Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.Congenital Disorders of Glycosylation: A genetically heterogeneous group of heritable disorders resulting from defects in protein N-glycosylation.Tunicamycin: An N-acetylglycosamine containing antiviral antibiotic obtained from Streptomyces lysosuperificus. It is also active against some bacteria and fungi, because it inhibits the glucosylation of proteins. Tunicamycin is used as tool in the study of microbial biosynthetic mechanisms.PolysaccharidesAsparagine: A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Oligosaccharides: Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.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.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.Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase: An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. It requires the presence of more than two amino-acid residues in the substrate for activity. This enzyme was previously listed as EC 3.2.2.18.Glycopeptides: Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Carbohydrate Metabolism, Inborn ErrorsProtein Modification, Translational: Any of the enzymatically catalyzed modifications of the individual AMINO ACIDS of PROTEINS, and enzymatic cleavage or crosslinking of peptide chains that occur pre-translationally (on the amino acid component of AMINO ACYL TRNA), co-translationally (during the process of GENETIC TRANSLATION), or after translation is completed (POST-TRANSLATIONAL PROTEIN PROCESSING).Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)Glycosyltransferases: Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4.Carbohydrate Conformation: The characteristic 3-dimensional shape of a carbohydrate.Mannosyltransferases: Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57.Glycomics: The systematic study of the structure and function of the complete set of glycans (the glycome) produced in a single organism and identification of all the genes that encode glycoproteins.N-Acetylglucosaminyltransferases: Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.GlucosamineGlycoside HydrolasesCell Line: Established cell cultures that have the potential to propagate indefinitely.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Acetylglucosamine: The N-acetyl derivative of glucosamine.Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase: A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.N-Acetylneuraminic Acid: An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)Swainsonine: An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.FucoseMutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.N-Acetylgalactosaminyltransferases: Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Dolichol: Eicosamethyl octacontanonadecasen-1-o1. Polyprenol found in animal tissues that contains about 20 isoprene residues, the one carrying the alcohol group being saturated.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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)Phosphotransferases (Phosphomutases): A group of enzymes that catalyze an intramolecular transfer of a phosphate group. It has been shown in some cases that the enzyme has a functional phosphate group, which can act as the donor. These were previously listed under PHOSPHOTRANSFERASES (EC 2.7.-). (From Enzyme Nomenclature, 1992) EC 5.4.2.Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Dystroglycans: Dystrophin-associated proteins that play role in the formation of a transmembrane link between laminin-2 and DYSTROPHIN. Both the alpha and the beta subtypes of dystroglycan originate via POST-TRANSLATIONAL PROTEIN PROCESSING of a single precursor protein.Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization: A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.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)Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Dolichol Phosphates: Phosphoric acid esters of dolichol.Glycosides: Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)Galactosyltransferases: Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Acetylgalactosamine: The N-acetyl derivative of galactosamine.IndolizinesMolecular Weight: The sum of the weight of all the atoms in a molecule.1-Deoxynojirimycin: An alpha-glucosidase inhibitor with antiviral action. Derivatives of deoxynojirimycin may have anti-HIV activity.Guanosine Diphosphate Mannose: A nucleoside diphosphate sugar which can be converted to the deoxy sugar GDPfucose, which provides fucose for lipopolysaccharides of bacterial cell walls. Also acts as mannose donor for glycolipid synthesis.Monosaccharides: Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Viral Envelope Proteins: Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.Membrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Mucins: High molecular weight mucoproteins that protect the surface of EPITHELIAL CELLS by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Carbohydrate Metabolism: Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.Sialic Acids: A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Glycosylation End Products, Advanced: Products derived from the nonenzymatic reaction of GLUCOSE and PROTEINS in vivo that exhibit a yellow-brown pigmentation and an ability to participate in protein-protein cross-linking. These substances are involved in biological processes relating to protein turnover and it is believed that their excessive accumulation contributes to the chronic complications of DIABETES MELLITUS.Oligosaccharides, Branched-Chain: Oligosaccharides containing various types of glycosidic linkages that yield branching or antennae. The number of antennae (such as bi-, tri-, tetra-, or penta-antennary) in the oligosaccharides on the PROTEOGLYCANS; GLYCOPROTEINS; or LIPOPOLYSACCHARIDES contribute to their biological activities, such as receptor binding and metabolism.Hexosyltransferases: Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.Uridine Diphosphate N-Acetylgalactosamine: A nucleoside diphosphate sugar which serves as a source of N-acetylgalactosamine for glycoproteins, sulfatides and cerebrosides.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Sialyltransferases: A group of enzymes with the general formula CMP-N-acetylneuraminate:acceptor N-acetylneuraminyl transferase. They catalyze the transfer of N-acetylneuraminic acid from CMP-N-acetylneuraminic acid to an acceptor, which is usually the terminal sugar residue of an oligosaccharide, a glycoprotein, or a glycolipid. EC 2.4.99.-.Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Galactose: An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.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.Uridine Diphosphate N-Acetylglucosamine: Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.Kinetics: The rate dynamics in chemical or physical systems.Cricetulus: A genus of the family Muridae consisting of eleven species. C. migratorius, the grey or Armenian hamster, and C. griseus, the Chinese hamster, are the two species used in biomedical research.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.beta-Fructofuranosidase: A glycoside hydrolase found primarily in PLANTS and YEASTS. It has specificity for beta-D-fructofuranosides such as SUCROSE.Glucosyltransferases: Enzymes that catalyze the transfer of glucose from a nucleoside diphosphate glucose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.HexosaminesProtein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Pichia: Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.Amino Sugars: SUGARS containing an amino group. GLYCOSYLATION of other compounds with these amino sugars results in AMINOGLYCOSIDES.Acetylglucosaminidase: A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Dolichol Monophosphate Mannose: A lipophilic glycosyl carrier of the monosaccharide mannose in the biosynthesis of oligosaccharide phospholipids and glycoproteins.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.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.Mannose-6-Phosphate Isomerase: An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC 5.3.1.8.Glycoconjugates: Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Protein PrecursorsCOS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Hemagglutinin Glycoproteins, Influenza Virus: Membrane glycoproteins from influenza viruses which are involved in hemagglutination, virus attachment, and envelope fusion. Fourteen distinct subtypes of HA glycoproteins and nine of NA glycoproteins have been identified from INFLUENZA A VIRUS; no subtypes have been identified for Influenza B or Influenza C viruses.Gastric Mucins: Mucins that are found on the surface of the gastric epithelium. They play a role in protecting the epithelial layer from mechanical and chemical damage.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Fucosyltransferases: Enzymes catalyzing the transfer of fucose from a nucleoside diphosphate fucose to an acceptor molecule which is frequently another carbohydrate, a glycoprotein, or a glycolipid molecule. Elevated activity of some fucosyltransferases in human serum may serve as an indicator of malignancy. The class includes EC 2.4.1.65; EC 2.4.1.68; EC 2.4.1.69; EC 2.4.1.89.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Uridine Diphosphate Galactose: A nucleoside diphosphate sugar which can be epimerized into UDPglucose for entry into the mainstream of carbohydrate metabolism. Serves as a source of galactose in the synthesis of lipopolysaccharides, cerebrosides, and lactose.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Campylobacter jejuni: A species of bacteria that resemble small tightly coiled spirals. Its organisms are known to cause abortion in sheep and fever and enteritis in man and may be associated with enteric diseases of calves, lambs, and other animals.Walker-Warburg Syndrome: Rare autosomal recessive lissencephaly type 2 associated with congenital MUSCULAR DYSTROPHY and eye anomalies (e.g., RETINAL DETACHMENT; CATARACT; MICROPHTHALMOS). It is often associated with additional brain malformations such as HYDROCEPHALY and cerebellar hypoplasia and is the most severe form of the group of related syndromes (alpha-dystroglycanopathies) with common congenital abnormalities in the brain, eye and muscle development.Epitopes: Sites on an antigen that interact with specific antibodies.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Uridine Diphosphate Glucose: A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Polyisoprenyl Phosphate Oligosaccharides: These compounds function as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. Include the pyrophosphates.HIV Envelope Protein gp120: External envelope protein of the human immunodeficiency virus which is encoded by the HIV env gene. It has a molecular weight of 120 kDa and contains numerous glycosylation sites. Gp120 binds to cells expressing CD4 cell-surface antigens, most notably T4-lymphocytes and monocytes/macrophages. Gp120 has been shown to interfere with the normal function of CD4 and is at least partly responsible for the cytopathic effect of HIV.Polyisoprenyl Phosphate Monosaccharides: These compounds function as activated monosaccharide carriers in the biosynthesis of glycoproteins and oligosaccharide phospholipids. Obtained from a nucleoside diphosphate sugar and a polyisoprenyl phosphate.Mucin-1: Carbohydrate antigen elevated in patients with tumors of the breast, ovary, lung, and prostate as well as other disorders. The mucin is expressed normally by most glandular epithelia but shows particularly increased expression in the breast at lactation and in malignancy. It is thus an established serum marker for breast cancer.Viral Proteins: Proteins found in any species of virus.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Spectrometry, Mass, Electrospray Ionization: A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Polyisoprenyl Phosphate Sugars: Compounds functioning as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. They include the polyisoprenyl pyrophosphates.Trisaccharides: Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Concanavalin A: A MANNOSE/GLUCOSE binding lectin isolated from the jack bean (Canavalia ensiformis). It is a potent mitogen used to stimulate cell proliferation in lymphocytes, primarily T-lymphocyte, cultures.Microsomes: Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Mannosidases: Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.AmidohydrolasesBiological 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.Biotinylation: Incorporation of biotinyl groups into molecules.Deoxy SugarsCercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.Flagellin: A protein with a molecular weight of 40,000 isolated from bacterial flagella. At appropriate pH and salt concentration, three flagellin monomers can spontaneously reaggregate to form structures which appear identical to intact flagella.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.

The Saccharomyces cerevisiae CWH8 gene is required for full levels of dolichol-linked oligosaccharides in the endoplasmic reticulum and for efficient N-glycosylation. (1/9988)

The Saccharomyces cerevisiae mutant cwh8 was previously found to have an anomalous cell wall. Here we show that the cwh8 mutant has an N -glycosylation defect. We found that cwh8 cells were resistant to vanadate and sensitive to hygromycin B, and produced glycoforms of invertase and carboxypeptidase Y with a reduced number of N -chains. We have cloned the CWH8 gene. We found that it was nonessential and encoded a putative transmembrane protein of 239 amino acids. Comparison of the in vitro oligosaccharyl transferase activities of membrane preparations from wild type or cwh8 Delta cells revealed no differences in enzyme kinetic properties indicating that the oligosaccharyl transferase complex of mutant cells was not affected. cwh8 Delta cells also produced normal dolichols and dolichol-linked oligosaccharide intermediates including the full-length form Glc3Man9GlcNAc2. The level of dolichol-linked oligosaccharides in cwh8 Delta cells was, however, reduced to about 20% of the wild type. We propose that inefficient N -glycosylation of secretory proteins in cwh8 Delta cells is caused by an insufficient supply of dolichol-linked oligosaccharide substrate.  (+info)

Salivary mucin MG1 is comprised almost entirely of different glycosylated forms of the MUC5B gene product. (2/9988)

The MG1 population of mucins was isolated from human whole salivas by gel chromatography followed by isopycnic density gradient centrifugation. The reduced and alkylated MG1 mucins, separated by anion exchange chromatography, were of similar size (radius of gyration 55-64 nm) and molecular weight (2.5-2.9 x 10(6) Da). Two differently-charged populations of MG1 subunits were observed which showed different reactivity with monoclonal antibodies to glycan epitopes. Monosaccharide and amino acid compositional analyses indicated that the MG1 subunits had similar glycan structures on the same polypeptide. An antiserum recognizing the MUC5B mucin was reactive across the entire distribution, whereas antisera raised against the MUC2 and MUC5AC mucins showed no reactivity. Western blots of agarose gel electrophoresis of fractions across the anion exchange distribution indicated that the polypeptide underlying the mucins was the product of the MUC5B gene. Amino acid analysis and peptide mapping performed on the fragments produced by trypsin digestion of the two MG1 populations yielded data similar to that obtained for MUC5B mucin subunits prepared from respiratory mucus (Thornton et al., 1997) and confirmed that the MUC5B gene product was the predominant mucin polypeptide present. Isolation of the MG1 mucins from the secretions of the individual salivary glands (palatal, sublingual, and submandibular) indicate that the palatal gland is the source of the highly charged population of the MUC5B mucin.  (+info)

The sialylation of bronchial mucins secreted by patients suffering from cystic fibrosis or from chronic bronchitis is related to the severity of airway infection. (3/9988)

Bronchial mucins were purified from the sputum of 14 patients suffering from cystic fibrosis and 24 patients suffering from chronic bronchitis, using two CsBr density-gradient centrifugations. The presence of DNA in each secretion was used as an index to estimate the severity of infection and allowed to subdivide the mucins into four groups corresponding to infected or noninfected patients with cystic fibrosis, and to infected or noninfected patients with chronic bronchitis. All infected patients suffering from cystic fibrosis were colonized by Pseudomonas aeruginosa. As already observed, the mucins from the patients with cystic fibrosis had a higher sulfate content than the mucins from the patients with chronic bronchitis. However, there was a striking increase in the sialic acid content of the mucins secreted by severely infected patients as compared to noninfected patients. Thirty-six bronchial mucins out of 38 contained the sialyl-Lewis x epitope which was even expressed by subjects phenotyped as Lewis negative, indicating that at least one alpha1,3 fucosyltransferase different from the Lewis enzyme was involved in the biosynthesis of this epitope. Finally, the sialyl-Lewis x determinant was also overexpressed in the mucins from severely infected patients. Altogether these differences in the glycosylation process of mucins from infected and noninfected patients suggest that bacterial infection influences the expression of sialyltransferases and alpha1,3 fucosyltransferases in the human bronchial mucosa.  (+info)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (4/9988)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

Possible role for ligand binding of histidine 81 in the second transmembrane domain of the rat prostaglandin F2alpha receptor. (5/9988)

For the five principal prostanoids PGD2, PGE2, PGF2alpha, prostacyclin and thromboxane A2 eight receptors have been identified that belong to the family of G-protein-coupled receptors. They display an overall homology of merely 30%. However, single amino acids in the transmembrane domains such as an Arg in the seventh transmembrane domain are highly conserved. This Arg has been identified as part of the ligand binding pocket. It interacts with the carboxyl group of the prostanoid. The aim of the current study was to analyze the potential role in ligand binding of His-81 in the second transmembrane domain of the rat PGF2alpha receptor, which is conserved among all PGF2alpha receptors from different species. Molecular modeling suggested that this residue is located in close proximity to the ligand binding pocket Arg 291 in the 7th transmembrane domain. The His81 (H) was exchanged by site-directed mutagenesis to Gln (Q), Asp (D), Arg (R), Ala (A) and Gly (G). The receptor molecules were N-terminally extended by a Flag epitope for immunological detection. All mutant proteins were expressed at levels between 50% and 80% of the wild type construct. The H81Q and H81D receptor bound PGF2alpha with 2-fold and 25-fold lower affinity, respectively, than the wild type receptor. Membranes of cells expressing the H81R, H81A or H81G mutants did not bind significant amounts of PGF2alpha. Wild type receptor and H81Q showed a shallow pH optimum for PGF2alpha binding around pH 5.5 with almost no reduction of binding at higher pH. In contrast the H81D mutant bound PGF2alpha with a sharp optimum at pH 4.5, a pH at which the Asp side chain is partially undissociated and may serve as a hydrogen bond donor as do His and Gln at higher pH values. The data indicate that the His-81 in the second transmembrane domain of the PGF2alpha receptor in concert with Arg-291 in the seventh transmembrane domain may be involved in ligand binding, most likely not by ionic interaction with the prostaglandin's carboxyl group but rather as a hydrogen bond donor.  (+info)

N-Linked glycosylation and sialylation of the acid-labile subunit. Role in complex formation with insulin-like growth factor (IGF)-binding protein-3 and the IGFs. (6/9988)

Over 75% of the circulating insulin-like growth factors (IGF-I and -II) are bound in 140-kDa ternary complexes with IGF-binding protein-3 (IGFBP-3) and the 84-86-kDa acid-labile subunit (ALS), a glycoprotein containing 20 kDa of carbohydrate. The ternary complexes regulate IGF availability to the tissues. Since interactions of glycoproteins can be influenced by their glycan moieties, this study aimed to determine the role of ALS glycosylation in ternary complex formation. Complete deglycosylation abolished the ability of ALS to associate with IGFBP-3. To examine this further, seven recombinant ALS mutants each lacking one of the seven glycan attachment sites were expressed in CHO cells. All the mutants bound IGFBP-3, demonstrating that this interaction is not dependent on any single glycan chain. Enzymatic desialylation of ALS caused a shift in isoelectric point from 4.5 toward 7, demonstrating a substantial contribution of anionic charge by sialic acid. Ionic interactions are known to be involved in the association between ALS and IGFBP-3. Desialylation reduced the affinity of ALS for IGFBP-3. IGF complexes by 50-80%. Since serum protein glycosylation is often modified in disease states, the dependence of IGF ternary complex formation on the glycosylation state of ALS suggests a novel mechanism for regulation of IGF bioavailability.  (+info)

Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells. (7/9988)

The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the interactions involved in the binding of MAG to neuronal axons, we performed this study to identify the binding partners for MAG on neuronal cells. Experiments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastoma cell line N2A. From extracts of [3H]glucosamine-labelled N2A cells several glycoproteins with molecular weights between 20 and 230 kDa were affinity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG.  (+info)

The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex. (8/9988)

In the yeast Saccharomyces cerevisiae many of the N-linked glycans on cell wall and periplasmic proteins are modified by the addition of mannan, a large mannose-containing polysaccharide. Mannan comprises a backbone of approximately 50 alpha-1,6-linked mannoses to which are attached many branches consisting of alpha-1,2-linked and alpha-1,3-linked mannoses. The initiation and subsequent elongation of the mannan backbone is performed by two complexes of proteins in the cis Golgi. In this study we show that the product of the MNN10/BED1 gene is a component of one of these complexes, that which elongates the backbone. Analysis of interactions between the proteins in this complex shows that Mnn10p, and four previously characterized proteins (Anp1p, Mnn9p, Mnn11p, and Hoc1p) are indeed all components of the same large structure. Deletion of either Mnn10p, or its homologue Mnn11p, results in defects in mannan synthesis in vivo, and analysis of the enzymatic activity of the complexes isolated from mutant strains suggests that Mnn10p and Mnn11p are responsible for the majority of the alpha-1, 6-polymerizing activity of the complex.  (+info)

Abstract. Many West Nile (WN) virus isolates associated with significant outbreaks possess a glycosylation site on the envelope (E) protein. E-protein glycosylated variants of New York (NY) strains of WN virus are more neuroinvasive in mice than the non-glycosylated variants. To determine how E protein glycosylation affects the interactions between WN virus and avian hosts, we inoculated young chicks with NY strains of WN virus containing either glycosylated or non-glycosylated variants of the E protein. The glycosylated variants were more virulent and had higher viremic levels than the non-glycosylated variants. The glycosylation status of the variant did not affect viral multiplication and dissemination in mosquitoes in vivo. Glycosylated variants showed more heat-stable propagation than non-glycosylated variants in mammalian (BHK) and avian (QT6) cells but not in mosquito (C6/36) cells. Thus, E-protein glycosylation may be a requirement for efficient transmission of WN virus from avian hosts to
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Centralized Modularity of N-Linked Glycosylation Pathways in Mammalian Cells. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
N-linked glycosylation has a profound effect on the proper folding, oligomerization and stability of glycoproteins. These glycans impart many properties to proteins that may be important for their proper functioning, besides having a tendency to exert a chaperone-like effect on them. Certain glycosylation sites in a protein however, are more important than other sites for their function and stability. It has been observed that some N-glycosylation sites are conserved over families of glycoproteins over evolution, one such being the tyrosinase related protein family. The role of these conserved N-glycosylation sites in their trafficking, sorting, stability and activity has been examined here. By scrutinizing the different glycosylation sites on this family of glycoproteins it was inferred that different sites in the same family of polypeptides can perform distinct functions and conserved sites across the paralogues may perform diverse functions.. ...
A majority of all biologically active proteins are glycosylated and various diseases have proven to correlate with alterations in protein glycosylation. Sensitive identification of different glycoprotein glycoforms is therefore of great diagnostic value. Here we describe a method with potential for glycoprotein profiling, based on lectins as capture probes immobilized on particulate substrates in the nm-range. The nanoparticles present high concentrations of attachment sites for specific ligands and cause minimal steric hindrance to binding. In the present model study the mannose-binding lectin ConA has been coupled to polystyrene nanoparticles via a poly(ethyleneoxide) linker which protects the protein conformation and activity and prevents unspecific protein adsorption. The ConA-coated particles are accommodated at different spots on the analytical surface via oligonucleotide linkage. This attachment, which relies on the hybridization of complementary oligonucleotides, allows firm fixation of ...
HIV-1 envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs) and the focus for design of an antibody-based HIV vaccine. The Env trimer is covered by ∼90N-linked glycans, which shield the underlying protein from immune surveillance. bNAbs to HIV develop during infection, with many showing dependence on glycans for binding to Env. The ability to routinely assess the glycan type at each glycosylation site may facilitate design of improved vaccine candidates. Here we present a general mass spectrometry-based proteomics strategy that uses specific endoglycosidases to introduce mass signatures that distinguish peptide glycosites that are unoccupied or occupied by high-mannose/hybrid or complex-type glycans. The method yields ,95% sequence coverage for Env, provides semi-quantitative analysis of the glycosylation status at each glycosite. We find that most glycosites in recombinant Env trimers are fully occupied by glycans, varying in the proportion of ...
Glycosylation, or the attachment of glycans (sugars) to proteins, is the most abundant post-translational modification in nature and plays a pivotal role in protein folding and activity. Glycans are involved in almost every human disease and biological process. Glycosylation is also important in biotechnology; about 70% of protein therapeutics approved or in development are glycosylated. By merging bottom-up engineering design principles with innovative molecular biology methodologies in a cell-free environment, we seek to create a simplified framework for studying and engineering glycosylation. Our envisioned platform will broaden the glycoengineering toolkit, facilitate discovery of the structural and functional consequences of glycan attachment, and enable a new era of applications in glycoprotein therapeutics and conjugate vaccines.. ...
Flavocytochrome b558 of the NADPH oxidase which generates superoxide in phagocytic cells, is a α1β1 heterodimer of gp91phox and p22phox, which together form a membrane-spanning electron-transport chain that transfers electrons from NADPH in the cytosol to oxygen. The C-terminal portion of gp91phox is a member of the ferredoxin-NADP+ reductase family of reductases. Little is known of the organization of the N-terminal section of this molecule, which is associated with the two haem structures. It is N-glycosylated, and site-directed mutagenesis has been used to eliminate the five potential N-linked glycosylation consensus sites. Mutated cDNAs were expressed in vitro. This approach provided evidence for glycosylation of residues Asn131, Asn148 and Asn239, but not of Asn96 and Asn429.. ...
Site-directed mutagenesis has been used to remove 15 of the 18 potential N-linked glycosylation sites, in 16 combinations, from the human exon 11-minus receptor isoform. The three glycosylation sites not mutated were asparagine residues 25, 397 and 894, which are known to be important in receptor biosynthesis or function. The effects of these mutations on proreceptor processing into α and β subunits, cell-surface expression, insulin binding and receptor autophosphorylation were assessed in Chinese hamster ovary cells. The double mutants 16+78, 16+111, 16+215, 16+255, 337+418, the triple mutants 295+337+418, 295+418+514, 337+418+514 and 730+743+881 and the quadruple mutants 606+730+743+881 and 671+730+743+881 seemed normal by all criteria examined. The triple mutant 16+215+255 showed only low levels of correctly processed receptor on the cell surface, this processed receptor being autophosphorylated in response to insulin. The quadruple mutant 624+730+743+881 showed normal processing and ligand ...
Kathrin Stavenhagen: Glycopeptide analysis remains challenging because of its sample heterogeneity resulting from the degree of glycosylation site occupancy (macroheterogeneity) and the different glycoforms attached to individual glycosylation sites (microheterogeneity).. With respect to the latter one, qualitative site-specific glycosylation information of glycoproteins can be obtained by unspecific protease treatment resulting in small amino acid stretches carrying the glycan. This improves determination of the glycosylation sites. However, detecting these glycopeptides by 1D-LC-ESI-MS/MS is challenging due to insufficient or irreversible retention on the stationary phase and thus multiple analyses with different LC-setups are required. Since biological sample amounts are usually limited, methods for acquiring comprehensive information in a single run are necessary.. To obtain qualitative information of the glycosylation site we set up an integrated C18-porous graphitized carbon ...
Abnormal glycosylation is a hallmark of many cancers that contributes to tumor growth and invasion. There are many protein receptors that are regulated abnormally in cancer due to mutations and/or alterations in glycosylation. Studies to link specific glycosylation changes to signaling outcomes have primarily focused on studies of individual receptors or specific pathways.
The structure of N-linked glycosylation is a very important quality attribute for therapeutic monoclonal antibodies. Different carbon sources in cell culture media, such as mannose and galactose, have been reported to have different influences on the glycosylation patterns. Accurate prediction and control of the glycosylation profile are important for the process development of mammalian cell cultures. In this study, a mathematical model, that we named Glycan Residues Balance Analysis (GReBA), was developed based on the concept of Elementary Flux Mode (EFM), and used to predict the glycosylation profile for steady state cell cultures. Experiments were carried out in pseudo-perfusion cultivation of antibody producing Chinese Hamster Ovary (CHO) cells with various concentrations and combinations of glucose, mannose and galactose. Cultivation of CHO cells with mannose or the combinations of mannose and galactose resulted in decreased lactate and ammonium production, and more matured glycosylation ...
Following the footsteps of genomics and proteomics, recent years have witnessed the growth of large-scale experimental methods in the field of glycomics. In parallel, there has also been growing interest in developing Systems Biology based methods to study the glycome. The combined goals of these endeavors is to identify glycosylation-dependent mechanisms regulating human physiology, check points that can control the progression of pathophysiology, and modifications to reaction pathways that can result in more uniform biopharmaceutical processes. In these efforts, mathematical models of N- and O-linked glycosylation have emerged as paradigms for the field. While these are relatively few in number, nevertheless, the existing models provide a basic framework that can be used to develop more sophisticated analysis strategies for glycosylation in the future. The current review surveys these computational models with focus on the underlying mathematics and assumptions, and with respect to their ...
Two urea transporters, UT-A1 and UT-A3, are expressed in the kidney terminal inner medullary collecting duct (IMCD) and are important for the production of concentrated urine. UT-A1, as the largest isoform of all UT-A urea transporters, has gained much attention and been extensively studied; however, the role and the regulation of UT-A3 are less explored. In this study, we investigated UT-A3 regulation by glycosylation modification. A site-directed mutagenesis verified a single glycosylation site in UT-A3 at Asn279. Loss of the glycosylation reduced forskolin-stimulated UT-A3 cell membrane expression and urea transport activity. UT-A3 has two glycosylation forms, 45 and 65 kDa. Using sugar-specific binding lectins, the UT-A3 glycosylation profile was examined. The 45-kDa form was pulled down by lectin concanavalin A (Con A) and Galant husnivalis lectin (GNL), indicating an immature glycan with a high amount of mannose (Man), whereas the 65-kDa form is a mature glycan composed of ...
patterns, provoking an immune response when treating humans with GPs produced in plants. State of the art approaches are based either on glycosylation mutants or overproduction of the desired protein product (intending to override the cellular glycosylation machinery). Though the mutants either show impaired yield or loss of vitality in comparison to wild type, or the proteins do not terminate in mannose residues, which is essential for the biological uptake via mannose receptors in patients with lysosomal storage diseases. This invention provides a new device to generate GPs with hypo-allergenic properties in a cost-effective way: In contrast to current methods, the new technique enables effective production of heterologous GPs by vital plants without impairments. The technology is based on a genetic modification of the N-glycosylation pathway. It is applicable to Solanaceous and other plants of agronomical interest as transgenic producers of GPs. The suppression of a specific enzyme leads to a ...
Increased understanding of the role of protein- and lipid-linked carbohydrates in a wide range of biological processes has led to interest in drugs that target the enzymes involved in glycosylation. But given the importance of carbohydrates in fundamental cellular processes such as protein folding, therapeutic strategies that modulate, rather than ablate, the activity of enzymes involved in glycosylation are likely to be a necessity. Two such approaches that use imino sugars to affect glycosylation enzymes now show considerable promise in the treatment of viral infections, such as hepatitis B, and glucosphingolipid storage disorders, such as Gaucher disease.
A variety of sulfo-protected monosaccharide donors and acceptors were investigated in glycosylation reactions. Trifluoroethylsulfonate (SO3TFE) group was compatible with a wide range of activation conditions commonly used with fluoride, imidate, and sulfide donors. In addition, the influence of a SO3TFE group, at the critical 2-position in glycosyl donor, on the stereoselectivity of the glycosylation reaction was studied ...
A chemical gycosylation reaction involves the coupling of a glycosyl donor, to a glycosyl acceptor forming a glycoside. If both the donor and acceptor are sugars, then the product is an oligosaccharide. The reaction requires activation with a suitable activating reagent. The reactions often result in a mixture of products due to the creation of a new stereogenic centre at the anomeric position of the glycosyl donor. The formation of a glycosidic linkage allows for the synthesis of complex polysaccharides which may play important roles in biological processes and pathogenesis and therefore having synthetic analogs of these molecules allows for further studies with respect to their biological importance. The glycosylation reaction involves the coupling of a glycosyl donor and a glycosyl acceptor via initiation using an activator under suitable reaction conditions. A glycosyl donor is a sugar with a suitable leaving group at the anomeric position. This group, under the reaction conditions, is ...
There are multiple factors that drive glycosylation and several currently available approaches to influence glycosylation patterns. Notable factors that influence glycosylation include the following: cell culture process conditions, ingredients in cell culture, genetic selection or engineering, and directly impacting the physiological organelles responsible for glycosylation (endoplasmic reticulum - the ER - and Golgi apparatus). In cell line development there are opportunities to use genetic engineering tools to manipulate the glycosylation pathway. In upstream development, cell culture process conditions (ie. temperature and pH) can be manipulated. Lastly, commercially available constituents in the glycan process, such as precursors and enzymes, can be added to cell culture media to further hone glycoprofiles. However, there have been limited available approaches to improve the functionality of the ER and Golgi.. One relatively unexplored lever to improve ER and Golgi functionality, and thus ...
Dr Fahey (Saldova)s main area of expertise is Glycobiology. She focuses on development and utilisation of technologies for glycan analyses, including automated high-throughput glycan analysis as well as detailed glycan characterization.. She also focuses on the role of system biology in regulation of glycosylation in health and disease (disorders of glycosylation, cancer and chronic inflammatory diseases). She has been looking at "Epigenetic regulation of glycosylation and the impact on chemoresistance in cancer" (SFI-SIRG) which follows on from novel published findings demonstrating that changes in DNA methylation in ovarian cancer cells are concomitant with significant alterations in the expression of key enzymes that form part of glycosylation. Epigenetic alterations, tumour hypoxia and glycosylation are integral aspects of carcinogenesis. Determining the mechanism of epigenetic regulation of glycosylation and the link with hypoxia and drug resistance will help to improve the treatment of ...
Protein glycosylation, an important PTM, plays an essential role in a wide range of biological processes such as immune response, intercellular signaling, inflammation, and host-pathogen interaction. Aberrant glycosylation has been correlated with various diseases. However, studying protein glycosylation remains challenging because of low abundance, microheterogeneities of glycosylation sites, and ...
Direct mass spectrometric analysis of aberrant protein glycosylation is a challenge to the current analytical techniques. Except lectin affinity chromatography, no other glycosylation enrichment techniques are available for analysis of aberrant glycosylation. In this study, we developed a combined chemical and enzymatic strategy as an alternative for the mass spectrometric analysis of aberrant glycosylation. Sialylated glycopeptides were enriched with reverse glycoblotting, cleaved by endoglycosidase F3 and analyzed by mass spectrometry with both neutral loss triggered MS3 in collision induced dissociation (CID) and electron transfer dissociation (ETD). Interestingly, a great part of resulted glycopeptides were found with fucose attached to the N-acetylglucosamine (N-GlcNAc), which indicated that the aberrant glycosylaton that is carrying both terminal sialylation and core fucosylation was identified. Totally, 69 aberrant N-glycosylation sites were identified in sera samples from hepatocellular ...
The most abundant modification of proteins in eukaryotes is N-linked glycosylation:more than 10000 different acceptor sites are N-glycosylated in the mouse proteome. The process is essential because it underpins the folding and quality control of non-cytoplasmic (organelle-targeted), membrane-embedded, or secreted proteins. N-glycosylation is involved in organism development, the immune response, and host-pathogen interactions. Finally, a multitude of diseases are linked to the dysfunction of this process, including the various congenital disorders of glycosylation (CDGs).This proposal focuses on the central enzyme in the N-glycosylation pathway, oligosaccharyltransferase (OST). OST is a complex molecular machine that is embedded in the membrane of the Endoplasmic Reticulum (ER), where it catalyzes the transfer of a glycan moiety from a lipid-linked oligosaccharide (LLO) onto acceptor proteins that contain a recognition sequence N-X-S/T (the glycosylation sequon). After its covalent attachment ...
To-date, no claim regarding finding a consensus sequon for O-glycosylation has been made. Thus, predicting the likelihood of O-glycosylation with sequence and structural information using classical regression analysis is quite difficult. In particular, if a binary response is used to distinguish between O-glycosylated and non-O-glycosylated sequences, an appropriate set of non-O-glycosylatable sequences is hard to find. Three sequences from similar post-translational modifications (PTMs) of proteins occurring at, or very near, the S/T-site are analyzed: N-glycosylation, O-mucin type (O-GalNAc) glycosylation, and phosphorylation. Results found include: 1) The consensus composite sequon for O-glycosylation is: ~(W-S/T-W), where
AGA of pentasaccharide 5 utilized three different glycosylation modules (A1, B1 and B1*, see Scheme 1 and ESI†). Each module uses three times three equivalents of glycosylating agent followed by an activator wash step with TMSOTf solution added at −30 °C, and the resin is agitated for 1 min before removal of the activator. Glycosylation module A1 activates three equivalents of glycosyl phosphate building block 1 with stoichiometric amounts of TMSOTf at −30 °C. After maintaining −30 °C for 10 min, the temperature is raised to −15 °C and maintained for 25 min. Glycosylation module B1 activates three equivalents of glycosyl phosphate building block 2 at −30 °C and allows 10 min for glycosylation, but raises the temperature to −10 °C and maintains it for 25 min to account for the lower reactivity of 2 caused by the presence of the Lev group. Glycosylation module B1* uses B1 reaction conditions for building block 1 since the C3-hydroxyl of 2 is expected to be a weaker nucleophile ...
Experts say glycosylation analysis is the most important and least precise area of chemical analysis. Moreover, there is no magic bullet for analyzing glycosylation in monoclonal antibodies. The methods for identifying the chemical structures are not well developed at this time. Even two results from the same lab using the same method on the same sample can vary.
Mannose is a succar monomer o the aldohexose series o carbohydrates. Mannose is a C-2 epimer o glucose. Mannose is important in human metabolism, especially in the glycosylation o certain proteins. Several congenital disorders o glycosylation are associated wi mutations in enzymes involved in mannose metabolism.[1]. ...
Profiling of glycosylation gene expression in CHO fed-batch cultures in response to glycosylation-enhancing medium components. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
DUGi: Viewing Item from repository Recercat: Glycoconjugates constitute a major class of biomolecules which include glycoproteins, glycosphingolipidsand proteoglycans. The enzymatic process in which glycans (sugar chains) are linked toproteins or lipids is called glycosylation. Glycosylation is involved in many biological processes, bothphysiological and pathological, inlcuding host-pathogen interactions, tumour invasion, cell traffickingand signalling. Changes in glycan structure are thought be be at least partly responsible for the developmentof inflammation, infection, arteriosclerosis, immune defects and autoimmunity. Such changeshave been observed in human diseases such as diabetes mellitus, rheumatoid arthritis and AlzheimersDisease. Aberrant patterns of glycosylation are also a universal feature of cancer cells. The field ofglycobiology thus shows great potential for the discovery of glycan biomarkers for disease diagnosisand prognosis.Here we focus specifically on N-glycans, that is, glycans
Glycosylation is a post-translational modification (PTM) that exerts profound structural and functional effects on the modified protein. Glycan synthesis and conjugation to proteins are regulated by a myriad of factors, both genetic and environmental, and are also influenced by external stressors. Glycosylation patterns are known to vary in correlation to a large number of diseases; therefore, it is possible to study such alterations to identify reliable biomarkers and help elucidate mechanisms underlying the disease. For these reasons, the development of analytical methods able to investigate the glycosylation of proteins in complex samples and to measure and characterize disease-related alterations is of great importance.. In this thesis, the development and application of rapid and small-scale methods for the analysis of the glycosylation pattern on specific proteins in biological fluids, with a high degree of automation and potential for parallel sample treatment, is presented.. Paper I ...
In past years, several strategies have been evaluated in our laboratory to express rFel d 1, starting with separate expression of both chains of the molecule in P. pastoris (unpublished data), and subsequently, expression of both chains coupled by a linker sequence (this study). In our hands, this approach resulted in a rFel d 1 preparation with good immune reactivity but an undesirable degree of molecular heterogeneity caused by hyperglycosylation of a fraction of the molecules at the N-linked glycosylation site in the β-chain of Fel d 1. Additionally, some instability of the linker sequence resulted in partial cleavage of the two-chain heterodimer (confirmed by N-terminal sequencing of the resulting fragments). Both post-translational modifications did not significantly affect immune reactivity but the observed heterogeneity is less favorable from a production standpoint. A mutant lacking the N-linked glycosylation site showed decreased heterogeneity, but was still partially cleaved (not ...
Acetylation and glycosylation are widespread posttranslational modifications (PTMs) involved in diverse cellular processes and can affect the structure of proteins. We have demonstrated that proteins can misfold and form amyloid structures upon inhibition of histone deacetylases (HDACs) in clinically relevant concentrations. Acetylation plays a role in the aetiology of ageing-related proteinopathies such as in Alzheimers disease, Parkinsons disease or Huntingtons disease. Furthermore, aggregate formation is fostered by mis-glycosylation of proteins; for instance, mutations in one key enzyme of terminal glycosylation (sialylation) are responsible for the age-dependent GNE (bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetyl-mannosamine kinase) myopathy. We aim to investigate how acetylation and glycosylation influence protein folding and misfolding, in particular proteins involved in ageing-related diseases. We also analyse, how protein shuttling factors can ameliorate protein misfolding ...
Characterization of post-translational modifications (PTMs) of therapeutic proteins is very important during the bioprocess development to maintain desired product quality and during the submission process to regulatory authorities for product approval. Monitoring glycosylation in pharmacokinetic studies can be useful to evaluate the dependence of clearance rates on different glycoforms. The cost and efficiency of characterization affect the speed to market of biopharmaceutical proteins. A reduction in the number of manual processing steps, cost of reagents and consumption of sample, as well as the time required for chemical analysis, is therefore necessary.. The research presented in this thesis is focused on the potential of using microfluidic discs for automated, miniaturized, parallel and rapid sample preparation for PTM characterization of therapeutic monoclonal antibodies. Paper I describes the method development for N-linked glycosylation profiling. Several sample preparation steps have ...
Malignant transformation of cells is associated with aberrant glycosylation presented on the cell-surface. Commonly observed changes in glycan structures during malignancy encompasses aberrant expression and glycosylation of mucins; abnormal branching of N-glycans; and increased presence of sialic acid on proteins and glycolipids. Accumulating evidence supports the notion that the presence of certain glycan structures correlates with cancer progression by affecting tumor cell invasiveness, ability to disseminate through the blood circulation and to metastasize in distant organs. During metastasis tumor cell-derived glycans enable binding to cells in their microenvironment including endothelium and blood constituents through glycan-binding receptors - lectins. In this review we will discuss current concepts how tumor cell-derived glycans contribute to metastasis with the focus on three types of lectins: siglecs, galectins and selectins. Siglecs are present on virtually all hematopoetic cells and usually
Drug Metabolism and Toxicology, Faculty of Pharmaceutical Sciences, Kanazawa University, Kakuma-machi, Kanazawa, Japan (S.O., Y.K., T.F., T.Y., M.N.); CLEA Japan, Fujinomiya, Japan (M.H.); DMPK Research Laboratories, Sohyaku Innovative Research Division, Mitsubishi Tanabe Pharma Corporation, Toda, Japan (A.I.); and Discovery Technology Laboratories, Sohyaku Innovative Research Division, Mitsubishi Tanabe Pharma Corporation, Toda, Japan (T.K.) ...
The present invention provides methods and compositions for improved expression and production of recombinant antibodies in prokaryotic expression systems. Particularly contemplated are prokaryotic expression and production of full length aglycosylated antibodies. The antibody products of the invention can be used in various aspects of biological research, diagnosis and medical treatment.
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How is low-molecular-mass highly glycosylated protein abbreviated? L-HGP stands for low-molecular-mass highly glycosylated protein. L-HGP is defined as low-molecular-mass highly glycosylated protein rarely.
Asn-linked glycosylation of proteins is a universal cotranslational and posttranslational modification of proteins entering the secretory pathway. In all eukaryotes, a hallmark of N-glycosylation is the en bloc transfer of a common preassembled oligosaccharide (Glc3Man9GlcNAc2) from the lipid carrier dolichol pyrophosphate to selected Asn residues in the sequence Asn-X-Ser/Thr (where X ≠ P) within nascent polypeptides. This transfer takes place in the lumen of the endoplasmic reticulum (ER) and is catalyzed by the oligosaccharyltransferase (OST), a heteromeric membrane protein complex (Kelleher and Gilmore, 2006). In yeast (Saccharomyces cerevisiae) and mammals, OST consists of a catalytically active subunit (STAUROSPORIN AND TEMPERATURE SENSITIVE3 [STT3]) and several different noncatalytic subunits that contribute to N-glycosylation by regulation of the substrate specificity, stability, or assembly of the complex (Yan and Lennarz, 2002; Mohorko et al., 2011). In yeast, the OST complex is ...
The stereoselectivity of glycosylation … … reactions can depend critically on the reactivity of the acceptor glycoside (the nucleophile in the reaction). In their Communication on page 8240 ff., J. D. CodEe et al. report a facile system that maps the relationship between glycosyl acce...
Sevigny M.B., Li C.F., Alas M., Hughes-Fulford M.. Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H(2). COX-2 exists as 72 and 74kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn(580). In this study, Asn(580) was mutated to determine the biological significance of this variable glycosylation. COS-1 cells transfected with the mutant gene were unable to express the 74kDa glycoform and were found to accumulate more COX-2 protein and have five times greater COX-2 activity than cells expressing both glycoforms. Thus, COX-2 turnover appears to depend upon glycosylation of the 72kDa glycoform.. FEBS Lett. 580:6533-6536(2006) [PubMed] [Europe PMC] ...
A purified mammalian proteoglycan, and genetic information encoding such proteoglycans, having a core polypetide molecular weight of about 30 kD to about 35 kD, and comprising a hydrophilic amino terminal extracellular region, a hydrophilic carboxy terminal cytoplasmic region, a transmembrane hydrophobic region between said cytoplasmic and extracellular regions, a protease susceptible cleavage sequence extracellularly adjacent the transmembrane region of the peptide, and at least one glycosylation site for attachment of a heparan sulfate chain to said extracellular region, said glycosylation site comprising a heparan sulfate attachment sequence represented by a formula Xac-Z-Ser-Gly-Ser-Gly, where Xac represents an amino acid residue having an acidic sidechain, and Z represents from 1 to 10 amino acid residues. Additional peptides having this glycosylation site and genetic information useful for preparing a number of variations based on this glycosylation site are also provided.
Toda la información sobre las últimas publicaciones científicas de la Clínica Universidad de Navarra. Acquired potential N-glycosylation sites within the tumor-specific immunoglobulin heavy chains of B-cell malignancies
The hyaluronan (HA)-binding function (lectin function) of the leukocyte homing receptor, CD44, is tightly regulated. Herein we address possible mechanisms that regulate CD44 isoform-specific HA binding. Binding studies with melanoma transfectants expressing CD44H, CD44E, or with soluble immunoglobulin fusions of CD44H and CD44E (CD44H-Rg, CD44E-Rg) showed that although both CD44 isoforms can bind HA, CD44H binds HA more efficiently than CD44E. Using CD44-Rg fusion proteins we show that the variably spliced exons in CD44E, V8-V10, specifically reduce the lectin function of CD44, while replacement of V8-V10 by an ICAM-1 immunoglobulin domain restores binding to a level comparable to that of CD44H. Conversely, CD44 bound HA very weakly when exons V8-V10 were replaced with a CD34 mucin domain, which is heavily modified by O-linked glycans. Production of CD44E-Rg or incubation of CD44E-expressing transfectants in the presence of an O-linked glycosylation inhibitor restored HA binding to CD44H-Rg and ...
N-linked glycosylation is not required for hIL-6 receptor binding, STAT signaling or cytokine-dependent B9.11 cell proliferation. (A) Calibration of quantities
One of the most common posttranslational modifications of eukaryotic proteins is glycosylation. Glycosylation of proteins can affect many biological activities. For therapeutic glycoproteins, it can modify biological activity, targeting, trafficking, serum half life, clearance, and recognition by receptors (1, 2). For such reasons, biomanufacturers must monitor and characterize the glycosylation patterns of their recombinant therapeutic proteins (3, 4). Therapeutic proteins have two main types of glycosylation: N-linked glycans and O-linked glycans (5). Attachment of an N-glycan starts in the endoplasmic…. ...
The LIP-6 MAb was produced against the undifferentiated cell line bh2-1 and recognizes an antigen expressed on all pre-B and B cell lines tested and some myeloid lineage lines. FACS analysis of normal tissues showed that LIP-6 is expressed on B lineage cells at all stages of differentiation, from bone marrow pre-B to plasma cells. T cells and thymocytes are LIP-6-, and splenic CD11b+ cells are heterogeneous for LIP-6 expression. The LIP-6 MAb was shown to precipitate a major 75-kDa and a minor 85-kDa protein under reducing conditions and a large protein of | 240 kDa under nonreducing conditions. Removal of N-linked sugars from the reduced lysates resulted in a single 65-kDa protein, suggesting that there is differential glycosylation of a single 65-kDa protein that forms disulfide-linked multimers. Finally, the LIP-6 antigen was shown not to be linked to the cell surface via a GPI linkage.
Highly conserved threonine residues were noted near the C-terminus of the external surface glycoproteins of HIV-1, SIV, and influenza A virus; this threonine residue was shown to be the efficient target of O-glycosylation on all three viruses. In all three cases, this O-glycosylated threonine was essential for the infectivity of the virus. We will define the functional role of C-terminal threonine glycosylation for HIV-1 and we will develop assays amenable to high throughput screening for the development of antiviral drugs. We will delineate protein-peptide and peptide-peptide interactions that are dependent on the O-glycosylated threonine of gp120. We will also examine whether there are rare examples of naturally-occurring HIV-1 sequences that are functional without an O-glycosylated threonine at this location ...
Highlights: • Glycosylatable GFP (gGFP) is developed for the use in mammalian cells. • gGFP selectively loses its fluorescence upon N-linked glycosylation in the ER lumen. • Differential fluorescence/glycosylation pattern probes membrane protein topology. • Membrane topology of URG7, MRP6{sub 102}, and SP-C was determined by gGFP tagging in vivo. - Abstract: Experimental tools to determine membrane topology of a protein are rather limited in higher eukaryotic organisms. Here, we report the use of glycosylatable GFP (gGFP) as a sensitive and versatile membrane topology reporter in mammalian cells. gGFP selectively loses its fluorescence upon N-linked glycosylation in the ER lumen. Thus, positive fluorescence signal assigns location of gGFP to the cytosol whereas no fluorescence signal and a glycosylated status of gGFP map the location of gGFP to the ER lumen. By using mammalian gGFP, the membrane topology of disease-associated membrane proteins, URG7, MRP6{sub 102}, SP-C(Val) and ...
Structural Analysis of Glycosylated Peptides in Complex Mixtures with Ion Trap MS n Shiaw-Lin Wu Pavel Bondarenko Tom Shaler Paul Shieh and William S. Hancock Protein Glycosylation The data presented here can be acquired using a,Structural,Analysis,of,Glycosylated,Peptides,in,Complex,Mixtures,with,,,,,,,,,,,,Ion,Trap,MSn,biological,advanced biology technology,biology laboratory technology,biology device technology,latest biology technology
O-linked glycosylation[edit]. Main article: O-linked glycosylation. O-linked glycosylation is a form of glycosylation that ... N-linked glycosylation[edit]. Main article: N-linked glycosylation. N-linked glycosylation is a very prevalent form of ... disorders of protein N-glycosylation, disorders of protein O-glycosylation, disorders of lipid glycosylation and disorders of ... Chemical glycosylation[edit]. Glycosylation can also be effected using the tools of synthetic organic chemistry. Unlike the ...
Glycosylation[edit]. In biology, glycosylation is the process by which a carbohydrate is covalently attached to an organic ... N-linked glycosylation involves oligosaccharide attachment to asparagine via a beta linkage to the amine nitrogen of the side ... In N-glycosylation for eukaryotes, the oligosaccharide substrate is assembled right at the membrane of the endoplasmatic ... Peter-Katalinić J (2005). "Methods in enzymology: O-glycosylation of proteins". Methods in Enzymology. 405: 139-71. doi:10.1016 ...
Glycosylation and aggregation[edit]. Mucin genes encode mucin monomers that are synthesized as rod-shape apomucin cores that ... are post-translationally modified by exceptionally abundant glycosylation. The dense "sugar coating" of mucins gives them ...
Feizi T, Larkin M (September 1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID ... Dedera DA, Gu RL, Ratner L (March 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 ... implications for glycosylation and CD4 binding". Genetic Analysis, Techniques and Applications. 7 (6): 160-71. doi:10.1016/0735 ... effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452-6. PMC 250699. PMID 2542563.. ...
Congenital_disorder_of_glycosylation[redigér , redigér wikikode]. [2] [3] N-acetyl-5-methoxytryptamine ...
Dong DL, Xu ZS, Chevrier MR, Cotter RJ, Cleveland DW, Hart GW (August 1993). "Glycosylation of mammalian neurofilaments. ...
Initial glycosylation as assembly continues. This is N-linked (O-linking occurs in the Golgi). *N-linked glycosylation: If the ...
Types of glycosylation[edit]. There are several types of glycosylation, although the first two are the most common. ... In P-glycosylation, sugars are attached to phosphorus on a phosphoserine.. *In C-glycosylation, sugars are attached directly to ... N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins.[1] ... In O-glycosylation, sugars are attached to oxygen, typically on serine or threonine, but also on tyrosine or non-canonical ...
This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked glycosylation ... if the defective step occurs after the action of OST in the N-linked glycosylation pathway or involves O-linked glycosylation.[ ... CDG syndromes are genetic disorders of the glycosylation pathway. They are labelled "Type I" if the defective gene is for an ... Imperiali B (November 1997). "Protein Glycosylation: The Clash of the Titans". Accounts of Chemical Research. 30 (11): 452-459 ...
1995). "Site-specific glycosylation of bovine butyrophilin". J. Biochem. 117 (1): 147-57. PMID 7775382.. ...
Brownlee, M. D. (1995). "Advanced Protein Glycosylation in Diabetes and Aging". Annual Review of Medicine. 46: 223-234. doi: ... protein glycosylation and the resulting collagen abnormalities lead to greater transversal section - i.e. thickening - of ... in the body end up in uncontrolled covalent bonding of aldose sugars to a protein or lipid without any normal glycosylation ...
These subunits are heavily modified by glycosylation. The alpha subunit is common to each protein dimer (well conserved within ...
Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L (Nov 1986). "Glycosylation inhibitors block the ... Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human ... Dedera DA, Gu RL, Ratner L (Mar 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 ... "Entrez Gene: GANC glucosidase, alpha; neutral C". Feizi T, Larkin M (Sep 1990). "AIDS and glycosylation". Glycobiology. 1 (1): ...
Feizi T, Larkin M (1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID 2136376. Németh ... Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 ...
1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. ... 1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 ... Check date values in: ,access-date= (help) Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi: ... Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 ...
Genetic Glycosylation Diseases. 1792 (9): 881-887. doi:10.1016/j.bbadis.2009.07.001. PMC 2748147 . PMID 19596068. Eisenberg I, ...
Alterations in glycosylation are often acquired in cases of cancer and inflammation, which may have important functional ... Rhodes J, Campbell BJ, Yu LG (2001). "Glycosylation and Disease". Encyclopedia of Life Sciences. John Wiley & Sons, Inc. doi: ... Patterson MC (2005). "Metabolic mimics: the disorders of N-linked glycosylation". Seminars in Pediatric Neurology. 12 (3): 144- ... N-linked glycosylation can be seen in antibodies, on cell surfaces, and on various proteins throughout the matrix. ...
Genetic Glycosylation Diseases. 1792 (9): 915-920. doi:10.1016/j.bbadis.2008.12.005. "Ferritin: Reference Range, Interpretation ...
Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human ... Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L (1987). "Glycosylation inhibitors block the ... Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID 2136376. Land A ... Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 ...
One possible N-glycosylation site was predicted, but a signal peptide was not detected. Thus, it is possible that CCDC29 does ... ". "ExPASy N-glycosylation". "ExPASy Phosphorylation". "ExPASy Phyre2". "ExPASy SOSUI". ...
1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 ... Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID 2136376. Boot ... Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency ... Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 ...
glycosylation. A catch-all name for a set of very common and very heterogeneous chemical modifications. Sugar moieties can be ... All glycosylation can be blocked with certain inhibitors, such as tunicamycin.. *deamidation (succinimide formation) ...
Roos MD, Su K, Baker JR, Kudlow JE (Nov 1997). "O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions ... OGT inhibits the activity of 6-phosophofructosekinase PFKL by mediating the glycosylation process. This then acts as a part of ... For the same-site occupancy, OGT competes with kinase to catalyze the glycosylation of the protein instead of phosphorylation. ... Konrad RJ, Kudlow JE (Nov 2002). "The role of O-linked protein glycosylation in beta-cell dysfunction". International Journal ...
GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview GeneReviews/NIH/NCBI/UW entry on PMM2-CDG (CDG- ... Mutations in the gene have been shown to cause defects in the protein glycosylation pathway which manifest as congenital ... Jaeken J, Matthijs G (2002). "Congenital disorders of glycosylation". Annual Review of Genomics and Human Genetics. 2: 129-51. ... "Mutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia)". Human Mutation. 16 (5): 386-94. doi: ...
His research has largely focused on molecular cell biology and, in particular, how protein glycosylation contributes to the ... Marth, J.D.; Grewal, P.K. (2008). "Mammalian glycosylation in immunity". Nat. Rev. Immunol. 8: 874-887. doi:10.1038/nri2417. ... Ohtsubo, K.; Marth, J.D. (2006). "Glycosylation in cellular mechanisms of health and disease". Cell. 126: 855-867. doi:10.1016/ ... 30 January 2001). "Genetic remodeling of protein glycosylation in vivo induces autoimmune disease". Proc Natl Acad Sci USA. 98 ...
Advanced Glycosylation End Products: Products derived from the nonenzymatic reaction of glucose and proteins in vivo that ... Advanced Glycosylation End Products. Subscribe to New Research on Advanced Glycosylation End Products ... Advanced Glycosylation End Products: 2322*advanced glycation end products-bovine serum albumin: 35 ... 12/01/1994 - "Immunohistochemical study of human advanced glycosylation end-products (AGE) in chronic renal failure.". 01/01/ ...
Targeted-glycosylation of "non-core region" of interleukin-11 modulates its biological function. (57.15). Saeko Yanaka-Okada, ... Second, glycosylation of a predicted mini alpha-helix led to cytokine inactivation, demonstrating that this structural element ... Targeted-glycosylation of non-core region of interleukin-11 modulates its biological function. (57.15) ... Targeted-glycosylation of "non-core region" of interleukin-11 modulates its biological function. (57.15) ...
Protein Glycosylation. Glycosylation. Localization. PTMs for Polypeptide GalNac Transferase 10/GALNT10. Learn more about PTMs ...
Many eukaryotic proteins can be produced in E. coli but are produced in a nonfunctional, unfinished form, since glycosylation ...
Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins. Furthermore, rAAL can be ... 3 Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins.4 Furthermore, rAAL can be ...
... and questions answered by our Genetic and Rare Diseases Information Specialists for Congenital disorders of glycosylation ... disorders of glycosylation (CDG) are a group of inherited. metabolic disorders. that affect a process called glycosylation. ... Congenital disorders of glycosylation Title Other Names:. CDG; Carbohydrate-deficient glycoprotein syndromes; Congenital ... Glycosylation is the complex process by which all human cells. build long sugar chains that are attached to proteins. , which ...
O-linked glycosylation[edit]. Main article: O-linked glycosylation. O-linked glycosylation is a form of glycosylation that ... N-linked glycosylation[edit]. Main article: N-linked glycosylation. N-linked glycosylation is a very prevalent form of ... disorders of protein N-glycosylation, disorders of protein O-glycosylation, disorders of lipid glycosylation and disorders of ... Chemical glycosylation[edit]. Glycosylation can also be effected using the tools of synthetic organic chemistry. Unlike the ...
Moreover, there is no magic bullet for analyzing glycosylation in monoclonal antibodies. The methods for identifying the ... Experts say glycosylation analysis is the most important and least precise area of chemical analysis. ... "Glycosylation analysis is the most important and least precise area of chemical analysis," Stein said. "The methods for ... "Were just trying to measure things better." Part of that involves glycosylation of mAbs, which make up a common class of ...
... Ivan J Delgado delgadoi at PILOT.MSU.EDU Mon Feb 3 16:02:11 EST 1997 *Previous message: Transfection of B cells ... A question regarding glycosylation of proteins and how that looks in a western. I have two different antibodies raised against ... Could this be glycosylation?. How could one test for it? Ivan ... Next message: glycosylation * Messages sorted by: [ date ] [ ...
... Smeekens wbtmcbw at cc.ruu.nl Wed Nov 24 03:07:59 EST 1993 *Previous message: GUS RT-PCR ... Dear Netters I am looking for the GUS gene from which the glycosylation sites have been removed by site directed mutagenesis. I ...
DOLK-congenital disorder of glycosylation (DOLK-CDG, formerly known as congenital disorder of glycosylation type Im) is an ... Glycosylation changes proteins in ways that are important for their functions. During glycosylation, sugars are added to ... called alpha-dystroglycan, has been shown to have reduced glycosylation in people with DOLK-CDG. Impaired glycosylation of ... The other signs and symptoms of DOLK-CDG are likely due to the abnormal glycosylation of additional proteins in other organs ...
PMM2-congenital disorder of glycosylation (PMM2-CDG, also known as congenital disorder of glycosylation type Ia) is an ... Glycosylation modifies proteins so they can perform a wider variety of functions. Mutations in the PMM2 gene lead to the ... Krasnewich D, OBrien K, Sparks S. Clinical features in adults with congenital disorders of glycosylation type Ia (CDG-Ia). Am ... Haeuptle MA, Hennet T. Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol- ...
Glycosylation. A process in which antibodies are decorated in a specific way with carbohydrates to make it acknowledgeable by ... The glycosylation of antibodies. Antibodies, like many other natural proteins, are normally decorated with sugars. Optimizing ... Drawn to Science cheat sheet for Glycosylation of antibodies. Antibodies. Y-shaped proteins that our bodies use to identify and ... Used in a process called glycosylation to make therapeutic antibodies acceptable to the human body. ...
Even though O-glycosylation has been expected on the spike protein of SARS-Cov-2, this is the first report of the site of O- ... Glycosylation of the S protein is also complex and important, as we can see from the previous studies. Different expressing ... 3. Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2[3]. Azadis team from the ... In this article, a few recent studies are outlined in order to look at the more scientific details about the glycosylation of ...
Glycosylation RT2 Profiler PCR Array The Human Glycosylation RT² Profiler PCR Array profiles the expression of 84 key genes ... Glycosylation RT2 Profiler PCR Array The Mouse Glycosylation RT² Profiler PCR Array profiles the expression of 84 key genes ... Glycosylation RT2 Profiler PCR Array The Rat Glycosylation RT² Profiler PCR Array profiles the expression of 84 key genes ... The process of glycosylation adds and removes sugar residues to and from oligosaccharides covalently linked to proteoglycans, ...
Inherent differences in glycosylation (unique glycosylation signatures) among ion channel subunits and isoforms as described ... Regulated and aberrant glycosylation modulate cardiac electrical signaling. Marty L. Montpetit, Patrick J. Stocker, Tara A. ... Regulated and aberrant glycosylation modulate cardiac electrical signaling. Marty L. Montpetit, Patrick J. Stocker, Tara A. ... Regulated and aberrant glycosylation modulate cardiac electrical signaling Message Subject (Your Name) has sent you a message ...
Glycosylation of membrane proteins plays a crucial role in various physiological events, including intercellular recognition ... Pavić T., Gornik O. (2017) Analysis of N-Glycosylation of Total Membrane Proteins. In: Lauc G., Wuhrer M. (eds) High-Throughput ... Glycosylation of membrane proteins plays a crucial role in various physiological events, including intercellular recognition ... Haltiwanger RS, Lowe JB (2004) Role of glycosylation in development. Annu Rev Biochem 73:491-537. doi: 10.1146/annurev.biochem. ...
In the past two decades more and more attention is being paid to changes in glycosylation and in this review we describe some ... Glycosylation of serum proteins in inflammatory diseases.. Gornik O1, Lauc G. ... but it is evident that glycosylation plays an important role in the inflammatory response. Maybe the greatest value of these ... clinical laboratories and further efforts have to be made to develop simple analytical tools to study changes in glycosylation. ...
Glycoprotein glycosylation and cancer progression.. Dennis JW1, Granovsky M, Warren CE. ... Glycosylation of glycoproteins and glycolipids is one of many molecular changes that accompany malignant transformation. GlcNAc ...
N-glycosylation, (2) O-glycosylation, (3) O-linked GlcNAc glycosylation, (4) proteoglycan biosynthesis, (5) glycolipid ... Glycosylation processes can be chemically regulated by inhibition of glycosyltransferases or glycosidases with natural and ... This review highlights recent developments in chemical regulation of glycosylation processes with specific targets including: ... These diverse structures are controlled by complex glycosylation processes in cells, which are mediated by various ...
Contact us today to find out how SGSs world-class Glycosylation Analysis can help determine how post-translational factors ... Home › Life Sciences › Biopharmaceutical Services › Laboratory Services › Glycosylation Analysis Life Sciences Glycosylation ... Glycosylation of Proteins: Structure, Function & Analysis. Download Glycosylation of Proteins: Structure, Function & Analysis ... Glycosylation site analysis. Our experts are always at hand to give advice on what may be most appropriate for you, whether you ...
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Direct Quantitative Determination of Ceramide Glycosylation in Vivo: A New Approach to Evaluate Cellular Enzyme Activity of ...
Van den Eijnden,D.H., Neeleman,A.P., Van der Knaap,W.P., Bakker,H., Agterberg,M., and van Die,I. (1995). Novel glycosylation ... van Die,I., Van Tetering,A., Bakker,H., Van den Eijnden,D.H., and Joziasse,D.H. (1996). Glycosylation in lepidopteran insect ... Startseite >Institute>Zentrum Biochemie>Institut für Klinische Biochemie>Research>Endoplasmic Reticulum glycosylation ...
Gene Ontology Term: protein glycosylation. GO ID. GO:0006486 Aspect. Biological Process. Description. A protein modification ... protein amino acid glycosylation, protein-carbohydrate complex assembly View GO Annotations in other species in AmiGO ...
  • Even though O-glycosylation has been expected on the spike protein of SARS-Cov-2, this is the first report of the site of O-glycosylation and identity of the O-glycans attached on the subunit S1. (news-medical.net)
  • In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O -linked pathway and the biological function of flagella glycosylation. (mdpi.com)
  • Owing to the complex nature of their biosynthesis, glycans are particularly versatile and apparently a large part of human variation derives from differences in protein glycosylation. (degruyter.com)
  • The specific hypothesis behind the proposed research is that reconstitution of a eukaryotic N-glycosylation pathway in E. coli will result in N-glycoproteins with structurally homogeneous human-like glycans. (sbir.gov)
  • A , For each site of N -linked glycosylation identified, the number of unique glycans identified was determined. (mcponline.org)
  • Due to the plasticity of glycosylation, mass spectrometry (MS)-based glycoproteomics characterizes glycoproteins at different levels, including glycosylation sites (glycosites), glycans, and glycosite-specific glycans 27 28 . (hupo.org)
  • In vivo synthesis by installation of new glycosylation pathways in CHO-cells and in vitro synthesis of O-glycans using glycosyltransferases produced at an industrial scale in CHO-cells, combined with recycling pathways for sugar nucleotide substrates have been studied. (europa.eu)
  • In addition to the structural variety of N-glycans, there is a difference in the glycosylation pattern of human amylase isozymes [5, both the N427 and N476 sites in human salivary amylase can be glycosylated to some extent, whereas those in human pancreatic amylase are either glycosylated to a lesser extent or not glycosylated. (scirp.org)
  • Eight NSs and outlets for host cell protein N-linked and O-linked glycans as well as mAb glycosylation have been considered. (aiche.org)
  • Glycans are generally attached to serine or threonine (O glycosylation) or to asparagine (N glycosylation) residues. (asm.org)
  • RAGE has two N-glycosylation sites on the V-domain and both sites are occupied by complex and hybrid or high mannose N-glycans. (atlasgeneticsoncology.org)
  • Recent studies have investigated the site occupancy of these types of glycosylation and also defined specific roles for these glycans on Notch structure and function. (springer.com)
  • Background Immunoglobulin G (IgG) effector functions are regulated by the composition of glycans attached to a conserved N-glycosylation site in the Fc part. (uni-muenchen.de)
  • I am trying now a different method using a kit for deglycosylation in reducing and native conditions (because I would like to measure the activity of my protein as well), then I run a western blotting and I hope to see different bands that correspond to the different levels of glycosylation of my protein, from 6 N-glycans (or 7 in my mutants) to 0 N-glycans. (scientistsolutions.com)
  • Furthermore, HABD is known to be N-glycosylated, and such glycosylation can diminish HA binding when the associated N-glycans are capped with sialic acid residues. (frontiersin.org)
  • Guo M, Hang H, Zhu T et al (2008) Effect of glycosylation on biochemical characterization of recombinant phytase expressed in Pichia pastoris . (springer.com)
  • We analyzed the glycosylation efficiency of N-glycosylation sites in recombinant Amy2A mutants produced by HEK293 cells and found that glycosylation efficiencies of N427 and N476 were 3% - 18% and 40% - 52%, respectively, indicating that the major N-glycosylation site of glycosylated Amy2A produced by HEK293 cells is N476. (scirp.org)
  • In this work, we describe a model-based platform for understanding the culture factors that affect recombinant protein glycosylation in Chinese hamster ovary (CHO) cells, the workhorse of the biopharmaceutical industry. (aiche.org)
  • These diverse structures are controlled by complex glycosylation processes in cells, which are mediated by various glycosyltransferases and glycosidases. (go.jp)
  • Glycosylation processes can be chemically regulated by inhibition of glycosyltransferases or glycosidases with natural and synthetic molecules. (go.jp)
  • This review presents a detailed insight into the exciting possibilities of multiple glycosylation using enzymes, particularly glycosyltransferases (EC 2.4). (rsc.org)
  • A female patient with cystic fibrosis showed high %CDT as well as a type 2 Tf-IEF profile, supporting the hypothesis that altered function of cystic fibrosis transmembrane conductance regulator (CFTR) affects the compartmentalization of glycosyltransferases in the Golgi, thereby disturbing protein glycosylation (39). (thefreedictionary.com)
  • Glycosylation (see also chemical glycosylation ) is the reaction in which a carbohydrate , i.e. a glycosyl donor , is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor ). (wikipedia.org)
  • These findings suggest that the changes in protein structures alter the efficiency of glycosylation in the SAA4 molecule. (hindawi.com)
  • This category of metabolic disorders can be divided into four basic groups depending on where the glycosylation process occurs on the molecule. (wikipathways.org)
  • N‐ linked glycosylation commences in the endoplasmic reticulum and is completed in the Golgi apparatus. (els.net)
  • O‐ linked glycosylation commences and is completed in the Golgi apparatus. (els.net)
  • Dean N (1999) Asparagine-linked glycosylation in the yeast golgi. (springer.com)
  • Although ER/Golgi-derived glycosylation is one of the most frequently occurring classes of PTMs ( 6 ), these extracellular modifications continue to be a major challenge because of technical difficulties both in their structural characterization and in deciphering their biological roles. (mcponline.org)
  • The cargo trafficking mechanisms and the glycosylation activities of the Golgi have been studied extensively but separately, leading to the development of two rather distinct research fields, which have interacted poorly over the years. (embo.org)
  • What is the role of membrane trafficking in the organization of the glycosylation machinery in the Golgi? (embo.org)
  • How are the trafficking and glycosylation functions of the Golgi coordinated? (embo.org)
  • Applicants presenting work on the interface between trafficking and glycosylation at the Golgi will be given preference. (embo.org)
  • The lowest scale model is the del Val glycosylation model describing the N-linked glycosylation process of the antibody heavy chain through the Golgi apparatus viewed as a plug flow reactor. (aiche.org)
  • Generally, N-glycosylation processes spread over three cellular compartments - cytosol, endoplasmic reticulum and Golgi apparatus. (wikipathways.org)
  • Millions afflicted with Chagas disease and other disorders of aberrant glycosylation suffer symptoms consistent with altered electrical signaling such as arrhythmias, decreased neuronal conduction velocity, and hyporeflexia. (pnas.org)
  • In patients with eye, brain and skeletal muscle abnormalities, O -glycosylation disorders involving abnormal posttranslational processing of alpha-dystroglycan should be considered. (oncologynurseadvisor.com)
  • Disorders of O -glycosylation are not detected by this screening test. (oncologynurseadvisor.com)
  • Studies of epigenetic modification of genes involved in protein glycosylation are still scarce, but their results indicate that this process might be very important for the regulation of protein glycosylation. (degruyter.com)
  • We identified 26 genes involved in glycosylation and examined 93 single nucleotide polymorphisms (SNP) with a minor allele frequency of ≥0.05 in relation to incident ovarian cancer. (aacrjournals.org)
  • These studies are significant because they should (i) provide the necessary genetic tools to help elucidate the crucial role of glycosylation in a myriad of biological phenomena and (ii) enable the biotechnological synthesis of novel glycoconjugates and potential immunostimulating agents for research, industrial and therapeutic applications. (sbir.gov)
  • Here, we demonstrate that the glycosylation of FTH_0069, DsbA, and PilA was affected in an isogenic mutant with a disrupted wbtDEF gene cluster encoding O-antigen synthesis and in a mutant with a deleted pglA gene encoding pilin oligosaccharyltransferase PglA. (diva-portal.org)
  • First, IgG1 glycosylation patterns were different in CSF vs. serum, in the MS group and even in control donors without intrathecal IgG synthesis. (uni-muenchen.de)
  • Fourth, CSF IgG1 glycosylation correlated with the degree of intrathecal IgG synthesis and CSF cell count. (uni-muenchen.de)
  • Fluorine-Directed Glycosylation Enables the Stereocontrolled Synthesis of Selective SGLT2 Inhibitors for Type II Diabetes. (bioportfolio.com)
  • Catalytic Glycosylations in Oligosaccharide Synthesis. (bioportfolio.com)
  • Haltiwanger RS, Lowe JB (2004) Role of glycosylation in development. (springer.com)
  • Here, we investigated the role of glycosylation in ASIC1a trafficking and acidosis-induced dendritic remodeling. (jneurosci.org)
  • Khidekel and colleagues also found that glycosylation is reversible, suggesting that it may serve a regulatory function akin to phosphorylation and other post-translational modifications. (alzforum.org)
  • The analysis of glycosylation is more complex than DNA and RNA or protein analysis as glycosylation is a non‐template‐driven event. (els.net)
  • We investigated BCL11B for O-glycosylation and discovered that BCL11B is not glycosylated, but changing glycosylation levels in the system changes the phosphorylation of BCL11B. (oregonstate.edu)
  • In addition to contribution by protein interaction domains, post-translational modifications such as glycosylation of the receptors, or acetylation or phosphorylation of ligands could also play important roles in defining specificity of interactions, multimerization and downstream signaling. (atlasgeneticsoncology.org)
  • Individuals with a CDG are missing one of the enzymes that is required for glycosylation. (nih.gov)
  • Many enzymes are involved in both N‐ and O‐ linked glycosylation. (els.net)
  • Here, we explored differences in glycosylation of CA125 between serum from patients with ovarian cancer and healthy controls. (mdpi.com)
  • Second, in MS patients vs. controls, IgG1 glycosylation patterns were altered in CSF, but not in serum. (uni-muenchen.de)
  • The difference in the glycosylation efficiency of each N-glycosylation site also seemed to contribute in part to generate different glycosylation patterns of human amylases. (scirp.org)
  • In this study, we evaluated the glycosylation state of human amylase isozymes and found that the different glycosylation patterns of human amylases were related to the types of amylase-producing cells rather than the types of amylase isozymes. (scirp.org)
  • These findings seem to be highly related to the different glycosylation pattern of human amylases. (scirp.org)
  • 1 In particular, scientists must characterize the addition of sugars-glycosylation-but that's no small feat. (genengnews.com)
  • During glycosylation, sugars are added to dolichol phosphate in order to build the oligosaccharide chain. (medlineplus.gov)
  • It has been shown that the process of protein glycosylation can be partially driven by the intracellular availability of nucleotide sugars (NSs), which are the co-substrates to the glycosylation reactions. (aiche.org)
  • In both cases, sugars are transferred en bloc by an oligosaccharyltransferase (OTase) named PglL in N. meningitidis and PilO in P. aeruginosa . (asm.org)
  • The in vivo oxidation of lipids and lipid-containing molecules has been discovered to be initiated by the concurrent reaction of such lipid materials with reducing sugars such as glucose, advanced glycosylation endproducts such as AGE-peptides, or a compound which forms advanced glycosylation endproducts, to form materials or particles known as AGE-lipids. (freepatentsonline.com)
  • Here we show that regulated and aberrant glycosylation modulate cardiac ion channel activity and electrical signaling through a cell-specific mechanism. (pnas.org)
  • A mechanism is described by which cardiac function is controlled and modulated through physiological and pathological processes that involve regulated and aberrant glycosylation. (pnas.org)
  • N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell-cell and cell-extracellular matrix attachment. (wikipedia.org)
  • Notch activity is regulated at several levels, but O -linked glycosylation of Epidermal Growth Factor (EGF) repeats in the Notch extracellular domain has emerged as a major regulator that, depending on context, can increase or decrease Notch activity. (springer.com)
  • 2 Working with NIST fellow Stephen Stein and others, De Leoz explored reports from 76 laboratories around the world to compare various methods of analyzing glycosylation of monoclonal antibodies (mAbs)-particularly a NIST reference (NISTmAb PS) and a modified version of it. (genengnews.com)
  • In thinking about the reports analyzed for this study, De Leoz said, "There is no magic method for analyzing glycosylation in monoclonal antibodies. (genengnews.com)
  • NIST interlaboratory study on glycosylation analysis of monoclonal antibodies: Comparison of results from diverse analytical methods. (genengnews.com)
  • The Env glycosylation is mostly conserved but continues to evolve to modulate viral infectivity. (ku.edu)
  • Dear Netters I am looking for the GUS gene from which the glycosylation sites have been removed by site directed mutagenesis. (bio.net)
  • They characterized the site-specific N-glycosylation of HEK293 cell expressed SARS-CoV-2 S1 protein and insect cell expressed S protein. (news-medical.net)
  • The N -glycosylation site of rNPI was analyzed by nano LC-MS/MS after digesting by trypsin and Glu-C, and the unique potential site Asn 41 of mature peptide was found to be glycosylated. (springer.com)
  • We also found that the glycosylation efficiencies of the N427 and N476 sites were different and the N476 site was more efficiently glycosylated than the N427 site. (scirp.org)
  • Glycosylation site alteration in the evolution of influenza A (H1N1) viruses. (thefreedictionary.com)
  • First, are you familiar with the N-glycosylation site mapping technique in which PNGaseF digestion is performed on tryptic peptides in the presence of O18 water? (scientistsolutions.com)
  • Then when you perform a LC-MS/MS-spec analysis and look at your MS-spec sequence fingerprint, you should be able to find that one extra tryptic peptide that contains the new N-glycosylation site in the mutant that is different from the spectra you get from the wild type sample. (scientistsolutions.com)
  • Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promo. (ingentaconnect.com)
  • Importantly, the use of PNGase F in these approaches results in the loss of all information regarding the oligosaccharide(s) present on specific glycosylation sites. (mcponline.org)
  • Drift variants contained HA substitutions and alterations in the potential N-linked glycosylation sites of HA. (eurosurveillance.org)
  • N -glycosylation of the two glycosylation sites, Asn393 and Asn366, has differential effects on ASIC1a biogenesis. (jneurosci.org)
  • Flagellin from 81-176 contains 19 sites of O-linked glycosylation to the monosaccharide pseudaminic acid (5,7-diacetamido-3,5,7,9-tetradeoxy- l - glycero - l - manno -nonulosonic acid) and analogs of pseudaminic acid ( 42 ). (asm.org)
  • This N-glycosylation profiling and determination of differences between distinct expression systems could shed light on the infection mechanism and promote the development of targeted therapeutics and vaccines. (news-medical.net)
  • In general, salivary amylase is more frequently glycosylated than pancreatic amylase, and it is still uncertain why differences in the glycosylation pattern among human amylase isozymes occur. (scirp.org)
  • It is still uncertain, however, why differences in the glycosylation pattern among human amylase isozymes occur. (scirp.org)
  • Discerning interclade and intraclade glycosylation variations could provide valuable information in understanding the molecular differences among the different HIV-1 clades and in designing new Env-based immunogens. (ku.edu)