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The release of cytokines, chemokines, and other immune-modulating mediators released from innate immune cells, including eosinophils, neutrophils, macrophages, dendritic cells, mast cells, and epithelial cells, is an important event in immunity. Cytokine synthesis and transportation occurs through the canonical protein trafficking pathway associated with endoplasmic reticulum and Golgi. How cytokines are released upon their exit from the trans-Golgi network varies enormously between cell types, and in many cells this has not yet been characterized. This issue delves into the plethora of cytokines released by innate immune cells, and where possible, shines light on specific mechanisms that regulate trafficking and release of Golgi-derived vesicles. Each cell type also shows varying degrees of dependency on microtubule organization and actin cytoskeleton remodeling for cytokine secretion. Understanding the mechanisms of cytokine secretion will reveal the inner workings of individual innate immune cell types, and allow identification of critical regulatory steps in cytokine release.
Cytokines. --- Chemokines. --- secretory granules --- Dendritic Cells --- GTPases --- SNAREs --- Neutrophils --- Epithelial Cells --- degranulation --- Macrophages --- Recycling endosomes --- Eosinophils
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The release of cytokines, chemokines, and other immune-modulating mediators released from innate immune cells, including eosinophils, neutrophils, macrophages, dendritic cells, mast cells, and epithelial cells, is an important event in immunity. Cytokine synthesis and transportation occurs through the canonical protein trafficking pathway associated with endoplasmic reticulum and Golgi. How cytokines are released upon their exit from the trans-Golgi network varies enormously between cell types, and in many cells this has not yet been characterized. This issue delves into the plethora of cytokines released by innate immune cells, and where possible, shines light on specific mechanisms that regulate trafficking and release of Golgi-derived vesicles. Each cell type also shows varying degrees of dependency on microtubule organization and actin cytoskeleton remodeling for cytokine secretion. Understanding the mechanisms of cytokine secretion will reveal the inner workings of individual innate immune cell types, and allow identification of critical regulatory steps in cytokine release.
Cytokines. --- Chemokines. --- secretory granules --- Dendritic Cells --- GTPases --- SNAREs --- Neutrophils --- Epithelial Cells --- degranulation --- Macrophages --- Recycling endosomes --- Eosinophils
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The release of cytokines, chemokines, and other immune-modulating mediators released from innate immune cells, including eosinophils, neutrophils, macrophages, dendritic cells, mast cells, and epithelial cells, is an important event in immunity. Cytokine synthesis and transportation occurs through the canonical protein trafficking pathway associated with endoplasmic reticulum and Golgi. How cytokines are released upon their exit from the trans-Golgi network varies enormously between cell types, and in many cells this has not yet been characterized. This issue delves into the plethora of cytokines released by innate immune cells, and where possible, shines light on specific mechanisms that regulate trafficking and release of Golgi-derived vesicles. Each cell type also shows varying degrees of dependency on microtubule organization and actin cytoskeleton remodeling for cytokine secretion. Understanding the mechanisms of cytokine secretion will reveal the inner workings of individual innate immune cell types, and allow identification of critical regulatory steps in cytokine release.
Cytokines. --- Chemokines. --- secretory granules --- Dendritic Cells --- GTPases --- SNAREs --- Neutrophils --- Epithelial Cells --- degranulation --- Macrophages --- Recycling endosomes --- Eosinophils
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Exostosin is a family of type II transmembrane glycosyltransferase enzymes, containing five members: EXT1, EXT2, EXTL1, EXTL2, EXTL3. These proteins are linked with heparan sulfate chains polymerization on heparan sulfate proteoglycans, but recent advances demonstrated that some of these members exhibit novel functions. Rab GTPases family is composed of at least 60 members of membrane-bound proteins that regulate many steps of membrane trafficking. The aim of this study is to analyse potential interplay between EXT and Rab family members in Notch signaling. Rab GTPases were cloned in an expression vector and transfected in human cells to observe their potential effect on NOTCH1 expression. Cell lines silenced for each EXT member were created and their characteristics assessed. EXT1 and EXT2 protein production in Yarrowia lipolytica was also considered to perform in vitro analyzes using purified proteins. As a result, a functional library of Rab GTPases in expression vector was created, verified, and is ready to be used for transfection experiments. Stable knockdown cell lines were successfully created for EXT genes, a reduction of NOTCH1 expression was observed when EXT2 or EXTL3 were silenced, probably due to modification of the trafficking mechanism and/or genetic co-regulation. Protein production did not show significant results. These results suggest a new model for increased NOTCH1 trafficking: overexpression of EXT2 and Rab10 with simultaneous silencing of EXT1. Rab GTPases were cloned in an expression vector and transfected in human cells to observe their potential effect on NOTCH1 expression. Cell lines silenced for each EXT member were created and their characteristics assessed. EXT1 and EXT2 protein production in Yarrowia lipolytica was also considered to perform in vitro analyzes using purified proteins. As a result, a functional library of Rab GTPases in expression vector was created, verified, and is ready to be used for transfection experiments. Stable knockdown cell lines were successfully created for EXT genes, a reduction of NOTCH1 expression was observed when EXT2 or EXTL3 were silenced, probably due to modification of the trafficking mechanism and/or genetic co-regulation. Protein production did not show significant results. These results suggest a new model for increased NOTCH1 trafficking: overexpression of EXT2 and Rab10 with simultaneous silencing of EXT1.
NOTCH1 --- Rab GTPases --- Exostosin --- Sciences du vivant > Biochimie, biophysique & biologie moléculaire
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Guanosine triphosphatase --- Guanosine triphosphatase. --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- Phosphatases --- Health Sciences --- Physiology --- Animal Biochemistry --- GTPases
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This detailed book expands upon the previous edition with a collection of methods for those performing experimental work on small GTPases of the Rho family. Split into four sections, the volume explores computational modeling and imaging procedures, biochemical methods related to post-translational modifications of Rho GTPases as well as some high throughput methods, functional assays that allow for monitoring the consequences of manipulating Rho GTPases in a variety of cell types and cell biology processes, and techniques specifically designed for studies in selected non-mammalian model organisms (zebrafish, social ameba, plants and algae). Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on trouble shooting and avoiding known pitfalls. Authoritative and up-to-date, Rho GTPases: Methods and Protocols, Second Edition constitutes an invaluable tool for all those with an interest in this remarkable family of signaling proteins.
Biochemistry. --- Protein Science. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Composition --- GTPases Rho --- Transducció de senyal cel·lular --- Manuals de laboratori --- Tècniques de laboratori --- Transducció de la informació cel·lular --- Regulació cel·lular --- Missatgers secundaris (Bioquímica) --- Família GTPasa Rho --- GTPases de la família Rho --- Proteïnes d'unió al GTP Rho --- Proteïnes G Rho --- Proteïnes GTP Rho --- Rho GTPases --- Rho (Enzims) --- Rho (Proteïnes)
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Pathogenic bacteria for human and animals have developed sophisticated weapons, termed virulence factors, to ensure their replication and persistence into their hosts. The first role of these virulence factors is to loosen the host defenses against microorganisms represented by innate and adaptive immunities. Small GTPases of the Rho subfamily have been shown top play important functions in theses systems. The authors of this volume present the synthesis on how the various host cellular Rho GTPases activities are manipulated by bacteria to fulfill their virulence.
Pathogenic bacteria. --- Virulence (Microbiology) --- Rho GTPases. --- Rho G proteins --- Rho GTP-binding proteins --- G proteins --- Guanosine triphosphatase --- Microbial virulence --- Pathogenic microorganisms --- Bacteria, Pathogenic --- Disease germs --- Bacteria --- Bacterial diseases --- Medical bacteriology --- Medical virology. --- Virology. --- Medical microbiology --- Virology --- Virus diseases --- Microbiology
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Guanosine triphosphatase --- Guanosine-trifosfatase --- Guanosinetriphosphatase --- Trifosfatase [Guanosine-] --- Triphosphatase [Guanosine] --- GTP Phosphohydrolases. --- GTP Phosphohydrolase --- GTPase --- GTPases --- Guanosine Triphosphate Phosphohydrolases --- Guanosinetriphosphatases --- Phosphohydrolase, GTP --- Phosphohydrolases, GTP --- Phosphohydrolases, Guanosine Triphosphate --- Triphosphate Phosphohydrolases, Guanosine --- Guanosine triphosphatase. --- Gtp phosphohydrolase --- Gtp phosphohydrolase. --- GTP Phosphohydrolases
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The Ras superfamily (>150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continua
Guanosine Triphosphate. --- Rho GTPases. --- rho GTP-Binding Proteins. --- Rho G proteins --- Rho GTP-binding proteins --- Guanosine triphosphatase. --- G proteins --- Guanosine triphosphatase --- GTP phosphohydrolase --- GTPase --- Guanosine triphosphate phosphohydrolase --- Guanosinetriphosphatase --- Phosphatases
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The critically acclaimed laboratory standard for more than 40 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today, truly an essential publication for researchers in all fields of life sciences.This volume and its companions (Volumes 255, 256, 257, and the forthcoming 325 and 329<
Guanosine triphosphatase. --- ras Proteins. --- ras Proteins --- Monomeric GTP-Binding Proteins --- GTP-Binding Proteins --- Intracellular Signaling Peptides and Proteins --- Peptides --- Carrier Proteins --- GTP Phosphohydrolases --- Proteins --- Amino Acids, Peptides, and Proteins --- Acid Anhydride Hydrolases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Ras proteins. --- G proteins. --- GTP-binding proteins --- GTP regulatory proteins --- Guanine nucleotide-binding proteins --- Guanine nucleotide regulatory proteins --- Guanosine triphosphatase --- Guanosine-trifosfatase --- Guanosinetriphosphatase --- Trifosfatase [Guanosine-] --- Triphosphatase [Guanosine] --- rho GTP-Binding Proteins --- Binding Protein --- Binding Proteins --- Transport Proteins --- Protein, Binding --- Proteins, Binding --- Proteins, Carrier --- Proteins, Transport --- G-Protein --- GTP-Binding Protein --- GTP-Regulatory Protein --- Guanine Nucleotide Coupling Protein --- G-Proteins --- GTP-Regulatory Proteins --- Guanine Nucleotide Regulatory Proteins --- G Protein --- G Proteins --- GTP Binding Protein --- GTP Binding Proteins --- GTP Regulatory Protein --- GTP Regulatory Proteins --- Protein, GTP-Binding --- Protein, GTP-Regulatory --- Proteins, GTP-Binding --- Proteins, GTP-Regulatory --- Intracellular Signaling Peptides --- Intracellular Signaling Proteins --- Peptides, Intracellular Signaling --- Proteins, Intracellular Signaling --- Signaling Peptides, Intracellular --- Signaling Proteins, Intracellular --- P21 (rho)Protein --- rho GTP-Binding Protein --- rho Protein P21 --- rho G-Proteins --- rho GTPases --- rho Small GTP-Binding Proteins --- G-Proteins, rho --- GTP-Binding Protein, rho --- GTP-Binding Proteins, rho --- GTPases, rho --- P21, rho Protein --- rho G Proteins --- rho GTP Binding Protein --- rho GTP Binding Proteins --- rho Small GTP Binding Proteins --- GTP Phosphohydrolase --- GTPase --- GTPases --- Guanosine Triphosphate Phosphohydrolases --- Guanosinetriphosphatases --- Phosphohydrolase, GTP --- Phosphohydrolases, GTP --- Phosphohydrolases, Guanosine Triphosphate --- Triphosphate Phosphohydrolases, Guanosine --- ras-Related G-Proteins --- ras-Related GTP-Binding Proteins --- G-Proteins, Monomeric --- GTP-Binding Proteins, Monomeric --- Monomeric G-Proteins --- Small G-Proteins --- Small GTPases --- ras-Related GTPases --- G Proteins, Monomeric --- G-Proteins, Small --- G-Proteins, ras-Related --- GTP Binding Proteins, Monomeric --- GTP-Binding Proteins, ras-Related --- GTPases, Small --- GTPases, ras-Related --- Monomeric G Proteins --- Monomeric GTP Binding Proteins --- Proteins, ras-Related GTP-Binding --- Small G Proteins --- ras Related G Proteins --- ras Related GTP Binding Proteins --- ras Related GTPases --- Anhydride Hydrolases, Acid --- Hydrolases, Acid Anhydride --- Biochemistry -- Periodicals. --- Biochemistry -- Technique. --- Enzymes -- Collections. --- Enzymes -- Periodicals. --- Enzymologie -- Technique -- Collections. --- GTP Phosphohydrolases. --- GTP phosphohydrolase --- Guanosine triphosphate phosphohydrolase --- GTP phosphohydrolases. --- Cytoplasmic Vesicles --- Physiological effect --- G proteins --- Membrane proteins --- Phosphatases --- Coenzymes and Enzymes --- Biocatalysts --- Molecular Mechanisms of Pharmacological Action --- Protein Binding --- Receptors, Transferrin --- Gene Products, Protein --- Gene Proteins --- Protein Gene Products --- Proteins, Gene --- Polypeptides --- Biocatalyst --- Enzyme --- Carrier Protein --- Transport Protein --- Protein, Carrier --- Protein, Transport --- Protein --- Peptide --- Polypeptide --- Hydrolase --- Small GTPase --- GTPase, Small --- rho GTPase --- GTPase, rho --- Gene expression. --- Gtp phosphohydrolases --- Map kinase signaling system --- Adp-ribosylation factors --- Gtp-binding proteins --- Gtp phosphohydrolase activators --- Gtp-binding protein regulators
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