Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Cyclopentanes: A group of alicyclic hydrocarbons with the general formula R-C5H9.Golgi Apparatus: A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)Protein Synthesis Inhibitors: Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.Monensin: An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.Coatomer Protein: A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.ADP-Ribosylation Factor 1: ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)ADP-Ribosylation Factors: MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47Adaptor Protein Complex gamma Subunits: A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.Coat Protein Complex I: A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.Nocodazole: Nocodazole is an antineoplastic agent which exerts its effect by depolymerizing microtubules.trans-Golgi Network: A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Cell Compartmentation: A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.Intracellular Membranes: Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Endosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Macrolides: A group of often glycosylated macrocyclic compounds formed by chain extension of multiple PROPIONATES cyclized into a large (typically 12, 14, or 16)-membered lactone. Macrolides belong to the POLYKETIDES class of natural products, and many members exhibit ANTIBIOTIC properties.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.Rho Guanine Nucleotide Exchange Factors: Signaling proteins which function as master molecular switches by activating Rho GTPases through conversion of guanine nucleotides. Rho GTPases in turn control many aspects of cell behavior through the regulation of multiple downstream signal transduction pathways.EsterasesBetamethasone Valerate: The 17-valerate derivative of BETAMETHASONE. It has substantial topical anti-inflammatory activity and relatively low systemic anti-inflammatory activity.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Dihydrotestosterone: A potent androgenic metabolite of TESTOSTERONE. It is produced by the action of the enzyme 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE.Receptors, Androgen: Proteins, generally found in the CYTOPLASM, that specifically bind ANDROGENS and mediate their cellular actions. The complex of the androgen and receptor migrates to the CELL NUCLEUS where it induces transcription of specific segments of DNA.Prostatic Neoplasms: Tumors or cancer of the PROSTATE.Androgens: Compounds that interact with ANDROGEN RECEPTORS in target tissues to bring about the effects similar to those of TESTOSTERONE. Depending on the target tissues, androgenic effects can be on SEX DIFFERENTIATION; male reproductive organs, SPERMATOGENESIS; secondary male SEX CHARACTERISTICS; LIBIDO; development of muscle mass, strength, and power.Cell Cycle: The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.Cell Line, Tumor: A cell line derived from cultured tumor cells.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Breast Neoplasms: Tumors or cancer of the human BREAST.Periventricular Nodular Heterotopia: A disorder resulting from a defect in the pattern of neuronal migration in which ectopic collections of neurons lie along the lateral ventricles of the brain or just beneath, contiguously or in isolated patches.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Arsenite Transporting ATPases: Efflux pumps that use the energy of ATP hydrolysis to pump arsenite across a membrane. They are primarily found in prokaryotic organisms, where they play a role in protection against excess intracellular levels of arsenite ions.Insulinoma: A benign tumor of the PANCREATIC BETA CELLS. Insulinoma secretes excess INSULIN resulting in HYPOGLYCEMIA.Aspartate-Ammonia Ligase: An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. EC 6.3.1.1.Islets of Langerhans: Irregular microscopic structures consisting of cords of endocrine cells that are scattered throughout the PANCREAS among the exocrine acini. Each islet is surrounded by connective tissue fibers and penetrated by a network of capillaries. There are four major cell types. The most abundant beta cells (50-80%) secrete INSULIN. Alpha cells (5-20%) secrete GLUCAGON. PP cells (10-35%) secrete PANCREATIC POLYPEPTIDE. Delta cells (~5%) secrete SOMATOSTATIN.Proinsulin: A pancreatic polypeptide of about 110 amino acids, depending on the species, that is the precursor of insulin. Proinsulin, produced by the PANCREATIC BETA CELLS, is comprised sequentially of the N-terminal B-chain, the proteolytically removable connecting C-peptide, and the C-terminal A-chain. It also contains three disulfide bonds, two between A-chain and B-chain. After cleavage at two locations, insulin and C-peptide are the secreted products. Intact proinsulin with low bioactivity also is secreted in small amounts.Endoplasmic Reticulum Stress: Various physiological or molecular disturbances that impair ENDOPLASMIC RETICULUM function. It triggers many responses, including UNFOLDED PROTEIN RESPONSE, which may lead to APOPTOSIS; and AUTOPHAGY.Unfolded Protein Response: A cellular response to environmental insults that cause disruptions in PROTEIN FOLDING and/or accumulation of defectively folded protein in the ENDOPLASMIC RETICULUM. It consists of a group of regulatory cascades that are triggered as a response to altered levels of calcium and/or the redox state of the endoplasmic reticulum. Persistent activation of the unfolded protein response leads to the induction of APOPTOSIS.Activating Transcription Factor 6: One of the BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS that is synthesized as a membrane-bound protein in the ENDOPLASMIC RETICULUM. In response to endoplasmic reticulum stress it translocates to the GOLGI APPARATUS. It is activated by PROTEASES and then moves to the CELL NUCLEUS to regulate GENETIC TRANSCRIPTION of GENES involved in the unfolded protein response.Transcription Factor CHOP: A CCAAT-enhancer binding protein that is induced by DNA DAMAGE and growth arrest. It serves as a dominant negative inhibitor of other CCAAT-enhancer binding proteins.Molecular Chaperones: A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.Research Personnel: Those individuals engaged in research.

Generation of CD8(+) T-cell responses to Mycobacterium bovis and mycobacterial antigen in experimental bovine tuberculosis. (1/1373)

Protective immunity against tuberculosis is considered to be essentially cell mediated, and an important role for CD8(+) T lymphocytes has been suggested by several studies of murine and human infections. The present work, using an experimental model of infection with Mycobacterium bovis in cattle, showed that live M. bovis elicits the activation of CD8(+) T cells in vitro. However, a sonic extract prepared from M. bovis (MBSE) and protein purified derivative (PPDb) also induced a considerable degree of activation of the CD8(+) T cells. Analysis of proliferative responses of peripheral blood mononuclear cells, purified CD8(+) T cells, and CD8(+) T-cell clones to M. bovis and to soluble antigenic preparations (MBSE, PPDb) showed that the responses of all three types of cells were always superior for live mycobacteria but that strong responses were also obtained with complex soluble preparations. Furthermore, while cytotoxic capabilities were not investigated, the CD8(+) T cells were found to produce and release gamma interferon in response to antigen (live and soluble), which indicated one possible protective mechanism for these cells in bovine tuberculosis. Finally, it was demonstrated by metabolic inhibition with brefeldin A and cytochalasin D at the clonal level that an endogenous pathway of antigen processing is required for presentation to bovine CD8(+) cells and that presentation is also dependent on phagocytosis of the antigen.  (+info)

Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells. (2/1373)

LY-A strain is a Chinese hamster ovary cell mutant resistant to sphingomyelin (SM)-directed cytolysin and has a defect in de novo SM synthesis. Metabolic labeling experiments with radioactive serine, sphingosine, and choline showed that LY-A cells were defective in synthesis of SM from these precursors, but not syntheses of ceramide (Cer), glycosphingolipids, or phosphatidylcholine, indicating a specific defect in the conversion of Cer to SM in LY-A cells. In vitro experiments showed that the specific defect of SM formation in LY-A cells was not due to alterations in enzymatic activities responsible for SM synthesis or degradation. When cells were treated with brefeldin A, which causes fusion of the Golgi apparatus with the endoplasmic reticulum (ER), de novo SM synthesis in LY-A cells was restored to the wild-type level. Pulse-chase experiments with a fluorescent Cer analogue, N-(4,4-difluoro-5,7-dimethyl-4-bora-3a, 4a-diaza-s-indacene-3-pentanoyl)-D-erythro-sphingosine (C5-DMB-Cer), revealed that in wild-type cells C5-DMB-Cer was redistributed from intracellular membranes to the Golgi apparatus in an intracellular ATP-dependent manner, and that LY-A cells were defective in the energy-dependent redistribution of C5-DMB-Cer. Under ATP-depleted conditions, conversion of C5-DMB-Cer to C5-DMB-SM and of [3H]sphingosine to [3H]SM in wild-type cells decreased to the levels in LY-A cells, which were not affected by ATP depletion. ER-to-Golgi apparatus trafficking of glycosylphosphatidylinositol-anchored or membrane-spanning proteins in LY-A cells appeared to be normal. These results indicate that the predominant pathway of ER-to-Golgi apparatus trafficking of Cer for de novo SM synthesis is ATP dependent and that this pathway is almost completely impaired in LY-A cells. In addition, the specific defect of SM synthesis in LY-A cells suggests different pathways of Cer transport for glycosphingolipids versus SM synthesis.  (+info)

Assembly of very low density lipoprotein: a two-step process of apolipoprotein B core lipidation. (3/1373)

The liver plays a primary role in lipid metabolism. Important functions include the synthesis and incorporation of hydrophobic lipids, triacylglycerols and cholesteryl esters into the core of water-miscible particles called lipoproteins and the secretion of these particles into the circulation for transport to distant tissues. In this article, we present a brief overview of one aspect of the assembly process of very low density lipoproteins, namely, possible mechanisms for combining core lipids with apolipoprotein B. This is a complex process in which apolipoprotein B interacts with core lipids to form very low density lipoproteins by a two-step process that can be dissociated biochemically.  (+info)

Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors. (4/1373)

Protein secretion through the endoplasmic reticulum and Golgi vesicular trafficking system is initiated by the binding of ADP-ribosylation factors (ARFs) to donor membranes, leading to recruitment of coatomer, bud formation, and eventual vesicle release. ARFs are approximately 20-kDa GTPases that are active with bound GTP and inactive with GDP bound. Conversion of ARF-GDP to ARF-GTP is regulated by guanine nucleotide-exchange proteins. All known ARF guanine nucleotide-exchange proteins contain a Sec7 domain of approximately 200 amino acids that includes the active site and fall into two classes that differ in molecular size and susceptibility to inhibition by the fungal metabolite brefeldin A (BFA). To determine the structural basis of BFA sensitivity, chimeric molecules were constructed by using sequences from the Sec7 domains of BFA-sensitive yeast Sec7 protein (ySec7d) and the insensitive human cytohesin-1 (C-1Sec7). Based on BFA inhibition of the activities of these molecules with recombinant yeast ARF2 as substrate, the Asp965-Met975 sequence in ySec7d was shown to be responsible for BFA sensitivity. A C-1Sec7 mutant in which Ser199, Asn204, and Pro209 were replaced with the corresponding ySec7d amino acids, Asp965, Gln970, and Met975, exhibited BFA sensitivity similar to that of recombinant ySec7d (rySec7d). Single replacement in C-1Sec7 of Ser199 or Pro209 resulted in partial inhibition by BFA, whereas replacement of Gln970 in ySec7d with Asn (as found in C-1Sec7) had no effect. As predicted, the double C-1Sec7 mutant with S199D and P209M was BFA-sensitive, demonstrating that Asp965 and Met975 in ySec7d are major molecular determinants of BFA sensitivity.  (+info)

Intracellular trafficking pathways in the assembly of connexins into gap junctions. (5/1373)

Trafficking pathways underlying the assembly of connexins into gap junctions were examined using living COS-7 cells expressing a range of connexin-aequorin (Cx-Aeq) chimeras. By measuring the chemiluminescence of the aequorin fusion partner, the translocation of oligomerized connexins from intracellular stores to the plasma membrane was shown to occur at different rates that depended on the connexin isoform. Treatment of COS-7 cells expressing Cx32-Aeq and Cx43-Aeq with brefeldin A inhibited the movement of these chimera to the plasma membrane by 84 +/- 4 and 88 +/- 4%, respectively. Nocodazole treatment of the cells expressing Cx32-Aeq and Cx43-Aeq produced 29 +/- 16 and 4 +/- 7% inhibition, respectively. In contrast, the transport of Cx26 to the plasma membrane, studied using a construct (Cx26/43T-Aeq) in which the short cytoplasmic carboxyl-terminal tail of Cx26 was replaced with the extended carboxyl terminus of Cx43, was inhibited 89 +/- 5% by nocodazole and was minimally affected by exposure of cells to brefeldin A (17 +/-11%). The transfer of Lucifer yellow across gap junctions between cells expressing wild-type Cx32, Cx43, and the corresponding Cx32-Aeq and Cx43-Aeq chimeras was reduced by nocodazole treatment and abolished by brefeldin A treatment. However, the extent of dye coupling between cells expressing wild-type Cx26 or the Cx26/43T-Aeq chimeras was not significantly affected by brefeldin A treatment, but after nocodazole treatment, transfer of dye to neighboring cells was greatly reduced. These contrasting effects of brefeldin A and nocodazole on the trafficking properties and intercellular dye transfer are interpreted to suggest that two pathways contribute to the routing of connexins to the gap junction.  (+info)

Initiation of galactosaminoglycan biosynthesis. Separate galactosylation and dephosphorylation pathways for phosphoxylosylated decorin protein and exogenous xyloside. (6/1373)

By using various radiolabelled precursors, glycosylation and phosphorylation of decorin in a rat fibroblast cell line was investigated in the presence of increasing concentrations of p-nitrophenyl-O-beta-d-xylopyranoside. Decorin core protein glycanation was suppressed to approximately 25% of the normal level in the presence of 2 mm and 3 mm xyloside. Glycans/saccharides were released from the core protein and size-separated by gel chromatography. The intracellular decorin obtained from cells treated with 2 mm xyloside was substituted with Xyl and also with Gal-Xyl and Gal-Gal-Xyl, but not with longer saccharides. Only the trisaccharide contained an almost fully phosphorylated Xyl. We conclude that galactosylation of endogenous, xylosylated decorin and exogenous xyloside probably follow separate pathways or that xylosides and early decorin glycoforms are kept separated. At the addition of the first glucuronic acid the two pathways seem to merge and dephosphorylation of decorin takes place. Xyloside-primed and secreted galactosaminoglycan chains produced simultanously retained phosphorylated Xyl. Inadequate dephosphorylation could be due to excess substrate or to a short transit.time. As shown previously [Moses, J., Oldberg, A., Eklund, E. & Fransson, L.-A. (1997) Eur. J. Biochem. 248, 767-774], brefeldin A-arrested decorin is substituted with the linkage-region extended with an undersulphated and incomplete galactosaminoglycan chain. In cells treated with this drug, xylosides were unable to prime galactosaminoglycan synthesis and unable to inhibit glycosylation and phosporylation of decorin.  (+info)

Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. (7/1373)

We demonstrate that the major in vivo targets of brefeldin A (BFA) in the secretory pathway of budding yeast are the three members of the Sec7 domain family of ARF exchange factors: Gea1p and Gea2p (functionally interchangeable) and Sec7p. Specific residues within the Sec7 domain are important for BFA inhibition of ARF exchange activity, since mutations in these residues of Gea1p (sensitive to BFA) and of ARNO (resistant to BFA) reverse the sensitivity of each to BFA in vivo and in vitro. We show that the target of BFA inhibition of ARF exchange activity is an ARF-GDP-Sec7 domain protein complex, and that BFA acts to stabilize this complex to a greater extent for a BFA-sensitive Sec7 domain than for a resistant one.  (+info)

Hormonal regulation of oligopeptide transporter pept-1 in a human intestinal cell line. (8/1373)

The intestinal oligopeptide transporter (cloned as Pept-1) has major roles in protein nutrition and drug therapy. A key unstudied question is whether expression of Pept-1 is hormonally regulated. In this experiment, we investigated whether insulin has such a role. We used a human intestinal cell monolayer (Caco-2) as the in vitro model of human small intestine and glycylglutamine (Gly-Gln) as the model substrate for Pept-1. Results showed that addition of insulin at a physiological concentration (5 nM) to incubation medium greatly stimulates Gly-Gln uptake by Caco-2 cells. This stimulation was blocked when genistein, an inhibitor of tyrosine kinase, was added to incubation medium. Studies of the mechanism of insulin stimulation showed the following. 1) Stimulation occurred promptly (30-60 min) after exposure to insulin. 2) There was no significant change in the Michaelis-Menten constant of Gly-Gln transport, but there was a nearly twofold increase in its maximal velocity. 3) Insulin effect persisted even when Golgi apparatus, which is involved in trafficking of newly synthesized Pept-1, was dismantled. 4) However, there was complete elimination of insulin effect by disruption of microtubules involved in trafficking of preformed Pept-1. 5) Finally, with insulin treatment, there was no change in Pept-1 gene expression, but the amount of Pept-1 protein in the apical membrane was increased. In conclusion, the results show that insulin, when it binds to its receptor, stimulates Gly-Gln uptake by Caco-2 cells by increasing the membrane population of Pept-1. The mechanism appears to be increased translocation of this transporter from a preformed cytoplasmic pool.  (+info)

Figure 3. Immunofluorescent localization of procollagen I and Hsp47 in the presence or absence of brefeldin A treatment in CEC. Cells were treated with 2 µg/ml brefeldin A for 30 min, fixed, permeabilized, and stained as described in the text. A. Procollagen I (green) and Hsp47 (red) in brefeldin A-treated cells. B. Prolyl 4-hydroxylase (green) and procollagen I (red) in brefeldin A-treated cells. C. Prolyl 4-hydroxylase (green) and Hsp47 (red) in brefeldin A-treated cells. D. Phase-contrast microscopy of C. Bar, 10 µm.. ...
(His)6-GBF1 is a BFA-resistant ARF-GEF. (A) Fractions enriched in (His)6-GBF1 display a GEF specific for ARFs. Identical volumes (5 μl) of the 50 mM imidazole
brefeldin A esterase: hydrolyzes brefeldin A to brefeldin A acid & also hydrolyzes ethyl valerate; 372 amino acids; amino acid sequence given in first source
In mammalian and yeast cells, the main target of brefeldin A appears to be a guanine nucleotide exchange factor (GEF) called GBF1.[8] GBF1 is a member of the Arf family of GEFs which are recruited to membranes of the Golgi.[9] It is responsible for the regulation of Arf1p GTPase.[9] It does this through converting the inactive GDP-bound form of Arf1p to the active GTP-bound form.[9] The nucleotide exchange occurs at the catalytic Sec7 domain of GBF1. Activated Arf1p then recruits coat protein β-COP, a subunit of the COP-I complex, to cargo-bound receptors on the membrane.[9] Coat protein recruitment is necessary for proper vesicle formation and transport. Brefeldin A reversibly inhibits the function of GBF1 uncompetitively by binding to the complex it forms with GDP-bound Arf1p and preventing conversion to the GTP-bound form.[9] The lack of active Arf1p prevents coat protein recruitment, which then ultimately induces the fusion of neighboring ER and Golgi membranes due to lack of vesicle ...
We examined the actions on ENaC recycling of reagents that alter membrane trafficking and cytoskeletal organization using the restimulation protocol. Treatment with BFA did not affect the first response to forskolin, but it produced a marked inhibition of the subsequent ΔISC. The finding that it was possible to elicit one cycle of forskolin stimulation-recovery suggests that ENaC-containing vesicles available for channel insertion are distal to the Golgi and TGN. The response to restimulation was significantly reduced, however, indicating that ENaC is recycled through BFA-sensitive compartments. Results from a study using BFA-treated toad bladder produced similar findings in response to repeated ADH stimulation; an initial stimulation could be elicited, but subsequent stimulations were abolished by pretreatment with 5 μg/ml BFA (Weng and Wade, 1994). The effect of BFA on ENaC recycling was unexpected in view of its well-documented inhibition of AP-1-dependent trafficking in early compartments ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) has been identified recently as a novel regulator of estrogen signalling in breast cancer cells. Despite being a potential target for new breast cancer treatment, its amino acid sequence suggests no association with any well-characterized protein family and provides little clues as to its molecular function. In this paper, we predicted the structure, function and interactions of BIG3 using a range of bioinformatic tools. Homology search results showed that BIG3 had distinct features from its paralogues, BIG1 and BIG2, with a unique region between the two shared domains, Sec7 and DUF1981. Although BIG3 contains Sec7 domain, the lack of the conserved motif and the critical glutamate residue suggested no potential guaninyl-exchange factor (GEF) activity. Fold recognition tools predicted BIG3 to adopt an α-helical repeat structure similar to that of the armadillo (ARM) family. Using state-of-the-art methods, we predicted interaction sites
We recently reported that brefeldin A-inhibited guanine nucleotide-exchange proteins 3 (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby leading to a reduction of function of the PHB2 growth suppressor in the nuclei of breasts tumor cells. PHB2 nuclear transfer may offer restorative strategies for managing Elizabeth2/Emergency room signs in breasts tumor cells. Introduction Prohibitin 1 and 2 (PHB and buy 808118-40-3 PHB2) proteins are highly conserved in eukaryotic cells and exhibit diverse subcellular localization with different functions [1C3]. These molecules are primarily observed in inner mitochondrial membranes via their buy 808118-40-3 N-terminal transmembrane domain but are also present in several other localizations such as the cytosol, endoplasmic reticulum, nucleus, and plasma membrane [1]. Both proteins form hetero-oligomeric ring structures in the inner mitochondrial membrane and function as chaperones buy 808118-40-3 that maintain mitochondrial integrity and stabilize ...
Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), (10ug), 10 µg.
gi,17538522,ref,NP_501092.1, component of oligomeric Golgi complex 2; brefeldin A-sensitive, LDLC related peripheral Golgi protein, required for normal Golgi function; contains an N myristoylation domain (78.6 kD) (4H802) [Caenorhabditis elegans] gi,2498513,sp,Q21444,COG2_CAEEL Conserved oligomeric Golgi complex component 2 (LDLC protein homolog) gi,1078836,pir,,B53542 brefeldin A-sensitive Golgi protein LDLC - Caenorhabditis elegans gi,807871,emb,CAA84428.1, Cog2 protein [Caenorhabditis elegans] ...
The Golgi apparatus has long been suggested to be important for directing secretion to specific sites on the plasma membrane in response to extracellular signaling events. However, the mechanisms by which signaling events are coordinated with Golgi apparatus function remain poorly understood. Here, we identify a scaffolding function for the Golgi matrix protein GM130 that sheds light on how such signaling events may be regulated. We show that the mammalian Ste20 kinases YSK1 and MST4 target to the Golgi apparatus via the Golgi matrix protein GM130. In addition, GM130 binding activates these kinases by promoting autophosphorylation of a conserved threonine within the T-loop. Interference with YSK1 function perturbs perinuclear Golgi organization, cell migration, and invasion into type I collagen. A biochemical screen identifies 14-3-3zeta as a specific substrate for YSK1 that localizes to the Golgi apparatus, and potentially links YSK1 signaling at the Golgi apparatus with protein transport events, cell
There are six subfamilies of Arf GEFs in eukaryotes (see poster). The GBF/Gea and BIG/Sec7 GEFs function sequentially in the secretory pathway, with GBF/Gea proteins acting at the early Golgi, and BIG/Sec7 proteins at the trans-Golgi and TGN (Donaldson and Jackson, 2011). The cytohesin/Arno, EFA6 and IQSEC/BRAG subfamilies function primarily in endosome-plasma-membrane trafficking pathways at the cell periphery, the latter two using Arf6 as a substrate (Casanova, 2007; Gillingham and Munro, 2007). The FBXO8 GEFs, restricted primarily to vertebrates, contain an F-box in addition to the Sec7 domain (Gillingham and Munro, 2007). Arf activation by GBF/Gea and BIG/Sec7 GEFs is inhibited by the drug brefeldin A, which traps a Sec7-domain-Arf-GDP complex (Mossessova et al., 2003; Peyroche et al., 1999; Renault et al., 2003).. Many GEFs exist in an autoinhibited state in the cytosol, with their activation coupled to membrane recruitment. At the plasma membrane, the Pleckstrin homology (PH) domains of ...
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is involved in the maintenance of Golgi structure and function through its interaction with the integral membrane protein giantin. It may also be involved in the hormonal regulation of steroid formation. [provided by RefSeq, Jul 2008 ...
Zinc Finger Protein Containing Five Transmembrane Domains; Null Mutant Exhibits Strongly Fragmented Vacuoles And Sensitivity To Brefeldin A, A Drug Which Is Known To Affect Intracellular Transport
A golgi apparatus, or golgi complex, is the main organelle responsible for mediating the transportation of protein and fat within the cell, according to Scitable, a learning website curated by...
The Golgi apparatus is an organelle found in the cytoplasm of most eukaryotic cells that is involved in the packaging and secretion of substances nece...
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Dr. Stéphanie Devineau, Unité BFA, équipe Réponses Moléculaires et Cellulaires aux Xénobiotiques (resp. J.M. Dupret) Titre : Crowning ...
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TY - JOUR. T1 - Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells. AU - Wang, E.. AU - Pennington, J. G.. AU - Goldenring, J. R.. AU - Hunziker, W.. AU - Dunn, Kenneth. PY - 2001. Y1 - 2001. N2 - Recent studies showing thorough intermixing of apical and basolateral endosomes have demonstrated that endocytic sorting is critical to maintaining the plasma membrane polarity of epithelial cells. Our studies of living, polarized cells show that disrupting endocytosis with brefeldin-A rapidly destroys the polarity of transferrin receptors in MDCK cells while having no effect on tight junctions. Brefeldin-A treatment induces tubulation of endosomes, but the sequential compartments and transport steps of the transcytotic pathway remain intact. Transferrin is sorted from LDL, but is then missorted from common endosomes to the apical recycling endosome, as identified by its nearly neutral pH, and association with GFP chimeras of Rabs 11a and ...
FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy. MISCELLANEOUS: In the process of transport, SEC12 itself may migrate to the Golgi apparatus and function in subsequent transport events. MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD medium ...
The reports of dual-targeted proteins in plants have steadily increased over the past years. The vast majority of these proteins are soluble proteins distributed between compartments of the non-secretory pathway, predominantly chloroplasts and mitochondria. In contrast, dual-targeted transmembrane proteins, especially of the secretory pathway, are rare and the mechanisms leading to their differential targeting remain largely unknown. Here, we report dual-targeting of the Arabidopsis DUF679 Membrane Protein 1 (DMP1) to the tonoplast (TP) and the plasma membrane (PM). In Arabidopsis and tobacco two equally abundant DMP1 isoforms are synthesized by alternative translation initiation: a full length protein, DMP1.1, and a truncated one, DMP1.2, which lacks the N-terminal 19 amino acids including a TP-targeting dileucine motif. Accumulation of DMP1.1 and DMP1.2 in the TP and the PM, respectively, is Brefeldin A-sensitive, indicating transit via the Golgi. However, DMP1.2 interacts with DMP1.1, leading to
The Golgi complex, also known as the Golgi apparatus or simply the Golgi, is a cytoplasmic organelle. It is found in eukaryote cells, as in animals, plants, and fungi. The complex was discovered by Camillo Golgi in 1898. Golgi, who worked at Pavia, Italy, was ignored. His discovery was said to be dirt on his lenses. Years later, electron microscope pictures showed structures just like in the original Golgi drawings. It is made of several flattened sac-like membranes which look like a stack of pancakes. The main function of the Golgi apparatus is to process and package macromolecules, such as proteins and lipids. They come to the Golgi after being built, and before they go to their destination. In general, what the Golgi does is Much of the enzymatic processing is post-translational modification of proteins. The Golgi complex inspects them for flaws and discards extra material added during their manufacture, wraps them up and then targets them for packaging. The Golgi complex is especially active ...
Endogenous hHK3 localizes to the Golgi complex. The localization of endogenous Hook proteins in Hep2 cells (A, D, G, J, and M) was compared with the Golgi marke
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Eukaryotic cells perform continuous recycling of the plasma membrane proteins and extracellular matrix molecules from the cell surface back to the cytoplasm (for plant cells, see Low and Chandra, 1994; Robinson et al., 1998). Our recent study (Baluška et al., 2002) provides experimental evidence that cell wall pectins are internalized after in muro de-esterification (Micheli, 2001) and cross-linking with calcium and boron (Matoh and Kobayashi, 1998;Kobayashi et al., 1999). These almost exclusive cell wall pectin epitopes, reactive to JIM5 and RGII antibodies, accumulate abundantly within intracellular BFA-induced compartments, which are obviously formed through aggregation of trans-Golgi networks and putative plant endosomes (Baluška et al., 2002). Here, we report that intracellular BFA compartments accumulate these cell wall pectins in meristematic cells of maize and wheat, but not of zucchini and alfalfa, root apices. Intriguingly, boron deprivation inhibits endocytosis of cell wall pectins. ...
XPLDHTNVTA PQASMMFQYF VKVVPTVYMK VDGEAPLPPQ VLRTNQFSVT RHEKVANGLL GDQGLPGVFV LYELSPMMVK LTEKHRSFTH FLTGVCAIIG GMFTVAGLID SLIYHSARAI QKKIDLGKTT ...
The mammalian Golgi complex is composed of stacks of flattened cisternae linked through tubules to form a contiguous juxtanuclear ribbon. The stacked cisternae reflect the compartmentalization of Golgi enzymes for the processing of transiting cargo (Mellman and Simons, 1992; Puthenveedu and Linstedt, 2005). Cargo movement through the stack has been variously suggested to occur in vesicles, in maturing cisternae, or by tubular connections between cisternae (Malhotra et al., 1989; Mollenhauer and Morre, 1991; Glick et al., 1997; Allan and Balch, 1999; Pelham and Rothman, 2000; Trucco et al., 2004). Although not exclusive of other processes, maturation has gained recent support (Emr et al., 2009). This model starts with the creation of cargo-containing cis-Golgi cisternae. The cargo stays within these cisternae and is sequentially processed when the cis enzymes are replaced with medial enzymes, which are subsequently replaced with trans enzymes. As cisternae progress through the Golgi stack, this ...
Supplementary MaterialsAdditional file 1: Table S1. group). Group (A & T), dual therapy with Adr (0.25?g/ml) and Tu (0.8?g/ml); Group (A), monotherapy with Adr (0.25?g/ml), and the control group. The colored dots represent over-expressed or under-expressed genes; the black dots represent unchanged genes. em P /em ? ?0.05. (PPTX 80 kb) 13046_2018_935_MOESM3_ESM.pptx (81K) GUID:?DD86D9AB-143A-41D8-8E65-23ABA4296B81 Additional file 4: Figure S3. Expression levels of CHOP, Cl-PARP and Cl-caspase 3 in SGC7901 detected by IF after treatment with monotherapy or dual therapy for 48?h. The concentrations of drugs were the same as those in Additional file 3: Physique S2. (400 ; scale bar, 50?m.) (PPTX 556 kb) 13046_2018_935_MOESM4_ESM.pptx (556K) GUID:?A2B89A2C-2E37-48C3-8062-7981706090A1 Additional file 5: Figure S4. Brefeldin A (BFA) can mimic the effects of Tu on MDR GC cells. a The effects of Tu on glycoproteins-L1CAM and TIMP1. GC cells were treated with Tu (0.8?g/ml) for 48?h before harvest. All ...
The Golgi apparatus is a packaging center Golgi apparatus or Golgi body or Golgi complex is a membrane-bound organelle, associated with the processing of…
We have studied changes in the Golgi morphology in Madin-Darby canine kidney cells as a result of chemically induced DNA damage, and how such morphological change affects synthesis and sorting of sulphated PGs in the cell line ...
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TY - JOUR. T1 - ADP ribosylation factor 6 regulates neuronal migration in the developing cerebral cortex through FIP3/arfophilin-1-dependent endosomal trafficking of N-cadherin. AU - Hara, Yoshinobu. AU - Fukaya, Masahiro. AU - Hayashi, Kanehiro. AU - Kawauchi, Takeshi. AU - Nakajima, Kazunori. AU - Sakagami, Hiroyuki. PY - 2016. Y1 - 2016. N2 - During neural development, endosomal trafficking controls cell shape and motility through the polarized transport of membrane proteins related to cellcell and cellextracellular matrix interactions. ADP ribosylation factor 6 (Arf6) is a critical small GTPase that regulates membrane trafficking between the plasma membrane and endosomes. We herein demonstrated that the knockdown of endogenous Arf6 in mouse cerebral cortices led to impaired neuronal migration in the intermediate zone and cytoplasmic retention of N-cadherin and syntaxin12 in migrating neurons. Rescue experiments with separation-of-function Arf6 mutants identified Rab11 familyinteracting ...
Transition zones are associated with the Golgi stacks. They are close to each other. This makes sense because the communication is more efficient. Vesicles dont need to travel long distances and the existence of the Golgi apparatus itself depends on a continuous process of vesicle incoming. It has been observed that a new transition zone led quickly to the nearby formation of a new Golgi stack. On the contrary, if a transition zone disappears, the associated Golgi cisternae are also lost. Transition zones can fuse with others and one transition zone can be split in two. Their associated Golgi stacks match this behavior. Vesicles budding from the transition zones are COPII coated vesicles ( COPII: coat protein II; Figure 1). Several proteins are involved in the formation of this COPII molecular framework: Sec16, Sar1 GTPases, Sec23/24 and Sec13/31. In this order, they are assembled at the cytosolic surface of the transition zone membranes. Transition zones are the more suitable environments for ...
Anti-Golgi complex antibodies (AGAs) are primarily associated with systemic lupus erythematosus and Sjögrens syndrome. Here we report on the immunoreactivity of AGAs against five Golgi autoantigens (giantin, golgin-245, golgin-160, golgin-95/GM130, and golgin-97) and provide data from epitope mapping on the most common Golgi autoantigen, namely giantin. A total of 80 human sera containing AGAs, as defined by indirect immunofluorescence on HEp-2 cells, were analyzed by ELISA using recombinant autoantigens and immunoprecipitation. The proportion of AGA sera that reacted with the five Golgi autoantigens was correlated with the molecular mass of the Golgi antigens. Autoantibodies to giantin, the largest Golgi autoantigen, were the predominant AGAs, being found in 50% of the AGA sera. Epitope mapping of giantin was performed using six recombinant fragments spanning the entire protein. Antigiantin-positive sera with low titer autoantibodies recognized epitopes in the carboxyl-terminal fragments that are
Constitutive Secretion: Advanced Look --, 2.) Exocytosis After leaving the Golgi apparatus, proteins following the constitutive secretion pathway merge with the cell membrane and release their cargo by a process called exocytosis. Clicking on each of the thumbnail images will bring up a larger, labeled version of the described scene.. To see the Flash movie for the following sequence of images, click here.. ...
Arl1 (ARF like protein1) is a poorly understood member of ARF family small GTPases. This thesis presents an original characterization of Arl1 and its effectors. Arl1 was localized to the tans Golgi under EM. Over expression of guanine nucleotide mutants of Arl1 dramatically affects the structure and function of Golgi apparatus. Arl1-GTP was found to interact with GRIP domain of Golgins (Golgin-97, Golgin-245, GCC1 and KIAA0336). The interaction was dependent on the conserved amino acids on both switch II region of Arl1 and the GRIP domain. Collectively, the research presented in this thesis reveals Arl1 is a new regulator of Golgi structure and function and one mechanism of Arl1a??s function is that it recruits and regulates its effectors a?? GRIP domain Golgins to Golgi ...
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COPⅠ囊泡:最初研究者利用三磷酸鳥苷(GTP)衍生物GTPγS(一種富含高爾基體膜的細胞質與抗水解的GTP衍生物)共培養時,發現高爾基體池之間存在一種囊泡轉運結構[9](後來在真核細胞中也證實此結構的存在[10])。除了脂質成分外,參與此囊泡形成的成份還有7種外被體蛋白(即外被體α、β、β′、γ、δ、ε、ζ)。這些外被體蛋白相互作用形成的復合物就是COPⅠ囊泡[11][12]。亞單位α、β′、ε在結構上與網格蛋白及COPⅡ囊泡的外層組分具有較高的一致性,形成復合物的內層組分稱為B亞復合物(主要負責與靶蛋白結合),而亞單位β、γ、δ、ζ 與網格蛋白及COPⅡ囊泡的內層組分相似,形成復合物的內層組分稱為F亞復合物,該亞復合物主要負責與靶蛋白結合,並且直接與COPⅠ囊泡形成的招募者ADP核糖基化因子(英语:ADP ribosylation factor)(ADP ribosylation ...
Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis (By similarity).
Figure 2. Flow cytometric characterization of γδ T cells in our patient demonstrates specific expansion of a homogeneous Vδ2+ T cell population. Flow cytometry performed on frozen PBMC either unstimulated for surface markers or PMA/ionomycin/brefeldin A stimulated for intracellular molecules. (A) FACS used to identify live, singlet lymphocytes (not shown), which were gated on to identify CD3+ T cells in the patient and a representative IFX-treated control (HC). CD3+ cells further gated on to identify Vδ1+/Vδ2+ T cells. The indicated plots display markers specific to the Vδ2+ T cell population with gates based on FMO control (not shown). (B) Mass cytometry used to identify live, singlet, CD3+CD14-CD19-TCRγδ+ cells in the patients PBMC for expression of the indicated markers. (C) viSNE analysis performed using 36 markers to cluster PBMC populations in the patient and 5 age-matched male patients with AS. CD3ε, CD4, CD8α, CD14, CD19, CD56, and TCRγδ antigens were used to gate indicated ...
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4423 Purpose: To study the mechanism by which an antibiotic brefeldin A (BFA) inhibits proliferation of androgen-responsive prostatic cancer LNCaP cells, focusing on cell cycle and androgen receptor (AR). Materials and Methods: Androgen-mediated cellular events in LNCaP cells were induced using 5α-dihydrotestosterone (DHT) as an androgenic mediator. Effect of BFA on DHT-stimulated cell growth was first assessed, and its regulatory mechanism(s) was further explored by examining cell cycle and AR activity/expression using flow cytometry, AR binding assay, and Western blot analysis. Results: DHT (1 nM) stimulated LNCaP cell growth by ∼37% above control; however, BFA (30 ng/ml) was capable of completely inhibiting such DHT-stimulated proliferation. Cell cycle analysis showed that this growth inhibition was associated with ∼75% reduction in the cell number in the S phase, indicating a blocking of G1-S phase transition. Such a G1 growth arrest was confirmed by a drastic (,80%) down-regulation of ...
Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. It is made up of two polypeptide chains (A and B) combined in three disulfide-linked dimeric forms (AA, AB, and BB). Here, the biosynthesis and proteolytic processing of the two homodimeric forms of PDGF (AA and BB) were studied in CHO cells stably transfected with A-chain (short splice version) or B-chain cDNA. PDGF-AA was processed to a 30-kD molecule which was secreted from the cells. In contrast, PDGF-BB formed two structurally distinct end products; a minor secreted 30-kD form and a major cell-associated 24-kD form. Immunocytochemical studies at light- and electron-microscopical levels revealed presence of PDGF in the Golgi complex, in lysosomes, and to a smaller extent in the ER. From analysis of cells treated with brefeldin A, an inhibitor of ER to Golgi transport, it was concluded that dimerization occurs in the ER, whereas the proteolytic processing of PDGF-AA and PDGF-BB precursors normally occurs in a ...
View Notes - Lecture 13 11 from BICD 110 at UCSD. Lecture 13 11/02/07 Golgi Structure/Function, Lysosome, Exocytosis Glycosylation Protects lysosome membrane proteins from autodegradation
The protein encoded by this gene resides in the golgi, and constitutes one of the 8 subunits of the conserved oligomeric Golgi (COG) complex, which is required for normal golgi morphology and localization. Mutations in this gene are associated with the congenital disorder of glycosylation type IIe.[provided by RefSeq, May 2010 ...
This book explores the role of sub-cellular trafficking in the pathogenesis, treatment and prevention of neurodegenerative diseases. Recent findings point
Complete information for ARF6 gene (Protein Coding), ADP Ribosylation Factor 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Researchers from Freiburg discovered a novel mechanism that ensures obstacle-free protein traffic into the powerhouse of the cell
Complete information for ARL6IP6 gene (Protein Coding), ADP Ribosylation Factor Like GTPase 6 Interacting Protein 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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Golgi Apparatus Cell function: packages proteins, lipids, enzymes from the ER for storage and secretion Analogy part and function: mailbox holds packages
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Maize root tips were fixed in potassium permanganate, embedded in epoxy resin, sectioned to show silver interference color, and studied with the electron microscope. All the cells were seen to contain an endoplasmic reticulum and apparently independent Golgi structures.. The endoplasmic reticulum is demonstrated as a membrane-bounded, vesicular structure comparable in many aspects to that of several types of animal cells. With the treatment used here the membranes appear smooth surfaced. The endoplasmic reticulum is continuous with the nuclear envelope and, by contact at least, with structures passing through the cell wall. The nuclear envelope is characterized by discontinuities, as previously reported for animal cells. The reticula of adjacent cells seem to be in contact at or through the plasmodesmata. Because of these contacts the endoplasmic reticulum of a given cell appears to be part of an intercellular system.. The Golgi structures appear as stacks of platelet-vesicles which apparently ...
Transcytosis is a type of transcellular transport in which various macromolecules are transported across the interior of a cell. Macromolecules are captured in vesicles on one side of the cell, drawn across the cell, and ejected on the other side. Examples of macromolecules transported include IgA, transferrin, and insulin. While transcytosis is most commonly observed in cells of an epithelium, the process is also present elsewhere. Blood capillaries are a well-known site for transcytosis, though it occurs in other cells, including neurons, osteoclasts and M cells of the intestine. The regulation of transcytosis varies greatly due to the many different tissues in which this process is observed. Various tissue specific mechanisms of transcytosis have been identified. Brefeldin A, a commonly used inhibitor of ER to Golgi apparatus transport, has been shown to inhibit transcytosis in dog kidney cells which provided the first clues as to the nature of transcytosis regulation. Transcytosis in dog ...
Biosynthesis of myeloperoxidase (MPO), a myeloid lysosomal hemoprotein critical for the optimal oxygen-dependent microbicidal activity of human neutrophils, is incompletely understood. The primary translation product undergoes cotranslational N-linked glycosylation with subsequent insertion of the Fe-containing prosthetic group into the peptide backbone, thereby converting the enzymatically inactive, heme- free apoproMPO into the peroxidatively active precursor, proMPO. Eventually, proMPO undergoes proteolytic processing into native, lysosomal MPO, with subunits of 59 and 13.5 Kd. We studied three unanswered questions regarding MPO biosynthesis: (1) At what point during MPO biosynthesis is the heme moiety inserted into the apoenzyme? (2) What consequences does heme-insertion have on subsequent processing events? (3) What role does the mannose-6-phosphate receptor (M6PR) system play in the delivery of MPO to the lysosome? Disruption of Golgi by brefeldin A (BFA) produced two major changes in MPO ...
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
D. Jones, B. Bax, S. Cockcroft; ADP-ribosylation factor GTPases in signal transduction and membrane traffic: independent functions?. Biochem Soc Trans 1 August 1999; 27 (4): 642-647. doi: https://doi.org/10.1042/bst0270642. Download citation file:. ...
Golgi bodies do not need to disassemble to divide, according to results from Uchiyama et al. on page 1067.. In mammalian cells, the Golgi apparatus disassembles into vesicles and short tubules before mitosis. Golgi breakdown requires that two membrane fusion pathways necessary for Golgi reassembly after mitosis be temporarily inhibited. For one, the NSF pathway, this inhibition is achieved by Cdc2-mediated phosphorylation of an NSF-associated factor at early mitosis. But how the cell cycle regulates the second, the p47/p97 pathway, was not known.. Uchiyama et al. have determined that Cdc2-mediated phosphorylation also inhibits the p47/p97 pathway. p97 is an ATPase that binds to the Golgi through its associated factor, p47. Uchiyama et al. find that p47 is phosphorylated by Cdc2 upon entry into mitosis. Phosphorylated p47 bound to p97 in mitotic cells and had a decreased binding affinity for Golgi membranes, thus releasing the complex from the Golgi.. Addition of a phosphorylation-insensitive ...
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Expression of ARFGEF1 (ARFGEP1, BIG1, DKFZP434L057, p200) in liver tissue. Antibody staining with HPA023399 and HPA023822 in immunohistochemistry.
The Golgi body, or Golgi apparatus is a collection of flattened membrane sacks called cisternae that carry out the processing,packaging, and sorting of a variety of cellular products in higher plants and animals.This important cellular organelle was named in honor of Camillo Golgi ,the Italian neuroanatomist who first described it in brain cells.
The protein encoded by this gene is reported to be a component of the Golgi matrix. It may act as a golgin protein by negatively regulating transit of secretory cargo and by acting as a structural scaffold of the Golgi. Alternative splicing results in multiple transcript variants ...
The protein encoded by this gene is reported to be a component of the Golgi matrix. It may act as a golgin protein by negatively regulating transit of secretory cargo and by acting as a structural scaffold of the Golgi. Alternative splicing results in multiple transcript variants ...
Question 1 Identify the structure highlighted in light yellow | | plasma membrane | | | endoplasmic reticulum | | | Golgi apparatus | | |
Systems and processes of controlling a function of a person support apparatus are provided. An example system includes a person support apparatus adapted to support a patient. The person support apparatus comprising a controller adapted to communicatively couple with at least one removable component of the person support apparatus. The controller is adapted to determine the absence or presence of the at least one removable component. In response to the determination, the controller is further adapted to disable at least one movement of the person support apparatus in response to a determination that the at least one removable component is not present or enable the at least one movement in response to a determination that the at least one removable component is present.
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Fungal highly reducing polyketide synthases (HRPKSs) are an enigmatic group of multidomain enzymes that catalyze the biosynthesis of structurally diverse compounds. This variety stems from their intrinsic programming rules, which permutate the use of tailoring domains and determine the overall number of iterative cycles. From genome sequencing and mining of the producing strain Eupenicillium brefeldianum ATCC 58665, we identified an HRPKS involved in the biosynthesis of an important protein transport-inhibitor Brefeldin A (BFA), followed by reconstitution of its activity in Saccharomyces cerevisiae and in vitro. Bref-PKS demonstrated an NADPH-dependent reductive tailoring specificity that led to the synthesis of four different octaketide products with varying degrees of reduction. Furthermore, contrary to what is expected from the structure of BFA, Bref-PKS is found to be a nonaketide synthase in the absence of an associated thiohydrolase Bref-TH. Such chain-length control by the partner ...
Coloured scanning electron micrograph (TEM) of Golgi apparatus, stacks of cisternae and vesicles (Euglena sp.). The Golgi apparatus is a cell organelle in all plant and animal cells. The apparatus consists of flattened membrane bound sacs located close to the endoplasmic reticulum. The Golgi apparatus receives proteins and lipids (fats) from the rough endoplasmic reticulum. It modifies some of them and sorts, concentrates and packs them into sealed droplets called vesicles. Depending on the contents these are despatched to one of three destinations: within the cell to lysosomes; to the cell plasma membrane; outside the cell. . Magnification: x11,010 when shortest axis printed at 25 millimetres. - Stock Image C032/1221
This assay is used to look for the responsiveness of T cells to a specific antigenic stimulation. Stimulation can be performed with mononuclear cells isolated from PBMC or whole blood. The assay is based on the principle by treating cells with an inhibitor of the secretory pathway to prevent secretion of the cytokine (e.g brefeldin A or monensin) the cytokines accumulate inside the cytoplasm and can be detected by staining the fixed and permeabilized cells.. By combining the intracellular cytokine stain with staining for phenotypic markers (as well as tetramers) it is possible to determine the type of cells that produce the cytokine as well as the quantity of cytokine produced per cell. This assay requires larger sample volumes than the ELISPOT but is the only assay that determines simultaneously the type of cytokine produced by a single cell and the phenotype of such a cell.. ...
BMI and waist circumference similarly predictincident heart failure (40). In such a case, PBPK modelingof the concentration time course in the target tissue fordifferent dosing routes or regimens might be necessary.For developmental toxicity, windows of susceptibilitymust also be considered. One obvious reason is that not everyone involved in communica-tion disorders research is necessarily a member of ASHA. Lin X buy modafinil in europe El-Sayed MS, Waterhouse J, Reilly T.Activation and disturbance of blood haemostasis fol-lowing strenuous physical exercise. observed using shuffling gait with hips buy modafinil in europe and trunk in slight flexion. Theflattened cisternaelocatedclosesttotherERrepresent the forming face buy modafinil in europe or the cis-Golgi network (CGN);the cisternae located away from the rER represent the maturingface, orthetrans-Golgi network (TGN); (Figs. Because of associatedneurobehavioral difficulties, DLB may be more commonin clinic cohorts, compared to the community ...
Interleukin 5 (IL-5) is pre-dominantly secreted by CD4+ T cells. It is involved in a range of allergic reactions and mediates immune reactions against parasites. IL-5 also acts on other cell types such as B cells. The Anti-IL-5 antibody has been designed for intracellular staining of IL-5-producing cells. Cells can be stimulated for IL-5-production, for example, by polyclonal stimulation with mitogens. For induction of IL-5 production by antigen-specific T cells, cells are restimulated with respective antigen. IL-5 can be accumulated in the cells by addition of secretion inhibitors like brefeldin A. After fixation and permeabilization of the cell sample, IL-5-producing cells can be stained intracellularly with Anti-IL-5 antibodies. Staining of surface markers allows simultaneous flow cytometric analysis of subsets and activation status of the IL-5-producing cells. Magnetically enriched cells can be stained intracellularly for IL-5 production directly on the MACS® Column. This procedure ensures higher
Similar to Golgi resident protein GCP60; Acyl-CoA-binding domain-containing protein 3; Golgi complex-associated protein 1; GOCAP1; Golgi phosphoprotein 1; GOLPH1; PBR- and PKA-associated protein 7; Peripheral benzodiazepine receptor-associated protein PAP7 ...
The Golgi apparatus is a relatively large, membrane-bound organelle and thus one of the easiest cell structures to study in detail [2]. The organelle is located nearby the cell nucleus and is closely associated with the endoplasmic reticulum. By observing via metallic impregnation, it can be seen through phase contrast microscopy that the Golgi has a convoluted, dense and "ill-formed" morphology [3]. Initial studies have shown that the organelle has great variance in its form dependent on the type of cell it is in as well as the state of activity that the cell is in. There are roughly around 40-100 Golgi apparatus stacks within a mammalian cell [4]. Overall, the Golgi apparatus is made of 4-8 flattened, membrane-bound sacs that are stacked upon one another [5]. These are known as cisternae. The Golgi also includes associated nearby vesicles. Each cisterna primarily contains products from the endoplasmic reticulum, which enter the Golgi at the cis face - the end that is closest to the ER and ...
The Golgi apparatus is a relatively large organelle and thus one of the easiest cell structures to study in detail [3]. The organelle is located nearby the cell nucleus and is closely associated with the endoplasmic reticulum. By observing via metallic impregnation, it can be seen through phase contrast microscopy that the Golgi has a convoluted, dense and "ill-formed" morphology [4]. Initial studies have shown that the organelle has great variance in its form dependent on the type of cell it is in as well as the state of activity that the cell is in. There are roughly around 40-100 Golgi apparatus stacks within a mammalian cell [5]. Overall, the Golgi apparatus is made of 4-8 flattened, membrane-bound sacs that are stacked upon one another [6]. These are known as cisternae. The Golgi also includes associated nearby vesicles. Each cisterna primarily contains products from the endoplasmic reticulum, which enter the Golgi at the cis face - the end that is closest to the ER and accepts incoming ...
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Expression of ARFGEF1 (ARFGEP1, BIG1, DKFZP434L057, p200) in spleen tissue. Antibody staining with HPA023399 and HPA023822 in immunohistochemistry.
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Cisterna definition, definition of cisterna, Anagrams of cisterna, words that start with Cisterna, and words that can be created from cisterna
also called the Golgi apparatus or golgi complex) a flattened, layered, sac-like organelle that looks like a stack of pancakes and is located near the nucleus. It produces the membranes that surround the lysosomes. The Golgi body packages proteins a ...
Our view of what happens to the Golgi and ER during mitosis in mammalian cells has been shaken once more. Rather than the Golgi contents being recycled through, or mixed with the ER, two recent studies taking complementary approaches, find that the contents of these organelles remain separate throughout mitosis.
Proposition 116 Allocation Amendment - City of Red Bluff - Red Bluff Park & Ride Facility. PPNO: 02-2507. EA: T0206A. Red Bluff is requesting to de-allocate $24,695 out of the $220,000 allocated under BFP-99-11 to close out FTA 02A0332. Red Bluff requests taht the $24,695 be added to $280,000 that are programmed but not allocated for the construction of the Park & Ride Facility, for a total allocation of $304,695 ...
Former fashion director at Vogue, Lucinda Chambers at London Fashion Week in February 2017.Image: Hunter Abrams/BFA/REX/Shutterstock The inner machinations of Vogue have been a source of intrigue and fascination for many years now. But, one former British Vogue editor just lifted the lid on what its really like to work at Vogue. And, her account […]. Read More ». ...
... - Clinical trials, Fialuridine, TGN This page was last edited on 20 May , at In addition, no signs of toxicity were observed in any of the physiological
There are a few stackable SARMs that are proving prime results. My best choice are LGD-4033 and Ostarine together. LGD-4033 is one of those SARMs that
TY - JOUR. T1 - Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells. T2 - Localization to the trans-Golgi network and recycling from the cell surface. AU - Varlamov, Oleg. AU - Fricker, Lloyd D.. PY - 1998. Y1 - 1998. N2 - Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be involved in the post-translational processing of peptides and proteins that transit the secretory pathway. In the present study, the intracellular distribution of CPD was examined in AtT-20 cells, a mouse anterior pituitary-derived corticotroph. Antisera to CPD stain the same intracellular structures as those labeled with furin and wheat germ agglutinin. This distribution is distinct from carboxypeptidase E, which is localized to the secretory vesicles in the cell processes. The perinuclear distribution of CPD is detected even when the AtT-20 cells are treated with brefeldin A for 1-30 minutes, suggesting that CPD is present in the ...
Ver más] The small GTP-binding protein ADP-ribosylation factor 1 (ARF1) is an essential component of the molecular machinery that catalyzes the formation of membranebound transport intermediates. By using an in vitro assay that reproduces recruitment of cytosolic proteins onto purified, high salt-washed Golgi membranes, we have analyzed the role of cAMP-dependent protein kinase A (PKA) on ARF1 incorporation. Addition to this assay of either pure catalytic subunits of PKA (C-PKA) or cAMP increased ARF1 binding. By contrast, ARF1 association was inhibited following C-PKA inactivation with either PKA inhibitory peptide or RIIa as well as after cytosol depletion of C-PKA. C-PKA also stimulated recruitment and activation of a recombinant form of human ARF1 in the absence of additional cytosolic components. The binding step could be dissociated from the activation reaction and found to be independent of guanine nucleotides and saturable. This step was stimulated by C-PKA in an ATP-dependent manner. ...
Tumor necrosis factor alpha (TNF-α) is produced by cells that are involved in inflammatory immune responses. TNF-α is secreted by activated CD4+ T cells, monocytes, macrophages, NK cells, and neutrophils.Anti-TNF-α antibodies have been designed for intracellular staining of TNF-α-producing cells. Cells can be stimulated for TNF-α production, for example, by polyclonal stimulation with mitogens. For induction of TNF-α production by antigen-specific T cells, cells are restimulated with the respective antigen. TNF-α can be accumulated in the cells by addition of secretion inhibitors like brefeldin A. After fixation and permeabilization of the cell sample, TNF-α-producing cells can be stained intracellularly with Anti-TNF-α antibodies. Staining for surface markers allows simultaneous flow cytometric analysis of subsets and activation status of the TNF-α-producing cells. - Lëtzebuerg
Natural cell death is a well-known degenerative phenomenon occurring during development of the nervous system. The role of trophic molecules produced by target and afferent cells as well as by glial cells has been extensively demonstrated. Literature data demonstrate that cAMP can modulate the survival of neuronal cells. Cultures of mixed retinal cells were treated with forskolin (an activator of the enzyme adenylyl cyclase) for 48 h. The results show that 50 M forskolin induced a two-fold increase in the survival of retinal ganglion cells (RGCs) in the absence of exogenous trophic factors. This effect was dose dependent and abolished by 1 M H89 (an inhibitor of protein kinase A), 1.25 M chelerythrine chloride (an inhibitor of protein kinase C), 50 M PD 98059 (an inhibitor of MEK), 25 M Ly 294002 (an inhibitor of phosphatidylinositol-3 kinase), 30 nM brefeldin A (an inhibitor of polypeptide release), and 10 M genistein or 1 ng/ml herbimycin (inhibitors of tyrosine kinase enzymes). The inhibition ...
Golgi Dynamics. How can it happen that the resident proteins appear to remain in place while the transient proteins, destined for other sites in the cell, move through the organelle in a cis to trans direction?. Over the years a number of ideas have been put forth they fall into two general models.. 1. Vesicle Transport Model. This model assumes that the cisternae are essentially stationary and contain their resident proteins. The transient proteins are selected and concentrated in vesicles by the process of vesicle formation that is driven by coat proteins and their interaction with cargo receptor proteins as described in the last lecture. See vesicle formation animation for review of how this works.. These transport vesicles bud from the periphery of the Golgi cisterna as shown in the picture above, and then fuse with the appropriate target cisterna (trans to the point of origin) via the normal vesicle targeting process. In this manner a transient protein makes is way down the Golgi stack, cis ...
golgi transport 1 homolog B products available through Novus Biologicals. Browse our golgi transport 1 homolog B product catalog backed by our Guarantee+.
Mouse anti Human ACBD3 antibody, clone 2G2 recognizes human Golgi resident protein GCP60, also known as ACBD3, acyl-CoA-binding domain-con
UPSEE UPTU Entrance Exam 2017 1st year B.Tech /B.Arch./B.Pharm./ BHMCT/BFAD/BFA & 2nd year in B.Tech and B.Pharm (Lateral Entry) Syllabus & paper Pattern Scheme
Accentuăm, cu riscul repetiției, următorul lucru însă:. *Invitații, indiferent de mediul artistic din care provin, vin și pun muzica lor preferată de pe suportul lor preferat. Publicul, select și el la rândul lui, respectă invitatul acordându-i credit și atenție, fără să intervină în spațiul său intim și privat și fără să îi conteste gusturile muzicale.. *Auditoriul, informat înainte de a veni la spectacol, în legătură cu produsul performativ ce urmează să îl primească, în urma cercetării proprii, sau în urma experienței muzicale sau chiar din documentația evenimentului se bucură alături de cei ce pun muzică și de personalul din club, urmând astfel să se formeze o legătură specială între cei implicați.. Selecția o face Omu Gnom. Atenția o primește de la Dan Basu.. ………………………………………………... Omu Gnom a făcut Sociologie și este în ciuda aparenței unul din "bătrânii" rap-ului românesc. A colaborat printre ...
Vesicles are small membrane-bound structures containing materials for export. They combine with the outer cell membrane, releasing their contents. Epithelial cells form lining layers. ...
Brefeldin A and blazein were isolated from A. subrufescens.[citation needed] Boletus badius has been shown to synthesize ... Subsequent discoveries included alamethicin, aphidicolin, brefeldin A, Cephalosporin, cerulenin, citromycin, eupenifeldin, ...
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the GBF1 ... Niu TK, Pfeifer AC, Lippincott-Schwartz J, Jackson CL (2005). "Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor ... "Entrez Gene: GBF1 golgi-specific brefeldin A resistance factor 1". Nakajima D, Okazaki N, Yamakawa H, et al. (2003). " ...
... is an anamorph fungus species of the genus of Penicillium which produces Brefeldin A a fungal ... brefeldin a). Formation in Penicillium brefeldianum". Tetrahedron. 39 (21): 3507-13. doi:10.1016/S0040-4020(01)88660-9. An, C. ... brefeldin a). Formation in Penicillium brefeldianum". Tetrahedron. 39 (21): 3507-13. doi:10.1016/S0040-4020(01)88660-9. ...
Nassoury, N., Wang, Y., & Morse, D. (2005). Brefeldin a inhibits circadian remodeling of chloroplast structure in the ...
... produces xanthomegin, brefeldin A and janthitrem B Rudd, L. E.; Perry, J. J.; Houk, V. S.; Williams, R. W ...
Saito T, Tanaka M, Yamaguchi I (November 1996). "Effect of brefeldin A on influenza A virus-induced apoptosis in vitro". J. Vet ...
... produces fatty acid, Brefeldin A and the antibiotic Cyanein Koman, V.; Betina, V.; BaráTh, Z. (1969). " ...
The major mechanism of action of Brefeldin A is through inhibition of ARF1. ARF1 has been shown to interact with: CHRM3, COPB1 ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 1 is a protein that in humans is encoded by the ARFGEF1 gene. ADP- ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ... Shen X, Hong MS, Moss J, Vaughan M (Jan 2007). "BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required ... It contains a Sec7 domain, which may be responsible for the guanine-nucleotide exchange activity and also the brefeldin A ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 2 is a protein that in humans is encoded by the ARFGEF2 gene. ADP- ... Xu KF, Shen X, Li H, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2005). "Interaction of BIG2, a brefeldin A-inhibited guanine ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ... Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ...
"LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function". J Cell Biol. 127 (3): 679- ...
Xu KF, Shen X, Li H, Pacheco-Rodriguez G, Moss J, Vaughan M (2005). "Interaction of BIG2, a brefeldin A-inhibited guanine ...
... domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)". Proc. Natl. Acad. Sci. U.S.A. 100 (4): 1627-32 ...
Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A- ...
Penicillin, cephalosporins, fusafungine, usnic acid, fusidic acid, fumagillin, brefeldin A, verrucarin A, alamethicin, are ...
Skop AR, Bergmann D, Mohler WA, White JG (May 2001). "Completion of cytokinesis in C. elegans requires a brefeldin A-sensitive ...
Brefeldin A is a very common inducer of the unfolded protein response or endoplasmic reticulum stress response (ER stress). ...
"Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of ... "Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of ...
"A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1". Cell. 69 (4): 625-35. doi: ...
... a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding ...
It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. It may ...
Brefeldin A (BFA) is a fungal metabolite used experimentally to disrupt the secretion pathway as a method of testing Golgi ...
AP-1 complex-associated regulatory protein (Gamma1-adaptin brefeldin A resistance protein) is a protein that in humans is ...
PIN3 is normally localized to the surface of hypocotyl and stem, but is also internalized in the presence of Brefeldin A (BFA ...
... membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46". The ...
Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) has been identified recently as a novel regulator of ... From: Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) is predicted to interact with its partner through an ...
Home » cDNA » Mouse cDNA » Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A- ... Properties for Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ... MC224976 Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ... "Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), ( ...
"SAFETY DATA SHEET Brefeldin A" (PDF). Cayman Chemical. 6 February 2015. "Material Safety Data Sheet. Brefeldin A (BFA) sc- ... Brefeldin A is a lactone antiviral produced by Eupenicillium brefeldianum. Brefeldin A inhibits protein transport from the ... "Brefeldin A (CAS 20350-15-6)". Santa Cruz Biotechnology. 8 May 2017. "Brefeldin A Supplier , CAS 20350-15-6 , Tocris Bioscience ... Brefeldin A was initially isolated with hopes to become an antiviral drug but is now primarily used in research to study ...
... brefeldin-A (brefeldin-A) in liquid culture by Eupenicillium brefeldianum, (B. Dodge) Stolk and Scott, ATCC... ... 7-epi-brefeldin A, a co-metabolite of brefeldin A inCurvularia lunata. J Chem Soc Perkin Trans I: 2387-2390.Google Scholar ... Fermentation conditions are described for the production of the antitumor antibiotic 7-(S)-brefeldin-A (brefeldin-A) in liquid ... brefeldin-A Eupenicillium brefeldianum antitumor antibiotic This is a preview of subscription content, log in to check access. ...
1000x Brefeldin A Solution, 1000x Life Sciences:Protein Biology:Antibody and Dye Based Assays ... Invitrogen eBioscience Brefeldin A Solution, 1000x Addition of Brefeldin A during the last hours of in vitro activation of ... Brefeldin A is an inhibitor of intracellular protein transport. *Incubation of cells in culture with Brefeldin A leads to ... Brefeldin A is effective for enhanced detection of a majority of mouse and human intracellular cytokines; however, it is ...
Wood SA, Park JE, and Brown WJ (1991) Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early ... Lippincott-Schwartz J, Yuan L, Tipper C, Amherdt M, Orci L, and Klausner RD (1991) Brefeldin As effects on endosomes, ... Hess MW, Müller M, Debbage PL, Vetterlein M, and Pavelka M (2000) Cryopreparation provides new insight into Brefeldin A-effects ... Klausner RD, Donaldson JG, and Lippincott-Schwartz J (1992) Brefeldin A: insights into the control of membrane traffic and ...
... without Brefeldin A) is a pre-mixed cocktail with optimized concentration of PMA (phorbol 12-myristate-13-acetate) and ... Generally, Brefeldin A is more toxic for longer term incubations, so for shorter stimulations (6 hrs or less) use Brefeldin A. ... The Brefeldin A solution freezes at 4°C . Is the solution still OK? We recommend to thaw in warm water after removing from the ... The Brefeldin A is dissolved in DMSO, which freezes at 18°C, so this is normal. No one has reported any problems with the ...
... hydrolyzes brefeldin A to brefeldin A acid & also hydrolyzes ethyl valerate; 372 amino acids; amino acid sequence given in ... brefeldin A esterase. Subscribe to New Research on brefeldin A esterase hydrolyzes brefeldin A to brefeldin A acid & also ...
Brefeldin A supplier , purchase Brefeldin A , Brefeldin A cost , Brefeldin A manufacturer , order Brefeldin A , Brefeldin A ... with half-maximal inhibition at 2 μM Brefeldin A. Brefeldin A prevents a wide variety of membrane traffic pathways. Brefeldin A ... 3] Brefeldin A induces fusion of the Golgi apparatus with the ER. Brefeldin A abolishes the inhibitory effect of the CERT ... The administration of 25 ng/mL of Brefeldin A completely blocks growth of HF4.9 and HF28RA cells, whereas higher Brefeldin A ...
Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes.. Wood SA1, Park JE, Brown WJ. ... Brefeldin A (BFA) is a fungal metabolite that causes a redistribution of the stacked cisternae of the Golgi complex into the ...
ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited)Imported. ,p>Information which has been ... brefeldin A-inhibited guanine nucleotide-exchange protein 1 isoform X1. Austrofundulus limnaeus ... tr,I3K9S1,I3K9S1_ORENI ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited) OS=Oreochromis ...
Brefeldin A is thus a specific inhibitor of antigen processing for class I-restricted T cell recognition. Its effect on antigen ... Brefeldin A, a specific inhibitor of exocytosis, completely and reversibly inhibited the presentation of viral proteins, but ... The effect of brefeldin A on antigen presentation correlated with its inhibition of intracellular transport of newly ... Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes ...
Indeed, like beta-COP, ARF is dissociated from the Golgi complex by treatment with brefeldin A and brefeldin A prevents ARF ... Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF.. Helms JB1, ... Brefeldin A added to cells causes the rapid and reversible dissociation of a Golgi-associated peripheral membrane protein (M(r ... 12; and D. J. Palmer et al., manuscript submitted), so the primary effect of brefeldin A seems to be on the reaction ...
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 - Q92538 (GBF1_HUMAN) ...
brefeldin A-inhibited guanine nucleotide-exchange protein;. CA,. calyculin A;. GEP,. guanine nucleotide-exchange protein;. GTP ... Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration ... Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein ... Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein ...
Brefeldin A] [20350-15-6] , Buy and find out price and availability, MSDS, properties of TCIs high quality specialty chemicals ... Brefeldin A: A Macrolide Lactone Antibiotic used as an Inhibitor of Protein Trafficking and Secretion. Brefeldin A (BFA) is a ... Brefeldin A: deciphering an enigmatic inhibitor of secretion (a review) *A. Nebenführ, C. Ritzenthaler, D. G. Robinson, Plant ... Brefeldin A: insights into the control of membrane traffic and organelle structure (a review) *R. D. Klausner, J. G. Donaldson ...
Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells. Robert B. Simon, ... Purpose: To study the mechanism by which an antibiotic brefeldin A (BFA) inhibits proliferation of androgen-responsive ... Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells ... Regulation of cell cycle and androgen receptor by brefeldin A in androgen-responsive prostate cancer cells ...
Home » Brefeldin A, a Cytotoxin from an Endophytic Fungal Strain of Eupenicillium brefeldianum Isolated from Arisaema ... Brefeldin A, a Cytotoxin from an Endophytic Fungal Strain of Eupenicillium brefeldianum Isolated from Arisaema erubescens. ... The toxic metabolite was determined as brefeldin A (BFA) based on nuclear magnetic resonance techniques and fast atom ...
Brefeldin A (BFA) was the most successful at inducing lipid accumulation and was used to evaluate secondary screens including ... Phenotypic screening identifies Brefeldin A/Ascotoxin as an inducer of lipid storage in the algae Chlamydomonas reinhardtii ... Brefeldin A (BFA) was the most successful at inducing lipid accumulation and was used to evaluate secondary screens including ...
Apoptosis, caspase activity, NSC 95397, brefeldin A National Category Medical and Health Sciences Identifiers. URN: urn:nbn:se: ... Conclusion: NSC 95397, brefeldin A, bortezomib and sanguinarine induced caspase-3 activation with modest changes in nuclear ... The most active agents were brefeldin A, emetine, bortezomib and idarubicin, having IC50 values (the concentration of the drug ... The aim of this study was to investigate the apoptosis resulting from NSC 95397, brefeldin A, bortezomib and sanguinarine in ...
Literature References: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity. Produced by Penicillium brefeldianum Dodge: E. Haerri et al., Helv. Chim. Acta 46, 1235 (1963). Also produced by P. decumbens: V. L. Singleton et al., Nature 181, 1072 (1958); P. cyaneum: V. Betina et al., Folia Microbiol. 7, 353 (1962). Structure: H. P. Sigg, Helv. Chim. Acta 47, 1401 (1964). Abs configuration: H. P. Weber et al., ibid. 54, 2763 (1971). Synthesis of (±)-form: E. J. Corey, R. H. Wollenberg, Tetrahedron Lett. 1976, 4705; E. J. Corey et al., ibid. 1977, 2243; R. Baudouy et al., ibid. 2973; P. A. Bartlett, F. R. Green, J. Am. Chem. Soc. 100, 4548 (1978); A. E. Greene et al., ibid. 102, 7583 (1980); M. Honda et al., Tetrahedron Lett. 1981, 2679. Total synthesis of (+)-form: T. Kitahara et al., ibid. 1979, 3021. Biosynthesis: B. E. Cross, P. Hendley, Chem. Commun. 1975, 124; C. R. Hutchinson et al., J. Am. Chem. Soc. 103, 2474, 2477 (1981); M. Sunagawa et al., J. ...
The two most widely used reagents are monensin and brefeldin A (BFA). These reagents differ somewhat in their mode of action, ... The Fungal Metabolite Brefeldin A Inhibits Dvl2-Plk1-Dependent Primary Cilium Disassembly. *Uijeong Lee, Sun-Ok Kim, +6 authors ... Brefeldin A, but not monensin, completely blocks CD69 expression on mouse lymphocytes: efficacy of inhibitors of protein ... article{Nylander1999BrefeldinAB, title={Brefeldin A, but not monensin, completely blocks CD69 expression on mouse lymphocytes: ...
Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi ... Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi ... cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment ... Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green ...
Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. R W Doms R W Doms ... Brefeldin A (BFA) has been reported to block protein transport from the ER and cause disassembly of the Golgi complex. We have ... R W Doms, G Russ, J W Yewdell; Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum.. J ... Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. ...
Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. ... S G Miller, L Carnell, H H Moore; Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to ... In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their ... Recent studies using the fungal metabolite brefeldin A (BFA) have provided important insights into the dynamics and the ...
  • manuscript submitted), so the primary effect of brefeldin A seems to be on the reaction responsible for ARF binding. (nih.gov)
  • The effect of brefeldin A (BFA) on generation of transport vesicles, synthesis of phospho-glycerides, sphingosine and ceramides, and utilization of the sphingolipid precursors in the formation of sphingomyelin and glycosphingolipids in Golgi was investigated. (naver.com)
  • Brefeldin A exerts its cytotoxic effects mainly by inducing differentiation and apoptosis in tumor cells. (selleckchem.com)
  • Apart from B-CLL cells, Brefeldin A reportedly causes apoptosis in multiple myeloma (U266, NCI-H929), Jurkat, HeLa, leukaemia (HL60, K562, BJAB), colon (HT-29) and prostate, as well as adenoid cystic sarcoma cells. (selleckchem.com)
  • The aim of this study was to investigate the apoptosis resulting from NSC 95397, brefeldin A, bortezomib and sanguinarine in neuroendocrine tumor cell lines. (diva-portal.org)
  • Lippincott-Schwartz J, Yuan L, Tipper C, Amherdt M, Orci L, and Klausner RD (1991) Brefeldin A's effects on endosomes, lysosomes, and TGN suggests a general mechanism for regulating organelle structure and membrane traffic. (springer.com)
  • Hess MW, Müller M, Debbage PL, Vetterlein M, and Pavelka M (2000) Cryopreparation provides new insight into Brefeldin A-effects on the structure of the HepG2 Golgi apparatus. (springer.com)
  • Brefeldin A induces fusion of the Golgi apparatus with the ER. (selleckchem.com)
  • Brefeldin A treatment, which induces fusion of the Golgi apparatus and the ER, rescues the limonoid-induced prevention of sphingomyelin biosynthesis. (selleckchem.com)
  • Brefeldin A (BFA) causes a block in the secretory system of eukaryotic cells by inhibiting vesicle formation at the Golgi apparatus. (semanticscholar.org)
  • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. (rupress.org)
  • Brefeldin A (BFA) has a profound effect on the structure of the Golgi apparatus, causing Golgi proteins to redistribute into the ER minutes after drug treatment. (rupress.org)
  • Brefeldin A, a commonly used inhibitor of ER to Golgi apparatus transport, has been shown to inhibit transcytosis in dog kidney cells which provided the first clues as to the nature of transcytosis regulation. (wikipedia.org)
  • Two transcript variants encoding different isoforms have been found for this gene, and a brefeldin A-sensitive association of RII-alpha protein with one of the isoforms has been demonstrated in the Golgi apparatus. (wikipedia.org)
  • Here we report the discovery of an enzyme in a Golgi-enriched fraction that catalyses guanine nucleotide (GDP-GTP) exchange on ARF-1 protein, and which is inhibited by brefeldin A. We suggest that activation of ARF proteins for membrane localization by compartmentalized exchange enzymes is in general the first committed step in membrane transformation pathways. (nih.gov)
  • Brefeldin A-inhibited guanine nucleotide-exchange proteins (GEPs) BIG1 and BIG2 activate ADP-ribosylation factor (ARF) GTPases, which are required for vesicular trafficking. (pnas.org)
  • Of these, Brefeldin A (BFA) was the most successful at inducing lipid accumulation and was used to evaluate secondary screens including measuring levels of fatty acids, photosynthetic pigments, proteins and carbohydrates. (unl.edu)
  • We have studied the effects of Brefeldin A (BFA) on the distribution of several SV membrane proteins (synaptophysin, synaptotagmin, synaptobrevin, p29, SV2 and rab3A) and on endosomal markers to investigate the relationship between SVs and the membranes with which they interact in cultured hippocampal neurons developing in isolation. (unimi.it)
  • These data are consistent with a model in which polarized sorting of basolateral membrane proteins occurs via a brefeldin-A-sensitive process of segregation into basolateral recycling vesicles. (elsevier.com)
  • Addition of Brefeldin A during the last hours of in vitro activation of cells results in enhanced detection of intracellular cytokines. (fishersci.com)
  • 1994. Enantioselective synthesis of the antifungal, antiviral and antimitotic compound, (+)-brefeldin A. J Chem Soc Chem Comm 4: 483-484. (springer.com)
  • Wagner M, Rajasekaran AK, Hanzel DK, Mayor S, and Rodriguez-Boulan E (1994) Brefeldin A causes structural and functional alterations of the trans -Golgi network of MDCK cells. (springer.com)
  • Phenotypic screening identifies Brefeldin A/Ascotoxin as an inducer o" by Nishikant Wase, Boqiang Tu et al. (unl.edu)
  • Two ≈200-kDa brefeldin A-inhibited GEPs, BIG 1 and BIG2, first purified together in macromolecular complexes from bovine brain ( 6 ), are 74% identical in overall amino acid sequences, with 90% identity in their Sec7 domains ( 7 ). (pnas.org)
  • Our studies of living, polarized cells show that disrupting endocytosis with brefeldin-A rapidly destroys the polarity of transferrin receptors in MDCK cells while having no effect on tight junctions. (elsevier.com)
  • Brefeldin A added to cells causes the rapid and reversible dissociation of a Golgi-associated peripheral membrane protein (M(r) 110,000) which was found to be identical to one of the subunits of the coat of Golgi-derived (non-clathrin) coated vesicles, beta-COP, implying that brefeldin A prevents transport by blocking the assembly of coats and thus the budding of enclosed vesicles. (nih.gov)
  • Brefeldin A was initially isolated with hopes to become an antiviral drug but is now primarily used in research to study protein transport. (wikipedia.org)
  • Human peripheral blood lymphocytes were stimulated with Cell Activation cocktail without Brefeldin A for six hours, then surface stained with CD3 APC and CD154 (clone 24-31) Brilliant Violet 421™ (top) or CD25 (clone BC96) PE (bottom). (biolegend.com)
  • Cell Activation Cocktail (without Brefeldin A) is a pre-mixed cocktail with optimized concentration of PMA (phorbol 12-myristate-13-acetate) and ionomycin. (biolegend.com)
  • Cell Activation Cocktail (without Brefeldin A) is composed of PMA and ionomycin. (biolegend.com)
  • Conclusion: NSC 95397, brefeldin A, bortezomib and sanguinarine induced caspase-3 activation with modest changes in nuclear morphology. (diva-portal.org)
  • Nevertheless, this candida species can be a meals spoilage agent, having the ability to conquer several harsh circumstances that are used in the meals industry to keep up the microbial balance of its Keratin 7 antibody items and avoid unwanted changes Brefeldin A within their organoleptic properties (Wayne and Stratford, 2003). (healthconnectionsvt.org)