulation of coated vesicles has been observed.
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.
Adaptor protein complex (AP) alpha subunits are a group of proteins that play a crucial role in the endocytic pathway of cells. These proteins are part of a larger protein complex called the AP-1 complex, which is involved in the sorting and transport of membrane proteins from the trans-Golgi network to endosomes. The AP-1 complex is composed of four subunits: alpha, beta, mu, and sigma. The alpha subunit is the largest subunit and is responsible for recognizing and binding to specific sorting signals on membrane proteins. There are four different isoforms of the alpha subunit, each of which is specific to a different subset of membrane proteins. The AP-1 complex is essential for the proper functioning of the endocytic pathway, which is responsible for the internalization and recycling of membrane proteins and lipids. Mutations in the genes encoding the AP-1 complex alpha subunits have been linked to a number of human diseases, including Hermansky-Pudlak syndrome and Chediak-Higashi syndrome.
Coated pits are invaginations or indentations in the plasma membrane of a cell. They are coated with a protein called clathrin, which helps to mediate the internalization of molecules from the cell surface. Coated pits can be found in many different types of cells and are involved in a variety of cellular processes, including endocytosis, the uptake of extracellular molecules into the cell, and the formation of vesicles, small membrane-bound compartments that transport materials within the cell.
Clathrin heavy chains are large protein molecules that play a crucial role in the process of endocytosis, which is the process by which cells take in substances from their environment. These heavy chains are a component of a protein complex called clathrin, which is responsible for forming a cage-like structure around the substances that a cell wants to internalize. This structure helps to pinch off the substance from the cell surface and form a vesicle, which can then be transported into the cell for further processing. Clathrin heavy chains are encoded by a group of genes called the CLTC gene family, and mutations in these genes can lead to a variety of diseases, including neurological disorders and cancer.
Adaptor proteins, vesicular transport are a class of proteins that play a crucial role in the process of vesicular transport in cells. These proteins function as molecular adaptors that link cargo molecules to the vesicles that transport them within the cell. In vesicular transport, cargo molecules are packaged into vesicles and transported to their destination within the cell or to other cells. Adaptor proteins help to recognize and bind to specific cargo molecules, and then link them to the vesicles that will transport them. This process is essential for the proper functioning of cells, as it allows for the transport of a wide variety of molecules, including proteins, lipids, and carbohydrates. Adaptor proteins, vesicular transport are involved in a number of different types of vesicular transport, including endocytosis, exocytosis, and intracellular trafficking. They are also involved in the regulation of a number of cellular processes, including signal transduction and the regulation of gene expression. In the medical field, adaptor proteins, vesicular transport are the subject of ongoing research, as they play a critical role in many cellular processes and are involved in a number of diseases and disorders. For example, defects in adaptor proteins have been implicated in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease. Additionally, alterations in the expression or function of adaptor proteins have been linked to a number of cancers, including breast cancer and prostate cancer.
IGF-2 receptor (IGF2R) is a protein that plays a role in cell growth and differentiation. It is a type of receptor that is activated by insulin-like growth factor 2 (IGF-2), a hormone that is involved in the regulation of growth and development. The IGF-2 receptor is expressed on the surface of many different types of cells, including cells in the liver, muscle, and bone. The IGF-2 receptor is a transmembrane protein that consists of an extracellular domain, a single transmembrane domain, and an intracellular domain. The extracellular domain binds to IGF-2, while the intracellular domain contains a tyrosine kinase domain that is activated when the receptor is bound to IGF-2. This activation leads to the phosphorylation of other proteins within the cell, which can trigger a variety of cellular responses, including cell growth, differentiation, and survival. Abnormalities in the IGF-2 receptor can lead to a number of different medical conditions. For example, mutations in the IGF2R gene have been associated with a rare genetic disorder called growth hormone deficiency, which can cause short stature and other growth-related problems. In addition, changes in the expression or function of the IGF-2 receptor have been implicated in the development of certain types of cancer, including breast cancer and ovarian cancer.
Monomeric clathrin assembly proteins (mCAPs) are a group of proteins that play a crucial role in the assembly of clathrin-coated vesicles in the endocytic pathway. Clathrin-coated vesicles are small membrane-bound structures that are involved in the internalization of proteins and other molecules from the cell surface into the cell interior. mCAPs are monomeric proteins that interact with clathrin and other components of the endocytic machinery to promote the assembly of clathrin lattices on the membrane. They are thought to function by stabilizing the clathrin triskelion, which is the basic building block of the clathrin lattice, and by facilitating the assembly of additional triskelia into a lattice. mCAPs are found in a variety of organisms, including humans, and are involved in a wide range of cellular processes, including endocytosis, intracellular trafficking, and signal transduction. Mutations in mCAP genes have been linked to a number of human diseases, including neurodegenerative disorders and immune system disorders.
Clathrin-coated vesicles are small, membrane-bound sacs that are involved in the transport of materials within cells. They are formed by the assembly of a protein lattice called clathrin on the cytoplasmic side of the plasma membrane, which then invaginates to form a vesicle. The vesicle is then pinched off from the plasma membrane and transported to its destination within the cell. Clathrin-coated vesicles are involved in a variety of cellular processes, including the uptake of nutrients and the transport of proteins and lipids within the cell. They are also involved in the secretion of materials from the cell, such as hormones and neurotransmitters. Disruptions in the formation or function of clathrin-coated vesicles can lead to a variety of diseases, including neurological disorders, immune system disorders, and certain types of cancer.
Clathrin light chains are small protein subunits that are essential components of the clathrin triskelion, a three-armed protein complex that is involved in the formation of vesicles in the endocytic pathway. The clathrin triskelion is composed of one heavy chain and three light chains, and it is responsible for the curvature of the vesicle membrane during the process of endocytosis. In the medical field, clathrin light chains are of interest because they are involved in a number of diseases, including cancer and neurodegenerative disorders. For example, mutations in the CLCN6 gene, which encodes one of the clathrin light chain subunits, have been associated with a form of inherited kidney disease called Dent's disease. Additionally, changes in the levels of clathrin light chains have been observed in various types of cancer, and they may play a role in the development and progression of these diseases.
Adaptor Protein Complex 2 (AP-2) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: alpha, beta, mu, and sigma, which together form a heterotetramer. AP-2 is involved in the recognition and sorting of cargo molecules destined for different cellular compartments, such as the plasma membrane, lysosomes, and endosomes. It recognizes specific sorting signals on the cargo molecules, such as tyrosine-based motifs, and binds to them through its alpha and beta subunits. Once bound to the cargo molecule, AP-2 recruits other proteins, such as clathrin, to form a coated pit on the plasma membrane. This coated pit then pinches off to form a vesicle that contains the cargo molecule, which is transported to its final destination within the cell. Disruptions in AP-2 function have been linked to various diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer.
In the medical field, auxilins are a group of proteins that play a role in the process of vesicle formation and membrane trafficking. Specifically, auxilins are involved in the disassembly of clathrin-coated vesicles, which are small membrane-bound structures that are involved in the transport of materials within cells. Clathrin-coated vesicles are formed by the assembly of a protein lattice called clathrin on the surface of the membrane, which is then coated with a layer of auxilin. As the vesicle is formed, auxilin binds to the clathrin lattice and helps to disassemble it, allowing the vesicle to be released from the membrane and transported to its destination within the cell. In addition to their role in vesicle formation and trafficking, auxilins have also been implicated in a number of other cellular processes, including the regulation of cell growth and division, and the maintenance of cell polarity.
Adaptor Protein Complex 1 (AP-1) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: AP-1A, AP-1B, AP-1C, and AP-1D, which are encoded by different genes. AP-1 is involved in the formation of coated vesicles, which are small vesicles that bud off from the plasma membrane and transport cargo to various cellular compartments. AP-1 recognizes specific signals on the cargo proteins and helps to sort them into the correct vesicles for transport. Disruptions in AP-1 function have been linked to a number of human diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer. Therefore, understanding the role of AP-1 in cellular trafficking is important for developing new treatments for these diseases.
In the medical field, the term "cattle" refers to large domesticated animals that are raised for their meat, milk, or other products. Cattle are a common source of food and are also used for labor in agriculture, such as plowing fields or pulling carts. In veterinary medicine, cattle are often referred to as "livestock" and may be treated for a variety of medical conditions, including diseases, injuries, and parasites. Some common medical issues that may affect cattle include respiratory infections, digestive problems, and musculoskeletal disorders. Cattle may also be used in medical research, particularly in the fields of genetics and agriculture. For example, scientists may study the genetics of cattle to develop new breeds with desirable traits, such as increased milk production or resistance to disease.
In the medical field, cytoplasmic vesicles are small, membrane-bound sacs that are found within the cytoplasm of cells. They are involved in a variety of cellular processes, including the transport of molecules and materials within the cell, the degradation of cellular waste, and the regulation of cellular signaling pathways. There are several different types of cytoplasmic vesicles, including endosomes, lysosomes, and exosomes. Endosomes are vesicles that are involved in the internalization and processing of extracellular molecules and materials. Lysosomes are vesicles that contain enzymes that are involved in the degradation of cellular waste and the breakdown of cellular components. Exosomes are vesicles that are released by cells and are involved in the communication between cells. Cytoplasmic vesicles play important roles in many different cellular processes and are involved in a wide range of diseases and conditions. For example, defects in the formation or function of cytoplasmic vesicles have been implicated in a number of neurological disorders, including Parkinson's disease and Alzheimer's disease.
Cell fractionation is a technique used in the medical field to isolate specific cellular components or organelles from a mixture of cells. This is achieved by fractionating the cells based on their size, density, or other physical properties, such as their ability to float or sediment in a solution. There are several different methods of cell fractionation, including differential centrifugation, density gradient centrifugation, and free-flow electrophoresis. Each method is designed to isolate specific cellular components or organelles, such as mitochondria, lysosomes, or nuclei. Cell fractionation is commonly used in research to study the function and interactions of different cellular components, as well as to isolate specific proteins or other molecules for further analysis. It is also used in clinical settings to diagnose and treat various diseases, such as cancer, by analyzing the composition and function of cells in tissues and fluids.
Dynamins are a family of GTPases that play important roles in various cellular processes, including endocytosis, exocytosis, vesicle trafficking, and intracellular signaling. They are characterized by their ability to hydrolyze GTP (guanosine triphosphate) and are involved in the regulation of membrane dynamics and the formation of vesicles. In the medical field, dynamins are of interest because they have been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease, as well as certain types of cancer.
HSC70 Heat-Shock Proteins (HSPs) are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins 70 (HSP70) and are found in all living organisms, from bacteria to humans. HSC70 HSPs play a crucial role in maintaining cellular homeostasis by helping to refold misfolded or damaged proteins, preventing protein aggregation, and assisting in the degradation of damaged proteins. They also play a role in the immune response by helping to transport antigens to the cell surface for presentation to the immune system. In the medical field, HSC70 HSPs have been studied for their potential therapeutic applications. For example, they have been shown to have anti-inflammatory and anti-cancer effects, and they are being investigated as potential treatments for a variety of diseases, including neurodegenerative disorders, cancer, and autoimmune diseases.
The cell membrane, also known as the plasma membrane, is a thin, flexible barrier that surrounds and encloses the cell. It is composed of a phospholipid bilayer, which consists of two layers of phospholipid molecules arranged tail-to-tail. The hydrophobic tails of the phospholipids face inward, while the hydrophilic heads face outward, forming a barrier that separates the inside of the cell from the outside environment. The cell membrane also contains various proteins, including channels, receptors, and transporters, which allow the cell to communicate with its environment and regulate the movement of substances in and out of the cell. In addition, the cell membrane is studded with cholesterol molecules, which help to maintain the fluidity and stability of the membrane. The cell membrane plays a crucial role in maintaining the integrity and function of the cell, and it is involved in a wide range of cellular processes, including cell signaling, cell adhesion, and cell division.
Adaptor protein complex gamma subunits, also known as AP-3 subunits, are a group of proteins that play a crucial role in the sorting and transport of proteins within cells. These subunits are part of a larger protein complex called the adaptor protein complex 3 (AP-3), which is involved in the formation of vesicles that transport specific cargo from the Golgi apparatus to lysosomes or other cellular compartments. The AP-3 complex is composed of four subunits: mu1A, mu1B, sigma2, and mu2A. These subunits interact with each other to form a stable complex that recognizes specific sorting signals on the cargo proteins and mediates their transport to the appropriate cellular compartment. Mutations in the genes encoding AP-3 subunits have been associated with a number of human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and Griscelli syndrome. These disorders are characterized by defects in the immune system, bleeding disorders, and other abnormalities, and are thought to result from impaired trafficking of specific proteins within cells.
Adaptor protein complex beta subunits are a group of proteins that play a crucial role in the formation and function of adaptor protein complexes (APCs). These complexes are involved in various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. The beta subunits of APCs are characterized by their ability to bind to specific proteins, such as clathrin, and to interact with other components of the APC. They are typically composed of a single membrane-spanning domain and a cytoplasmic tail that contains a number of conserved motifs, including an SH3 domain and a phosphotyrosine-binding domain. In the medical field, defects in the genes encoding adaptor protein complex beta subunits have been linked to a number of diseases, including neurodevelopmental disorders, immunodeficiencies, and cancer. For example, mutations in the APBB1 gene, which encodes the beta-1 subunit of the adaptor protein complex 2 (AP-2), have been associated with the neurodegenerative disorder frontotemporal dementia. Similarly, mutations in the APBB2 gene, which encodes the beta-2 subunit of AP-2, have been linked to the development of certain types of cancer.
Coatomer protein is a type of protein complex that plays a crucial role in the process of vesicle formation and membrane trafficking in cells. It is composed of multiple subunits, including the alpha, beta, and gamma subunits, and is involved in the formation of coated vesicles, which are small membrane-bound structures that transport materials within and between cells. The coatomer protein is responsible for recognizing and binding to specific proteins on the membrane, known as coat proteins, which are involved in the formation of the vesicle coat. The coatomer protein then assembles into a helical structure around the coat proteins, forming a coat around the vesicle. This coat is responsible for the stability and shape of the vesicle, and it also plays a role in the targeting of the vesicle to its final destination within the cell. Disruptions in the function of coatomer protein can lead to a variety of cellular defects, including impaired vesicle trafficking and the accumulation of abnormal vesicles within cells. These defects have been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, as well as certain types of cancer.
COP-coated vesicles are small, membrane-bound sacs that play a crucial role in the transport of molecules within cells. The acronym COP stands for coat protein complex, which refers to a group of proteins that are involved in the formation and function of these vesicles. COP-coated vesicles are involved in a variety of cellular processes, including the transport of proteins from the endoplasmic reticulum (ER) to the Golgi apparatus, the transport of lipids and other molecules between organelles, and the transport of materials out of the cell. The formation of COP-coated vesicles involves the interaction of several proteins, including COP I and COP II, which are responsible for the assembly and disassembly of the vesicle coat. Once a vesicle is formed, it is transported along the cytoskeleton to its destination, where it fuses with the target membrane and releases its contents. Disruptions in the function of COP-coated vesicles can have a range of effects on cellular processes and can contribute to the development of various diseases, including neurodegenerative disorders, lysosomal storage diseases, and certain types of cancer.
Adaptor protein complex mu subunits, also known as AP-μ subunits, are a type of protein that plays a role in the sorting and transport of proteins and lipids within cells. They are part of a larger family of adaptor proteins called AP complexes, which are involved in the formation of vesicles that transport cargo between different compartments within cells. The AP-μ subunits are composed of four different proteins, each with a specific role in the vesicle formation process. These proteins are encoded by genes located on different chromosomes and are highly conserved across different species. Mutations in the genes encoding AP-μ subunits have been associated with a number of human diseases, including a type of inherited lysosomal storage disorder called Chediak-Higashi syndrome. This disorder is characterized by the accumulation of large, abnormal lysosomes within cells, which can lead to a range of symptoms including immune deficiency, bleeding disorders, and neurological problems.
Vesicular transport proteins are a group of proteins that play a crucial role in the movement of molecules and ions across cell membranes. These proteins are responsible for the formation, transport, and fusion of vesicles, which are small, membrane-bound sacs that carry cargo within the cell. There are two main types of vesicular transport proteins: vesicle budding proteins and vesicle fusion proteins. Vesicle budding proteins are responsible for the formation of vesicles, while vesicle fusion proteins are responsible for the fusion of vesicles with their target membranes. Vesicular transport proteins are essential for many cellular processes, including the transport of neurotransmitters across the synaptic cleft, the transport of hormones and other signaling molecules, and the transport of nutrients and waste products within the cell. Mutations in vesicular transport proteins can lead to a variety of diseases, including neurological disorders, lysosomal storage disorders, and certain types of cancer.
In the medical field, the brain is the most complex and vital organ in the human body. It is responsible for controlling and coordinating all bodily functions, including movement, sensation, thought, emotion, and memory. The brain is located in the skull and is protected by the skull bones and cerebrospinal fluid. The brain is composed of billions of nerve cells, or neurons, which communicate with each other through electrical and chemical signals. These neurons are organized into different regions of the brain, each with its own specific functions. The brain is also divided into two hemispheres, the left and right, which are connected by a bundle of nerve fibers called the corpus callosum. Damage to the brain can result in a wide range of neurological disorders, including stroke, traumatic brain injury, Alzheimer's disease, Parkinson's disease, and epilepsy. Treatment for brain disorders often involves medications, surgery, and rehabilitation therapies to help restore function and improve quality of life.
Transferrin is a plasma protein that plays a crucial role in the transport of iron in the bloodstream. It is synthesized in the liver and transported to the bone marrow, where it helps to regulate the production of red blood cells. Transferrin also plays a role in the immune system by binding to and transporting iron to immune cells, where it is used to produce antibodies. In the medical field, low levels of transferrin can be a sign of iron deficiency anemia, while high levels may indicate an excess of iron in the body.
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.
In the medical field, cytoplasmic granules refer to small, dense structures found within the cytoplasm of certain cells. These granules are often involved in various cellular processes, such as protein synthesis, metabolism, and signaling. There are many different types of cytoplasmic granules, each with its own unique function and composition. Some examples of cytoplasmic granules include: - Lysosomes: These are organelles that contain digestive enzymes and are involved in breaking down and recycling cellular waste. - Peroxisomes: These are organelles that contain enzymes involved in the breakdown of fatty acids and other molecules. - Endosomes: These are organelles that are involved in the internalization and processing of extracellular molecules. - Ribosomes: These are small structures that are involved in protein synthesis. Cytoplasmic granules can be visualized using various microscopy techniques, such as light microscopy, electron microscopy, and immunofluorescence microscopy. The presence and distribution of cytoplasmic granules can provide important information about the function and health of a cell.
Biological transport refers to the movement of molecules, such as nutrients, waste products, and signaling molecules, across cell membranes and through the body's various transport systems. This process is essential for maintaining homeostasis, which is the body's ability to maintain a stable internal environment despite changes in the external environment. There are several mechanisms of biological transport, including passive transport, active transport, facilitated diffusion, and endocytosis. Passive transport occurs when molecules move down a concentration gradient, from an area of high concentration to an area of low concentration. Active transport, on the other hand, requires energy to move molecules against a concentration gradient. Facilitated diffusion involves the use of transport proteins to move molecules across the cell membrane. Endocytosis is a process by which cells take in molecules from the extracellular environment by engulfing them in vesicles. In the medical field, understanding the mechanisms of biological transport is important for understanding how drugs and other therapeutic agents are absorbed, distributed, metabolized, and excreted by the body. This knowledge can be used to design drugs that are more effective and have fewer side effects. It is also important for understanding how diseases, such as cancer and diabetes, affect the body's transport systems and how this can be targeted for treatment.
ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that play important roles in regulating various cellular processes, including vesicle trafficking, membrane fusion, and cytoskeleton dynamics. They are encoded by a group of genes located on human chromosome 12 and are widely expressed in most tissues and cell types. ARFs are activated by the exchange of GDP for GTP, which causes a conformational change in the protein that exposes a hydrophobic region that interacts with various effector proteins. These effector proteins can then bind to ARFs and modulate their activity, leading to changes in cellular behavior. In the context of vesicle trafficking, ARFs are involved in the recruitment of coat proteins to the membrane, which is necessary for the formation of transport vesicles. They also play a role in the fusion of vesicles with their target membranes, which is essential for the delivery of cargo to its destination. ARFs have also been implicated in a variety of cellular processes, including cell division, signal transduction, and the regulation of gene expression. Dysregulation of ARF activity has been linked to a number of diseases, including cancer, neurodegenerative disorders, and immune system disorders.
ADP-Ribosylation Factor 1 (ARF1) is a small GTPase protein that plays a crucial role in regulating various cellular processes, including vesicle trafficking, membrane fusion, and endocytosis. ARF1 is activated by the guanine nucleotide exchange factor (GEF) and inactivated by the GTPase-activating protein (GAP). ARF1 is involved in the formation of coated vesicles, which are small membrane-bound structures that transport cargo between different cellular compartments. ARF1 also plays a role in the fusion of vesicles with their target membranes, which is essential for the proper functioning of many cellular processes, including secretion, endocytosis, and intracellular trafficking. In addition to its role in vesicle trafficking, ARF1 has been implicated in various cellular signaling pathways, including the regulation of the actin cytoskeleton, the Wnt signaling pathway, and the regulation of cell proliferation and differentiation. Dysregulation of ARF1 activity has been linked to various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases.
Nerve tissue proteins are proteins that are found in nerve cells, also known as neurons. These proteins play important roles in the structure and function of neurons, including the transmission of electrical signals along the length of the neuron and the communication between neurons. There are many different types of nerve tissue proteins, each with its own specific function. Some examples of nerve tissue proteins include neurofilaments, which provide structural support for the neuron; microtubules, which help to maintain the shape of the neuron and transport materials within the neuron; and neurofilament light chain, which is involved in the formation of neurofibrillary tangles, which are a hallmark of certain neurodegenerative diseases such as Alzheimer's disease. Nerve tissue proteins are important for the proper functioning of the nervous system and any disruption in their production or function can lead to neurological disorders.
Taurodeoxycholic acid (TDC) is a bile acid that is produced in the liver and secreted into the small intestine. It is a conjugated bile acid, meaning that it is bound to a molecule of taurine, which helps to solubilize fats and cholesterol in the digestive tract. TDC is an important component of bile, which is a fluid produced by the liver that helps to digest fats and absorb fat-soluble vitamins. In the medical field, TDC is sometimes used as a diagnostic tool to evaluate liver function and to diagnose certain liver diseases. It is also used in the treatment of certain liver disorders, such as primary biliary cirrhosis, and as a component of some dietary supplements.
In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.
Coat Protein Complex I, also known as NADH:ubiquinone oxidoreductase, is a large enzyme complex that plays a crucial role in the electron transport chain of mitochondria. It is responsible for transferring electrons from NADH to ubiquinone, which is a coenzyme involved in the production of ATP, the energy currency of the cell. The complex is composed of 45 subunits, including 14 core subunits and 31 accessory subunits. It is located in the inner mitochondrial membrane and is responsible for the reduction of ubiquinone to ubiquinol, which is then used in the electron transport chain to generate ATP. Deficiencies in the function of Complex I have been linked to a number of diseases, including Leigh syndrome, a rare genetic disorder that affects the nervous system.
Brain chemistry refers to the chemical processes that occur within the brain, including the production, release, and regulation of neurotransmitters, hormones, and other chemical messengers. These chemical processes play a critical role in regulating mood, behavior, cognition, and other aspects of brain function. In the medical field, brain chemistry is often studied in the context of neurological and psychiatric disorders, such as depression, anxiety, schizophrenia, and addiction. By understanding the underlying chemical imbalances or abnormalities in the brain, researchers and healthcare providers can develop more effective treatments for these conditions. Some common neurotransmitters and hormones involved in brain chemistry include dopamine, serotonin, norepinephrine, acetylcholine, and cortisol. Medications such as antidepressants, antipsychotics, and mood stabilizers often work by altering the levels of these chemicals in the brain to improve symptoms of various disorders.
Adaptor protein complex sigma subunits, also known as AP-σ subunits, are a group of proteins that play a role in the sorting and transport of proteins and lipids within cells. They are part of a larger family of adaptor protein complexes, which are involved in the formation of vesicles that transport cargo between different compartments within cells. The AP-σ subunits are specifically involved in the formation of vesicles that bud from the trans-Golgi network (TGN) and transport cargo to the plasma membrane. They are thought to play a role in the sorting of specific proteins and lipids for transport to the plasma membrane, and they may also be involved in the regulation of membrane trafficking. In the medical field, the AP-σ subunits are of interest because they have been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Mutations in genes encoding AP-σ subunits have been linked to these conditions, and it is thought that dysfunction of the AP-σ complex may contribute to the development of these diseases.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
Receptors, Transferrin are proteins that are found on the surface of cells and are responsible for binding to the iron transport protein transferrin, which carries iron in the bloodstream. These receptors play a crucial role in regulating the uptake of iron by cells and are involved in a number of physiological processes, including the production of red blood cells and the maintenance of iron homeostasis in the body. In the medical field, the study of transferrin receptors is important for understanding the mechanisms of iron metabolism and for developing treatments for iron-related disorders, such as anemia and iron overload.
Phosphoproteins are proteins that have been modified by the addition of a phosphate group to one or more of their amino acid residues. This modification is known as phosphorylation, and it is a common post-translational modification that plays a critical role in regulating many cellular processes, including signal transduction, metabolism, and gene expression. Phosphoproteins are involved in a wide range of biological functions, including cell growth and division, cell migration and differentiation, and the regulation of gene expression. They are also involved in many diseases, including cancer, diabetes, and cardiovascular disease. Phosphoproteins can be detected and studied using a variety of techniques, including mass spectrometry, Western blotting, and immunoprecipitation. These techniques allow researchers to identify and quantify the phosphorylation status of specific proteins in cells and tissues, and to study the effects of changes in phosphorylation on protein function and cellular processes.
Brefeldin A (BFA) is a naturally occurring macrolide compound that was first isolated from the fungus Brefeldia nivea. It is a potent inhibitor of the Golgi apparatus, a organelle in eukaryotic cells responsible for sorting, packaging, and transporting proteins and lipids to their final destinations within the cell or for secretion outside the cell. In the medical field, BFA is used as a tool to study the function and dynamics of the Golgi apparatus and other intracellular organelles. It is often used in cell biology research to visualize and analyze the transport of proteins and lipids through the Golgi apparatus and to study the role of the Golgi apparatus in various cellular processes, such as cell growth, differentiation, and signaling. BFA is also being investigated as a potential therapeutic agent for various diseases, including cancer, neurodegenerative disorders, and infectious diseases. However, more research is needed to fully understand its potential therapeutic effects and to develop safe and effective treatments based on BFA.
Dynamin I is a large GTPase protein that plays a crucial role in the process of endocytosis, which is the process by which cells internalize extracellular material. Dynamin I is responsible for the constriction and scission of the vesicle neck during endocytosis, which allows the vesicle to pinch off from the plasma membrane and form a new intracellular compartment. In addition to its role in endocytosis, dynamin I has also been implicated in a number of other cellular processes, including neurotransmitter release, vesicle trafficking, and intracellular signaling. Mutations in the gene encoding dynamin I have been associated with a number of human diseases, including Charcot-Marie-Tooth disease type 2A (CMT2A) and hereditary spastic paraplegia type 7 (SPG7).
In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.
I'm sorry, but I couldn't find a specific medical term or definition for "Filipin" in the medical field. It's possible that you may have misspelled the term or that it is not commonly used in medical terminology. If you could provide more context or information about where you encountered this term, I may be able to provide more assistance.
GTP phosphohydrolases are a family of enzymes that hydrolyze guanosine triphosphate (GTP) into guanosine diphosphate (GDP) and inorganic phosphate (Pi). These enzymes play a crucial role in regulating various cellular processes, including signal transduction, protein synthesis, and cell division. In the medical field, GTP phosphohydrolases are of particular interest because they are involved in the regulation of many signaling pathways that are implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. For example, the enzyme Rho GTPase activating protein (RhoGAP) is a GTP phosphohydrolase that regulates the activity of Rho GTPases, which are involved in cell migration, cytoskeletal organization, and cell proliferation. Mutations in RhoGAP have been implicated in several human cancers, including breast cancer and glioblastoma. Other examples of GTP phosphohydrolases that are of medical interest include the enzyme GTPase-activating protein (GAP) for heterotrimeric G proteins, which regulates the activity of G protein-coupled receptors (GPCRs), and the enzyme dynamin, which is involved in endocytosis and autophagy. Mutations in these enzymes have been implicated in various diseases, including hypertension, diabetes, and neurodegenerative disorders.
In the medical field, a cell line refers to a group of cells that have been derived from a single parent cell and have the ability to divide and grow indefinitely in culture. These cells are typically grown in a laboratory setting and are used for research purposes, such as studying the effects of drugs or investigating the underlying mechanisms of diseases. Cell lines are often derived from cancerous cells, as these cells tend to divide and grow more rapidly than normal cells. However, they can also be derived from normal cells, such as fibroblasts or epithelial cells. Cell lines are characterized by their unique genetic makeup, which can be used to identify them and compare them to other cell lines. Because cell lines can be grown in large quantities and are relatively easy to maintain, they are a valuable tool in medical research. They allow researchers to study the effects of drugs and other treatments on specific cell types, and to investigate the underlying mechanisms of diseases at the cellular level.
Cell compartmentation refers to the physical separation of different cellular components and organelles within a cell. This separation allows for the efficient functioning of various cellular processes and helps to maintain cellular homeostasis. Each organelle has a specific function and is compartmentalized to allow for the proper execution of that function. For example, the mitochondria are responsible for energy production and are located in the cytoplasm, while the nucleus contains the genetic material and is located in the center of the cell. Cell compartmentation also plays a role in the regulation of cellular processes. For example, the endoplasmic reticulum (ER) is responsible for protein synthesis and folding, and its compartmentalization allows for the proper processing and transport of proteins within the cell. Disruptions in cell compartmentation can lead to various diseases and disorders, including neurodegenerative diseases, metabolic disorders, and cancer.
Mannosephosphates are a group of compounds that contain a combination of mannose and phosphate groups. They are found naturally in the body and are involved in various biological processes, including the immune response and the regulation of blood sugar levels. In the medical field, mannosephosphates are sometimes used as a dietary supplement or as a treatment for certain conditions. For example, they have been studied for their potential to improve immune function and to reduce inflammation. They have also been used to treat conditions such as diabetes and cancer. It is important to note that the use of mannosephosphates as a medical treatment is still being studied, and more research is needed to fully understand their potential benefits and risks. As with any medical treatment, it is important to consult with a healthcare professional before using mannosephosphates or any other supplement or medication.
Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.
Alpha-L-Fucosidase is an enzyme that is involved in the breakdown of certain complex carbohydrates, such as fucosylated glycoproteins and glycolipids. It is primarily found in the lysosomes of cells, where it plays a role in the degradation of these complex carbohydrates. Alpha-L-Fucosidase deficiency is a rare genetic disorder that can lead to the accumulation of fucosylated glycoproteins and glycolipids in the body, which can cause a range of symptoms and health problems. In the medical field, alpha-L-Fucosidase is used as a diagnostic tool to help identify individuals with alpha-L-Fucosidase deficiency, and it is also being studied as a potential target for the development of new treatments for this disorder.
Adenosine triphosphatases (ATPases) are a group of enzymes that hydrolyze adenosine triphosphate (ATP) to adenosine diphosphate (ADP) and inorganic phosphate (Pi). These enzymes play a crucial role in many cellular processes, including energy production, muscle contraction, and ion transport. In the medical field, ATPases are often studied in relation to various diseases and conditions. For example, mutations in certain ATPase genes have been linked to inherited disorders such as myopathy and neurodegenerative diseases. Additionally, ATPases are often targeted by drugs used to treat conditions such as heart failure, cancer, and autoimmune diseases. Overall, ATPases are essential enzymes that play a critical role in many cellular processes, and their dysfunction can have significant implications for human health.
Membrane lipids are a type of lipid molecule that are essential components of cell membranes. They are composed of fatty acids and glycerol, and are responsible for maintaining the structure and function of cell membranes. There are several types of membrane lipids, including phospholipids, glycolipids, and cholesterol. Phospholipids are the most abundant type of membrane lipid and are responsible for forming the basic structure of cell membranes. They consist of a hydrophilic (water-loving) head and two hydrophobic (water-fearing) tails, which allow them to spontaneously form a bilayer in an aqueous environment. Glycolipids are another type of membrane lipid that are composed of a fatty acid chain and a carbohydrate group. They are found on the surface of cell membranes and play a role in cell recognition and signaling. Cholesterol is a third type of membrane lipid that is important for maintaining the fluidity and stability of cell membranes. It is also involved in the regulation of membrane protein function. Membrane lipids play a crucial role in many cellular processes, including cell signaling, nutrient transport, and cell division. They are also important for maintaining the integrity and function of cell membranes, which are essential for the survival of cells.
Hexosephosphates are a group of compounds that consist of a hexose sugar (such as glucose, fructose, or galactose) attached to a phosphate group. In the medical field, hexosephosphates are often used as markers for certain diseases or conditions, such as diabetes or liver disease. They can also be used as diagnostic tools to help identify and monitor certain types of cancer, such as osteosarcoma or Ewing's sarcoma. Hexosephosphates are produced by the body as a result of certain metabolic processes, and their levels in the blood can provide important information about a person's overall health and well-being.
Proton-translocating ATPases are a group of enzymes that use the energy from ATP hydrolysis to pump protons across a membrane. These enzymes are found in various cellular compartments, including the inner mitochondrial membrane, the plasma membrane of eukaryotic cells, and the plasma membrane of bacteria. In the context of the medical field, proton-translocating ATPases are important because they play a crucial role in maintaining the proton gradient across cellular membranes. This gradient is essential for many cellular processes, including the production of ATP through oxidative phosphorylation in mitochondria, the regulation of intracellular pH, and the transport of ions across cell membranes. Proton-translocating ATPases can be classified into two main types: primary and secondary. Primary proton pumps, such as the ATP synthase in mitochondria, use the energy from ATP hydrolysis to directly pump protons across a membrane. Secondary proton pumps, such as the vacuolar ATPase in plant cells, use the energy from ATP hydrolysis to pump protons indirectly by coupling the proton gradient to the transport of other ions or molecules. Disruptions in the function of proton-translocating ATPases can lead to a variety of medical conditions, including metabolic disorders, neurological disorders, and cardiovascular diseases. For example, mutations in the ATP synthase gene can cause Leigh syndrome, a rare inherited disorder that affects the brain and muscles. Similarly, disruptions in the function of the vacuolar ATPase can lead to a variety of diseases, including osteoporosis, cataracts, and cancer.
Cytosol is the fluid inside the cytoplasm of a cell, which is the gel-like substance that fills the cell membrane. It is also known as the cytoplasmic matrix or cytosolic matrix. The cytosol is a complex mixture of water, ions, organic molecules, and various enzymes and other proteins that play important roles in cellular metabolism, signaling, and transport. It is the site of many cellular processes, including protein synthesis, energy production, and waste removal. The cytosol is also the site of many cellular organelles, such as the mitochondria, ribosomes, and endoplasmic reticulum, which are responsible for carrying out specific cellular functions.
Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.
In the medical field, cytoplasm refers to the gel-like substance that fills the cell membrane of a living cell. It is composed of various organelles, such as mitochondria, ribosomes, and the endoplasmic reticulum, as well as various dissolved molecules, including proteins, lipids, and carbohydrates. The cytoplasm plays a crucial role in many cellular processes, including metabolism, protein synthesis, and cell division. It also serves as a site for various cellular activities, such as the movement of organelles within the cell and the transport of molecules across the cell membrane. In addition, the cytoplasm is involved in maintaining the structural integrity of the cell and protecting it from external stressors, such as toxins and pathogens. Overall, the cytoplasm is a vital component of the cell and plays a critical role in its function and survival.
HSP70 heat shock proteins are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins because they are upregulated in cells exposed to high temperatures. HSP70 proteins play a crucial role in the folding and refolding of other proteins in the cell. They act as molecular chaperones, helping to stabilize and fold newly synthesized proteins, as well as assisting in the refolding of misfolded proteins. This is important because misfolded proteins can aggregate and form toxic structures that can damage cells and contribute to the development of diseases such as Alzheimer's, Parkinson's, and Huntington's. In addition to their role in protein folding, HSP70 proteins also play a role in the immune response. They can be recognized by the immune system as foreign antigens and can stimulate an immune response, leading to the production of antibodies and the activation of immune cells. Overall, HSP70 heat shock proteins are important for maintaining cellular homeostasis and protecting cells from damage. They are also of interest in the development of new therapies for a variety of diseases.
Adaptor Protein Complex 3 (AP-3) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: μ1A, μ1B, μ2A, and μ2B, which are encoded by different genes. AP-3 is involved in the sorting of cargo molecules destined for lysosomes, endosomes, and the plasma membrane. It recognizes specific sorting signals on the cargo molecules and mediates their binding to vesicles that transport them to their final destinations. Mutations in the genes encoding AP-3 subunits have been associated with several human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and a form of retinitis pigmentosa. These diseases are characterized by defects in the immune system, bleeding disorders, and vision problems, respectively.
Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.
In the medical field, "Cells, Cultured" refers to cells that have been grown and maintained in a controlled environment outside of their natural biological context, typically in a laboratory setting. This process is known as cell culture and involves the isolation of cells from a tissue or organism, followed by their growth and proliferation in a nutrient-rich medium. Cultured cells can be derived from a variety of sources, including human or animal tissues, and can be used for a wide range of applications in medicine and research. For example, cultured cells can be used to study the behavior and function of specific cell types, to develop new drugs and therapies, and to test the safety and efficacy of medical products. Cultured cells can be grown in various types of containers, such as flasks or Petri dishes, and can be maintained at different temperatures and humidity levels to optimize their growth and survival. The medium used to culture cells typically contains a combination of nutrients, growth factors, and other substances that support cell growth and proliferation. Overall, the use of cultured cells has revolutionized medical research and has led to many important discoveries and advancements in the field of medicine.
Horseradish Peroxidase (HRP) is an enzyme that is commonly used in medical research and diagnostics. It is a protein that catalyzes the oxidation of a wide range of substrates, including hydrogen peroxide, which is a reactive oxygen species that is produced by cells as a byproduct of metabolism. In medical research, HRP is often used as a label for antibodies or other molecules, allowing researchers to detect the presence of specific proteins or other molecules in tissues or cells. This is done by first attaching HRP to an antibody or other molecule of interest, and then using a substrate that reacts with HRP to produce a visible signal. This technique is known as immunohistochemistry or immunofluorescence. HRP is also used in diagnostic tests, such as pregnancy tests, where it is used to detect the presence of specific hormones or other molecules in urine or blood samples. In these tests, HRP is attached to an antibody that binds to the target molecule, and the presence of the target molecule is detected by the production of a visible signal. Overall, HRP is a versatile enzyme that is widely used in medical research and diagnostics due to its ability to catalyze the oxidation of a wide range of substrates and its ability to be easily labeled and detected.
In the medical field, binding sites refer to specific locations on the surface of a protein molecule where a ligand (a molecule that binds to the protein) can attach. These binding sites are often formed by a specific arrangement of amino acids within the protein, and they are critical for the protein's function. Binding sites can be found on a wide range of proteins, including enzymes, receptors, and transporters. When a ligand binds to a protein's binding site, it can cause a conformational change in the protein, which can alter its activity or function. For example, a hormone may bind to a receptor protein, triggering a signaling cascade that leads to a specific cellular response. Understanding the structure and function of binding sites is important in many areas of medicine, including drug discovery and development, as well as the study of diseases caused by mutations in proteins that affect their binding sites. By targeting specific binding sites on proteins, researchers can develop drugs that modulate protein activity and potentially treat a wide range of diseases.
Calcium-binding proteins are a class of proteins that have a high affinity for calcium ions. They play important roles in a variety of cellular processes, including signal transduction, gene expression, and cell motility. Calcium-binding proteins are found in many different types of cells and tissues, and they can be classified into several different families based on their structure and function. Some examples of calcium-binding proteins include calmodulin, troponin, and parvalbumin. These proteins are often regulated by changes in intracellular calcium levels, and they play important roles in the regulation of many different physiological processes.
Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, including energy metabolism, signal transduction, and protein synthesis. It is composed of a guanine base, a ribose sugar, and three phosphate groups. In the medical field, GTP is often studied in relation to its role in regulating cellular processes. For example, GTP is a key molecule in the regulation of the actin cytoskeleton, which is responsible for maintaining cell shape and facilitating cell movement. GTP is also involved in the regulation of protein synthesis, as it serves as a substrate for the enzyme guanine nucleotide exchange factor (GEF), which activates the small GTPase protein Rho. In addition, GTP is involved in the regulation of various signaling pathways, including the Ras/MAPK pathway and the PI3K/Akt pathway. These pathways play important roles in regulating cell growth, differentiation, and survival, and are often dysregulated in various diseases, including cancer. Overall, GTP is a critical molecule in cellular metabolism and signaling, and its dysfunction can have significant consequences for cellular function and disease.
GTP-binding proteins, also known as G proteins, are a family of proteins that play a crucial role in signal transduction in cells. They are involved in a wide range of cellular processes, including cell growth, differentiation, and metabolism. G proteins are composed of three subunits: an alpha subunit, a beta subunit, and a gamma subunit. The alpha subunit is the one that binds to guanosine triphosphate (GTP), a molecule that is involved in regulating the activity of the protein. When GTP binds to the alpha subunit, it causes a conformational change in the protein, which in turn activates or inhibits downstream signaling pathways. G proteins are activated by a variety of extracellular signals, such as hormones, neurotransmitters, and growth factors. Once activated, they can interact with other proteins in the cell, such as enzymes or ion channels, to transmit the signal and initiate a cellular response. G proteins are found in all eukaryotic cells and play a critical role in many physiological processes. They are also involved in a number of diseases, including cancer, neurological disorders, and cardiovascular diseases.
Centrifugation, density gradient is a laboratory technique used to separate cells, particles, or molecules based on their density. The sample is placed in a centrifuge tube and spun at high speeds, causing the particles to separate into layers based on their density. The heaviest particles settle at the bottom of the tube, while the lightest particles float to the top. This technique is commonly used in medical research to isolate specific cells or particles for further analysis or study. It is also used in the diagnosis of certain diseases, such as blood disorders, and in the purification of biological samples for use in medical treatments.
Alpha-mannosidase is an enzyme that is involved in the breakdown of complex carbohydrates, specifically mannose-containing oligosaccharides. It is a lysosomal enzyme that is found in many tissues throughout the body, including the liver, spleen, and brain. In the medical field, alpha-mannosidosis is a rare genetic disorder that is caused by a deficiency in alpha-mannosidase activity. This leads to the accumulation of undigested mannose-containing oligosaccharides in various tissues, which can cause a range of symptoms and complications, including intellectual disability, skeletal abnormalities, and hearing loss. Alpha-mannosidosis is typically diagnosed through a combination of clinical examination, laboratory tests, and genetic testing. Treatment for the disorder may involve enzyme replacement therapy, which involves administering alpha-mannosidase to replace the missing enzyme in the body. Other treatments may include supportive care to manage symptoms and complications.
Etorphine is a synthetic opioid analgesic that is used in veterinary medicine to immobilize large animals such as elephants, rhinos, and giraffes. It is a very potent drug, with a potency that is estimated to be 100 to 1,000 times greater than that of morphine. Etorphine is typically administered intramuscularly or intravenously, and its effects can last for several hours. It is also used in research to study the effects of opioids on the central nervous system. In humans, etorphine is a Schedule I controlled substance and is not used for medical purposes.
Vesicular transport adaptor protein
Beta2-adaptin C-terminal domain
Vesicle (biology and chemistry)
Mannose 6-phosphate receptor
Thyrotropin-releasing hormone receptor
J. Richard McIntosh
Short linear motif
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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
DeCS - Términos Nuevos
- COPI vesicles transport molecules between different parts of the Golgi body and from the Golgi back to the rough ER. (jove.com)
- COPII vesicles are formed in the ER membranes and mediate transport from ER to the Golgi. (jove.com)
- Coated vesicles are spherical, protein-coated carriers with a 50-100 nm diameter that mediate bidirectional transport between the ER and the Golgi. (jove.com)
- The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. (jove.com)
- Secretory proteins exit the endoplasmic reticulum (ER) in coat protein complex II (COPII)-coated vesicles and then progress through the Golgi complex before delivery to their final destination. (biologists.com)
- The OCRL1 protein is an inositol polyphosphate 5-phosphatase primarily located in the trans- Golgi network (TGN), on endosomes, and at the endocytic clathrin coated pits. (medscape.com)
- OCRL1 has been localized to the trans -Golgi network and various compartments of the endocytic pathway (traffic), where it is found in the clathrin-coated pits, clathrin-coated vesicles, variable functioning endosomes (early, signaling, recycling), and the basal body of primary cilia. (medscape.com)
- Carrier biogenesis relies on distinct protein networks changing membrane shape at the trans -Golgi network, each regulating coat assembly, F-actin-based mechanical forces, or the biophysical properties of lipid bilayers. (researcher-app.com)
- This study provides the first in vivo evidence of trapped SD proteins in clathrin-coated pits at the plasma membrane when this pathway is disrupted. (sdbonline.org)
- The SD protein endocytosis and recycling pathway was found to contain clathrin , dynamin , AP-2 complex, like-AP180 (Lap) , auxilin and Hsc70-4 (the endocytosis part) followed by Rab11 and the exocyst complex (the recycling part). (sdbonline.org)
- The absorption of LMW proteins occurs in the PTC through clathrin-mediated endocytosis via 2 multiligand receptors (megalin and cubilin) present in the PTC apical border. (medscape.com)
- We showed that AP2 phosphorylation not only leads to changes in its interactome, but is a major decision point in clathrin-mediated endocytosis, capable of affecting its rates. (cam.ac.uk)
- We are building on these findings by exploring systematically and mechanistically how kinases and phosphatases regulate clathrin-mediated endocytosis. (cam.ac.uk)
- Regulation of clathrin-mediated endocytosis by hierarchical allosteric activation of AP2. (cam.ac.uk)
- Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. (aacrjournals.org)
- The coat on the budding vesicle comprises two layers, an inner layer of adaptor proteins (gray ovals) and an outer layer that forms a polyhedral cage. (biologists.com)
- Recently, our collaborative efforts identified the molecular basis of the NAK kinase-mediated phosphorylation of the most abundant clathrin adaptor, AP2 ( link to paper ). (cam.ac.uk)
- Clathrin/adaptor protein-1-coated carriers connect the secretory and the endocytic pathways. (researcher-app.com)
- These findings provide a framework for synchronizing the chemical/biophysical properties of lipid bilayers, F-actin-based mechanical forces, and the activity of proteins sensing membrane shape during clathrin/adaptor protein-1-coated carrier biogenesis. (researcher-app.com)
- Based on the type of protein coats, these vesicles can be of three types: coat protein or COP-coated vesicles, COPI and COPII, and clathrin-coated vesicles. (jove.com)
- COPI and COPII vesicles are composed of similar coat protein complexes called coatomers. (jove.com)
- Their formation is driven by the assembly of different classes of coat proteins, namely COPI, COPII, clathrin, or retromer complex. (jove.com)
- The COPI and COPII coat proteins share similar structural features with Clathrin but differ in cargo sorting and vesicle formation mechanisms. (jove.com)
- Clathrin coated vesicles enable neurotransmitter receptors and other proteins to be endocytosed or taken up across neuronal membranes and across the membranes of other types of cells. (wikipedia.org)
- Specific coat proteins cover their cytosolic surface. (jove.com)
- Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. (jove.com)
- Coat proteins can help sort the cargo and assemble on the donor membrane to initiate vesicle formation. (jove.com)
- here, discrete export signals on the cargo are recognized and captured by specific receptors that are concentrated at sites of vesicle budding. (biologists.com)
- In attempts to attribute pathology of COVID-19 patients directly to tissue damage caused by SARS-CoV-2, investigators have inaccurately reported subcellular structures, including coated vesicles, multivesicular bodies, and vesiculating rough endoplasmic reticulum, as coronavirus particles. (cdc.gov)
- Bulk flow is the process by which cargo passively distributes between the donor compartment and the transport vesicles it generates, resulting in equal cargo concentration within these two compartments. (biologists.com)
- Different mechanisms of recruitment of cargo to transport vesicles. (biologists.com)
- The CLINT1 protein binds to the terminal domain of the clathrin heavy chain and stimulates clathrin cage vesicle assembly. (wikipedia.org)
- Cyclin-G-associated kinase (GAK) , a PD susceptibility gene identified through genome-wide association studies (GWAS), is a ubiquitous serine/threonine kinase involved in clathrin uncoating (see Drosophila Clathrin heavy chain ), though its PD-related function remains elusive. (sdbonline.org)
- Coated vesicles are transport vesicles that bud off from specialized regions of the cell membrane. (jove.com)
- Temporal ordering in endocytic clathrin-coated vesicle formation via AP2 phosphorylation. (cam.ac.uk)
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components. (ista.ac.at)
- Synaptojanin 2 (SYNJ2) is a phosphatidylinositol (PI) phosphatase that controls two distinct functions, clathrin-mediated endocytosis and tumor cell invadopodia formation and invasion. (nih.gov)
- Here, we identify a number of novel SYNJ2 binding partners, several of which have previously been shown to be necessary for invadopodia formation or clathrin-mediated endocytosis. (nih.gov)
- Phosphorylated derivatives of phosphatidylinositol (PIPs) are key membrane lipid residues involved in clathrin-mediated endocytosis (CME). (uzh.ch)
- Cells communicate with their environment and with other cells through their plasma membranes (PM). The major selective pathway for internalization from the plasma membrane is clathrin-mediated endocytosis (CME), which involves the assembly of clathrin coated pits (CCPs) that package cargo molecules, invaginate and pinch off into the cytosol forming clathrin coated vesicles (CCVs). (nih.gov)
- The absorption of LMW proteins occurs in the PTC through clathrin-mediated endocytosis via 2 multiligand receptors (megalin and cubilin) present in the PTC apical border. (medscape.com)
- Clathrin-mediated endocytosis, which depends on the AP2 complex, plays an essential role in many cellular and developmental processes in mammalian cells. (biologists.com)
- Importantly, Dynamin is essential for clathrin-coated vesicle formation in endocytosis, in transport from the trans Golgi network, as well as for ligand uptake through caveolae. (immune-system-research.com)
- The clathrin-mediated endocytosis pathway for LDL transport is considered to be the main one in eukaryotic cells. (istanbul.edu.tr)
- In this study, the COV434 human granulosa cells were cultured and divided into four groups where in some of the groups Dil-conjugated LDL and Icarugamycin (ICA) a clathrin-mediated endocytosis inhibitor were added. (istanbul.edu.tr)
- We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 +/- 30 k(B)T, i.e., approximately 20 times that of either the outer clathrin cage or inner vesicle membrane. (nih.gov)
- Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function. (nih.gov)
- 10. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. (nih.gov)
- We have reconstituted dynamin-catalyzed vesicle formation from fluid supported bilayers with excess membrane reservoir (SUPER) templates to gain insight into the mechanisms governing membrane fission. (nih.gov)
- Vesicles formed when cell-membrane coated pits ( COATED PITS, CELL-MEMBRANE ) invaginate and pinch off. (nih.gov)
- The nascent phagosome membrane has a dense coat of acidosomes docked at its cytosolic surface well before the nascent vacuole pinches off the cytopharynx. (ucsd.edu)
- 12.Kasai M,Yamamoto Y,Maeshima M,et al.Effects of in vivo treatment with abscisic acid and/or cytokinin on activities of vacuolar H + pumps of tonoplast-enriched membrane vesicles prepared from barley roots［J］.Plant and Cell Physiology,1993,34(7):1107-1115. (nefu.edu.cn)
- The role of counterion movement in endosomes is not clear, but a subpopulation of early endosomes, clathrin-coated vesicles (CCVs), has previously been shown to use external chloride (Cl - ) to allow V-ATPase-dependent acidification. (nih.gov)
- Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES . (nih.gov)
- These vesicles arise from early endosomes as clathrin coated vesicles and are about 100. (ucsd.edu)
- High resolution image of vesicles and early endosomes under the membranelles of the peniculus of the buccal cavity. (ucsd.edu)
- While unsuccessful at identifying the mechanism of anion transport, we used glutamate-facilitated acidification, density gradients, and mass spectrometry to show that most brain CCVs are synaptic vesicles, complementing results from earlier studies that argued similarity only on the basis on protein content. (nih.gov)
- Clathrin interactor 1 (CLINT1), also known as EPSIN4, is a protein which in humans is encoded by the CLINT1 gene. (wikipedia.org)
- The CLINT1 protein binds to the terminal domain of the clathrin heavy chain and stimulates clathrin cage vesicle assembly. (wikipedia.org)
- 18. Basolateral Sorting of the Sodium/Iodide Symporter Is Mediated by Adaptor Protein 1 Clathrin Adaptor Complexes. (nih.gov)
- Our data indicate that, despite the partial conservation of lipid markers and protein cohorts known to play important roles in dynamic endocytic events in well-characterized model systems, the Giardia lineage presents a strikingly divergent clathrin-centered network. (uzh.ch)
- The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN . (nih.gov)
- In addition, the encoded protein may regulate the formation of clathrin-coated vesicles and could be involved in synaptic vesicle recycling. (nih.gov)
- Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). (nih.gov)
- A ) A representative field (scale bar = 100 nm) of unprocessed image showing clathrin CCVs mostly between 80 and 100 nm in height (color-scale, right , 0-250 nm), obtained by using a sharpened and clean silicon nitride tip ( r ∼3 nm). (nih.gov)
- 17. Basolateral sorting of human poliovirus receptor alpha involves an interaction with the mu1B subunit of the clathrin adaptor complex in polarized epithelial cells. (nih.gov)
- However, there are no studies that elucidate LDL internalization in human granulosa cells clarifying whether the clathrin-mediated endocytic pathway is functional in this process. (istanbul.edu.tr)
- Quick-freeze deep-etch rotary-shadowed replica of an early endosome with two clathrin-coated evaginations. (ucsd.edu)
- The topics include from virus structures, architecture of postsynaptic machinery at neuronal synapses, architecture of bacterial chemotactic machinery and structure of clathrin-coated vesicles, and new tomography techniques based on energy-filtered imaging and STEM. (nih.gov)
- 3. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. (nih.gov)
- The role for clathrin assemblies in fluid phase uptake and their link to internal membranes via PIP-binding adaptors is unknown. (uzh.ch)
- Our results show that human granulosa cells as well use the LDL cholesterol for steroid biosynthesis and they may prefer the clathrin-mediated endocytotic pathway to internalize it. (istanbul.edu.tr)
- [ 48 ] It was found that coating the surface of liposomes with a polymer, such as polyethyleneglycol (PEG), or with the sugar portion of mucin, protected them against bile salt destabilization and increased the stability of these colloidal carriers in the GI tract. (medscape.com)
- 1.Forgac M.Structure,Mechanism and regulation of the Clathrin-Coated vesicle and yeast vacuolar H + -ATPases［J］.Journal of Experimental Biology,2000,203(1):71-80. (nefu.edu.cn)
- [ 51 ] It is interesting that liposomes coated with chitosan are more unstable than uncoated liposomes (retention of fluoresceine iso thiocyanate was approximately 20 vs 36% after 2 h exposure in simulated gastric fluid). (medscape.com)
- 8. Clathrin and clathrin adaptor AP-1 control apical trafficking of megalin in the biosynthetic and recycling routes. (nih.gov)
- Transmission EM reveals that that there is an LRRK2 GS kinase-dependent significant reduction in synaptic vesicle number and a greater abundance of clathrin-coated vesicles in DA neurons. (johnshopkins.edu)
- Vesicle Shrinking and Enlargement Play Opposing Roles in the Release of Exocytotic Contents. (nih.gov)
- The CLINT1 gene has been shown to be involved in the genetic aetiology of schizophrenia in four studies It is known that the antipsychotic drugs chlorpromazine and clozapine stabilise clathrin coated vesicles and this may be one reason why antipsychotic drugs are effective in treating delusions, auditory hallucinations and many of the other symptoms of schizophrenia. (wikipedia.org)
- The highly diverged parasitic protist Giardia lamblia presents disordered and static clathrin assemblies at PM invaginations, contacting specialized endocytic organelles called peripheral vacuoles (PVs). (uzh.ch)
- Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. (nih.gov)
- GAK (cyclin G-associated kinase) is a key regulator of clathrin-coated vesicle trafficking and plays a central role during development. (ox.ac.uk)
- 7. Immunoprecipitation and Western Blot Analysis of AP-1 Clathrin-Coated Vesicles. (nih.gov)
- Quick-freeze deep-etch image of rows of carrier vesicles lined up along the cytopharyngeal microtubular ribbons. (ucsd.edu)
- observed that uncoated liposomes released 20-50% of insulin in the presence of bile salts, whereas distearylphophoethanolamine-PEG-coated liposomes and mucin-coated liposomes released approximately 2 and 10% of insulin, respectively, within 6 h in the same medium. (medscape.com)
- sweet arrow peptide (SAP), HIV-1 Rev, flock house virus (FHV) coat, brome mosaic virus (BMV) Gag, human T-cell lymphotrophic virus (HTLV)-II Rex, and the nuclear localization signal (NLS) from nucleoplasmin. (proteopedia.org)
- D ) Typical ribbon synapse at a rod spherule in control retina with intact ribbon strut (asterisk) and densely packed surrounding glutamatergic vesicles. (jci.org)