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.
A genetically heterogeneous group of heritable disorders resulting from defects in protein N-glycosylation.
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.
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)
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
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.
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.
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.
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.
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
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.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
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).
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)
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.
The characteristic 3-dimensional shape of a carbohydrate.
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, EC, EC, and EC
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.
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.-.
Established cell cultures that have the potential to propagate indefinitely.
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.
The N-acetyl derivative of glucosamine.
A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.
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)
An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
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.
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.-.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Eicosamethyl octacontanonadecasen-1-o1. Polyprenol found in animal tissues that contains about 20 isoprene residues, the one carrying the alcohol group being saturated.
Proteins prepared by recombinant DNA technology.
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)
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.
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.
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.
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.
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.
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)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Phosphoric acid esters of dolichol.
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)
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.-.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The N-acetyl derivative of galactosamine.
The sum of the weight of all the atoms in a molecule.
An alpha-glucosidase inhibitor with antiviral action. Derivatives of deoxynojirimycin may have anti-HIV activity.
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.
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)
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
Glycoproteins found on the membrane or surface of cells.
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.
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.
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.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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 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.
Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.
A nucleoside diphosphate sugar which serves as a source of N-acetylgalactosamine for glycoproteins, sulfatides and cerebrosides.
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.
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.-.
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)
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.
The rate dynamics in chemical or physical systems.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A glycoside hydrolase found primarily in PLANTS and YEASTS. It has specificity for beta-D-fructofuranosides such as SUCROSE.
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.-.
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.
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).
Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.
SUGARS containing an amino group. GLYCOSYLATION of other compounds with these amino sugars results in AMINOGLYCOSIDES.
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.
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.
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.
A lipophilic glycosyl carrier of the monosaccharide mannose in the biosynthesis of oligosaccharide phospholipids and glycoproteins.
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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
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.
An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC
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)
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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).)
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)
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 used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
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.
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.
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.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
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; EC; EC; EC
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.
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 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.
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.
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.
Sites on an antigen that interact with specific antibodies.
Antibodies produced by a single clone of cells.
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.
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.
These compounds function as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. Include the pyrophosphates.
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.
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.
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.
Proteins found in any species of virus.
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.
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.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
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
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Compounds functioning as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. They include the polyisoprenyl pyrophosphates.
Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
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.
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.
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.
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)
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.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
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.
Incorporation of biotinyl groups into molecules.
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.
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.
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.
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.
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 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.
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)

TY - JOUR. T1 - NIST interlaboratory study on glycosylation analysis of monoclonal antibodies. T2 - comparison of results from diverse analytical methods. AU - De Leoz, Maria Lorna A.. AU - Duewer, David L.. AU - Fung, Adam. AU - Liu, Lily. AU - Yau, Hoi Kei. AU - Potter, Oscar. AU - Staples, Gregory O.. AU - Furuki, Kenichiro. AU - Frenkel, Ruth. AU - Hu, Yunli. AU - Sosic, Zoran. AU - Zhang, Peiqing. AU - Altmann, Friedrich. AU - Grünwald-Grube, Clemens. AU - Shao, Chun. AU - Zaia, Joseph. AU - Evers, Waltraud. AU - Pengelley, Stuart. AU - Suckau, Detlev. AU - Wiechmann, Anja. AU - Resemann, Anja. AU - Jabs, Wolfgang. AU - Beck, Alain. AU - Froehlich, John W.. AU - Huang, Chuncui. AU - Li, Yan. AU - Liu, Yaming. AU - Sun, Shiwei. AU - Wang, Yaojun. AU - Seo, Youngsuk. AU - An, Hyun Joo. AU - Reichardt, Niels Christian. AU - Ruiz, Juan Echevarria. AU - Archer-Hartmann, Stephanie. AU - Azadi, Parastoo. AU - Bell, Len. AU - Lakos, Zsuzsanna. AU - An, Yanming. AU - Cipollo, John F.. AU - ...
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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The site-specific glycosylation of soluble recombinant variants of human and rat CD4 (sCD4) expressed in Chinese hamster ovary (CHO) cells has been characterized. The presence of identical oligosaccharides at the conserved glycosylation site in domain 3 of rat and human sCD4 and the greater abundance of oligomannose and hybrid type glycans at the non-conserved glycosylation site of rat sCD4 clearly indicate that the protein structure influences oligosaccharide processing. Comparisons of rat sCD4 glycopeptides with mutant molecules with only single glycosylation sites and with a truncated form containing only the two NH2-terminal domains, indicate that independent processing occurs at each glycosylation site and that domain interactions can also affect oligosaccharide processing. These and other analyses of sCD2 expressed in CHO cells and Thy-1 purified from various tissues suggest that the diversity of oligosaccharide structures on a protein is regulated by the location of the glycosylation sites and
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.
Glycosylation in S2 cells is very similar to that of SF9, Sf21, and High Five cells. The nature of Drosophila N-linked glycosylation is less complex than mammalian glycosylation - it is generally of the paucimannose type and is not trimmed and sialylated.. O-linked glycosylation is similar, although not identical, to that obtained in mammalian cells. However, human glycosylation profiles are difficult to obtain, also glycosylation from CHO and HEK293 differ from human glycosylation. Human O-glycosylation can be divided into N-acetylGalactosamine linked (mucin type), N-acetylGlucosamine lined (O-GlcNAc type) and xylose linked (proteoglycans) families. The most abundant form is the mucin type, while O-GlcNac has only been found for cytoplasmic and nuclear proteins, the proteoglycans are of less interest here.. In CHO cells, O-glycosylation results in terminally sialated mucin type glycans, with a low percentage core-1 structure (T-antigen) reported. In Drosophila S2, cell O-glycosylation is less ...
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.. ...
Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time. The sTFR (residues 121−760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727). Although fully glycosylated sTFR is secreted into the tissue culture medium (∼40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor. Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor. Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant. The effect of glycosylation on binding to diferric human transferrin (Fe_2 hTF), an authentic monoferric hTF with iron in the C-lobe ...
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 ...
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 ...
In this study, we examined the potential N-glycosylation sites of RCL, and then discussed the functional significance of N-glycosylation on its secretion and enzymatic properties. RCL has four potential glycosylation sites in its gene sequence, three of which lie in the prosequence and the fourth of which is in the mature sequence (Figure 1B). Although the potential N-glycosylation sites of a protein can be predicted from the consensus sequence Asn-Xaa-Ser/Thr, not all such sites are fully occupied [33]. When RCL was expressed in P. pastoris, its N-terminal was truncated by Kex2. Thus, the three potential glycosylation sites in its prosequence were removed and only one glycosylation site at N-263 was retained in the truncated lipase r27RCLC (Figure 1). Enzymatic deglycosylation, which removed both high-mannose, hybrid-and complex-type N-linked glycans, was performed using glycosidases to investigate whether the potential glycosylation sites were glycosylated or not [3]. Endo Hf cleaved within ...
TY - JOUR. T1 - Nutritional therapies in congenital disorders of glycosylation (CDG). AU - Witters, Peter. AU - Cassiman, David. AU - Morava-Kozicz, Eva. PY - 2017/11/1. Y1 - 2017/11/1. N2 - Congenital disorders of glycosylation (CDG) are a group of more than 130 inborn errors of metabolism affecting N-linked, O-linked protein and lipid-linked glycosylation. The phenotype in CDG patients includes frequent liver involvement, especially the disorders belonging to the N-linked protein glycosylation group. There are only a few treatable CDG. Mannose-Phosphate Isomerase (MPI)-CDG was the first treatable CDG by high dose mannose supplements. Recently, with the successful use of D-galactose in Phosphoglucomutase 1 (PGM1)-CDG, other CDG types have been trialed on galactose and with an increasing number of potential nutritional therapies. Current mini review focuses on therapies in glycosylation disorders affecting liver function and dietary intervention in general in N-linked glycosylation disorders. We ...
Looking for online definition of protein glycosylation in the Medical Dictionary? protein glycosylation explanation free. What is protein glycosylation? Meaning of protein glycosylation medical term. What does protein glycosylation mean?
In the field of biochemistry, O-linked glycosylation is the attachment of a sugar molecule to an oxygen atom in an amino acid residue in a protein. O-linked glycosylation is a form of glycosylation that occurs in the Golgi apparatus in eukaryotes. It also occurs in archaea and bacteria. O-linked glycosylation occurs at a later stage during protein processing, probably in the Golgi apparatus. This is the addition of N-acetyl-galactosamine to serine or threonine residues by the enzyme UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (EC number, followed by other carbohydrates (such as galactose and sialic acid). This process is important for certain types of proteins such as proteoglycans, which involves the addition of glycosaminoglycan chains to an initially unglycosylated proteoglycan core protein. These additions are usually serine O-linked glycoproteins, which seem to have one of two main functions. One function involves secretion to form components of ...
Advanced Glycosylation End Products: 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.
Highlights: •Down-regulating FUT9 and ST3Gal4 expression blocks L1-induced neuronal differentiation of ESCs. •Up-regulating FUT9 and ST3Gal4 expression in L1-ESCs depends on the activation of PLCγ. •L1 promotes ESCs to differentiate into neuron through regulating cell surface glycosylation. -- Abstract: Cell recognition molecule L1 (CD171) plays an important role in neuronal survival, migration, differentiation, neurite outgrowth, myelination, synaptic plasticity and regeneration after injury. Our previous study has demonstrated that overexpressing L1 enhances cell survival and proliferation of mouse embryonic stem cells (ESCs) through promoting the expression of FUT9 and ST3Gal4, which upregulates cell surface sialylation and fucosylation. In the present study, we examined whether sialylation and fucosylation are involved in ESC differentiation through L1 signaling. RNA interference analysis showed that L1 enhanced differentiation of ESCs into neurons through the upregulation of FUT9 and ...
TY - JOUR. T1 - Nonenzymatic glycosylation and the pathogenesis of diabetic complications. AU - Brownlee, M.. AU - Vlassara, H.. AU - Cerami, A.. PY - 1984. Y1 - 1984. N2 - Glucose chemically attaches to proteins and nucleic acids without the aid of enzymes. Initially, chemically reversible Schiff base and Amadori product adducts form in proportion to glucose concentration. Equilibrium is reached after several weeks, however, and further accumulation of these early nonenzymatic glycosylation products does not continue beyond that time. Subsequent reactions of the Amadori product slowly give rise to nonequilibrium advanced glycosylation end-products which continue to accumulate indefinitely on longer-lived molecules. Excessive formation of both types of nonenzymatic glycosylation product appears to be the common biochemical link between chronic hyperglycemia and a number of pathophysiologic processes potentially involved in the development of long-term diabetic complications. The major biological ...
The N-linked glycosylation in recombinant monoclonal antibodies (mAb) occurs at Asn297 on the Fc region in the CH2 domain. Glycosylation heterogeneities have been well documented to affect biological activities such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) through their interaction with Fc-receptors. Hence, it is critical to monitor and characterize the N-linked glycosylation profile in a therapeutic protein such as a mAb for product consistency. In one approach, the glycans are first released from the mAb using an enzyme specific digestion, such as Protein N-Glycosidase F (PNGase) and subsequently they are labeled using a fluorophore, for example, 8-aminopyrene-1,3,6-trisulfonic acid (APTS) . Here we have applied this approach and used Capillary Electrophoresis with Laser-Induced Fluorescence detection (CE-LIF) to analyze a recombinant mAb produced in murine myeloma (NS0) cells. The technique provides short analysis times, efficient separations, and
Congenital disorder of glycosylation type 2A (CDG 2A) is a part of a group of rare inherited conditions that are present at birth (congenital) and involve defects in the glycosylation process. Glycosylation involves the joining of sugars and proteins (to form glycoproteins) by enzymes (proteins that function to convert specific substances in the body) in the cells of our bodies. These sugars (glycans) must be properly attached to specific proteins in the cells in order for the cells to function correctly. Due to the many functions of these glycoproteins throughout the body, if an error occurs in one of the many steps of the process, a wide variety of health problems may occur beginning in infancy. Symptoms can include psychomotor delays (movement, coordination, dexterity), mental retardation, and distinct physical features including thin lips, large gums, low-set rotated ears, and small head circumference. Some affected individuals may have gastrointestinal problems like diarrhea and reflux. ...
The interactions of B7-1 with CD28 and CTLA-4 modulate the course of human immune responses, making B7-1 an important target for developing structure-based therapeutics. B7-1 is, however, one of the most heavily glycosylated proteins found at the leukocyte cell surface, complicating the structural analysis of this molecule. Methods for the production, crystallization and selenomethionine labelling of a soluble deglycosylated form of this molecule are described. The protein readily forms both tetragonal plate and bipyramidal crystals belonging to space groups I4(1)22, with unit-cell parameters a = b = 56.9, c = 298.7 A, and P4(1)22 (or P4(3)22), with unit-cell parameters a = b = 89.0, c = 261.9 A, respectively. The I4(1)22 and primitive crystal forms diffract to 2.7 and 3.5 A, respectively. Surface plasmon resonance-based assays indicate that the ligand-binding properties of sB7-1 are unaffected by deglycosylation. Since none of the methods relied on any special structural properties of sB7-1, it is
Protein instability remains the main factor limiting the development of protein therapeutics. The fragile nature (structurally and chemically) of proteins makes them susceptible to detrimental events during processing, storage, and delivery. To overcome this, proteins are often formulated in the solid-state which combines superior stability properties with reduced operational costs. Nevertheless, solid protein pharmaceuticals can also suffer from instability problems due to moisture sorption. Chemical protein glycosylation has evolved into an important tool to overcome several instability issues associated with proteins. Herein, we employed chemical glycosylation to stabilize a solid-state protein formulation against moisture-induced deterioration in the lyophilized state. First, we investigated the consequences of moisture sorption on the stability and structural conformation of the model enzyme α-chymotrypsin (α-CT) under controlled humidity conditions. Results showed that α-CT aggregates and
View Notes - Glycobiology_Course_lesson_4_diagnostics from WE BIBI000000 at Ghent University. Glycobiology Course IV Clinical diagnostics based on glycosylation Roland Contreras Nico Callewaert
TY - JOUR. T1 - Migration of keratinocytes is impaired on glycated collagen I. AU - Morita, Keisuke. AU - Urabe, Kazunori. AU - Moroi, Yoichi. AU - Koga, Tetsuya. AU - Nagai, Ryuji. AU - Horiuchi, Seiko. AU - Furue, Masutaka. PY - 2005/1. Y1 - 2005/1. N2 - Advanced glycation end products are the chemical modification of proteins induced by sugars in a hyperglycemic condition. Extracellular matrix proteins are prominent targets of nonenzymatic glycation because of their slow turnover rates. The aim of this study was to investigate the influence of nonenzymatic glycation of type I collagen on the migration of keratinocytes. The migration of keratinocytes was dramatically promoted on native type I collagen-coated dishes compared with that on uncoated dishes. When type collagen was glycated with glycolaldehyde, large amounts of advanced glycation end products were produced; the glycated collagen I-coated dishes did not promote the migration of keratinocytes. Glycated collagen I did not affect the ...
Looking for online definition of glycosylation in the Medical Dictionary? glycosylation explanation free. What is glycosylation? Meaning of glycosylation medical term. What does glycosylation mean?
The primary hypothesis in this study is that adding simple milk sugar (galactose) to the diet of Congenital Disorders of Glycosylation patients will normalize the metabolic abnormalities. The secondary hypothesis posits that galactose intervention in Congenital Disorders of Glycosylation patients will normalize specific physiological biomarkers of protein glycosylation that can be utilized for future phase II/III trial development. The knowledge gained from the investigation of these two aims will help the investigators learn more about the disrupted metabolic mechanism of this disease and should lead to the identification of new disease biomarkers that can be used to evaluate clinical efficacy in future therapeutic trials.. Over a two-year period, the investigators will enroll patients diagnosed with Congenital Disorders of Glycosylation. The investigators propose to administer oral galactose supplementation for a period of 18 weeks in increasing dose to assess its effectiveness at normalizing ...
Human immunodeficiency virus type 1 (HIV-1) enters cells through the chemokine receptors CCR5 (R5 virus) and/or CXCR4 (X4 virus). Loss of N-linked glycans and increased net charge of the third variable loop (V3) of the gp120 envelope glycoprotein have been observed to be important steps towards CXCR4 use. All reported sequences using CCR5 or CXCR4 exclusively, or using both, were gathered from the Los Alamos HIV Database and analysed with regard to the V3 N-linked glycosylation motifs (sequons) and charge. The V3 loop glycan had a sensitivity of 0·98 and a 0·92 positive predictive value in the context of CCR5 use. The difference from X4 was remarkable (P<10−12). Especially, the sequon motif NNT within the V3 loop was conserved in 99·2 % of the major clades. The results suggest a close association between the V3 loop glycan and CCR5 use and may provide new insight into HIV-1 tropism and help to improve phenotype-prediction models.
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Glycosyl ortho-alkynylbenzoates have emerged as a new generation of donors for glycosidation under the catalysis of gold(I) complexes such as Ph3PAuOTf and Ph3PAuNTf2 (Tf= trifluoromethanesulfonate). A wide variety of these donors, including 2-deoxy sugar and sialyl donors, are easily prepared and shelf stable. The glycosidic coupling yields with alcohols are generally excellent; even direct coupling with the poorly nucleophilic amides gives satisfactory yields. Moreover, excellent alpha-selective glycosylation with a 2-deoxy sugar donor and beta-selective sialylation have been realized. Application of the present glycosylation protocol in the efficient synthesis of a cyclic triterpene tetrasaccharide have further demonstrated the versatility and efficacy of this new method, in that a novel chemoselective glycosylation of the carboxylic acid and a new one-pot sequential glycosylation sequence have been implemented ...
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In this work different horseradish transformed lines (tumour and teratoma) were compared with control samples of leaf tissue in electrophoretic pattern of total cell proteins and their glycosylation. Emphasis was put on the comparison of these tissues in structure and composition of N-glycans of endoplasmic reticulum proteins. Despite its central metabolic role, the endoplasmic reticulum is also a starting point of protein glycosylation in eukaryotic cells. Two forms of protein glycosylation are known, N- and Oglycosylation. N-glycosylation is a major modification of proteins in plant cells. Plant N-glycans can be classified into four basic groups: high-mannose-type, complex-type, paucimannosidic-type and hybrid-type. N-glycosylation is a well described process whereas O-glycosylatin is not well characterized. Glycoproteins were separated on SDS-PAGE and subsequently transferred onto nitrocellulose membrane. Glycosylated proteins were detected with Con A. N-glycans were further characterized by ...
article{04b8831a-870b-4baa-b2ba-da9ecd197697, abstract = {Activated Factor V (FVa) functions as a membrane-bound cofactor to the enzyme factor Xa (FXa) in the conversion of prothrombin to thrombin, increasing the catalytic efficiency of FXa by several orders of magnitude. To map regions on FVa that are important for binding of FXa, site-directed mutagenesis resulting in novel potential glycosylation sites on FV was used as strategy. The consensus sequence for N-linked glycosylation was introduced at sites, which according to a computer model of the A-domains of FVa, were located at the surface of FV. In total, thirteen different regions on the FVa surface were probed, including sites that are homologous to FIXa-binding sites on FVIII. The interaction between the FVa variants and FXa and prothrombin were studied in a functional prothrombin activation assay, as well as in a direct binding assay between FVa and FXa. In both assays, the four mutants carrying a carbohydrate side chain at position ...
Samples can be sent for analysis by post or courier. Glycosylation is a stable modification and even in case of protein degradation, the corresponding glycoprofile can be determined. Depending on the analysis required, the proteins can be delivered at room temperature as lyophilised or precipitated samples, or on dry/wet ice when in solution. The results will be reported and discussed online, meaning no personal travel is required.. Analysis includes:. • Intact glycoprotein mass will be determined by MALDI TOF analysis using ultrafleXtreme MALDI TOF/TOF instrument (Bruker). The level of glycosylation can be estimated by comparison of the intact glycoprotein with its deglycosylated form.. • Analysis of N-glycoprofile includes protein denaturation, deglycosylation, isolation of released glycans with subsequent permethylation and analysis by MALDI TOF/TOF mass spectrometry (ultrafleXtreme, Bruker).. • The protein glycosylation sites will be determined by proteolytic cleavage, heavy atom ...
A glycosyl donor is a carbohydrate mono- or oligosaccharide that will react with a suitable glycosyl acceptor to form a new glycosidic bond. By convention, the donor is the member of this pair that contains the resulting anomeric carbon of the new glycosidic bond. The resulting reaction is referred to as a glycosylation or chemical glycosylation. In a glycosyl donor, a leaving group is required at the anomeric position. The simplest leaving group is the OH group that is naturally present in monosaccharides, but it requires activation by acid catalysis in order to function as leaving group (in the Fischer glycosylation). More effective leaving groups are in general used in the glycosyl donors employed in chemical synthesis of glycosides. Typical leaving groups are halides, thioalkyl groups, or imidates, but acetate, phosphate, and O-pentenyl groups are also employed. Natural glycosyl donors contain phosphates as leaving groups. The so-called armed-disarmed principle The concept of armed and ...
The selectin family of cell adhesion molecules mediates the tethering and rolling of leukocytes on blood vessel endothelium. It has been postulated that the molecular basis of this highly dynamic adhesion is the low affinity and rapid kinetics of selectin interactions. However, affinity and kinetic analyses of monomeric selectins binding their natural ligands have not previously been reported. Leukocyte selectin (L-selectin, CD62L) binds preferentially to O-linked carbohydrates present on a small number of mucin-like glycoproteins, such as glycosylation-dependent cell adhesion molecule-1 (GlyCAM-1), expressed in high endothelial venules. GlyCAM-1 is a soluble secreted protein which, following binding to CD62L, stimulates beta2-integrin-mediated adhesion of lymphocytes. Using surface plasmon resonance, we show that a soluble monomeric form of CD62L binds to purified immobilized GlyCAM-1 with a dissociation constant (Kd) of 108 microM. CD62L dissociates from GlyCAM-1 with a very fast dissociation rate
The hexosamine biosynthetic pathway, whose end product is UDP-N acetylglucosamine (UDP-GlcNAc), lies at the base of cellular glycosylation pathways, including glycosylation of lipids, formation of heparin sulfated proteoglycans, and N- and O-linked glycosylation of proteins. Forward genetic studies in Drosophila have revealed that mutations in genes encoding different enzymes of the hexosamine biosynthetic pathway result in reduction of UDP-GlcNAc to different extents, with a consequent disruption of distinct glycosylation pathways and developmental processes. A maternal and zygotic loss-of-function screen has identified mutations in nesthocker (nst), which encodes an enzyme in the hexosamine biosynthetic pathway. Embryos lacking maternal and zygotic nst gene products show defective O-GlcNAcylation of a fibroblast growth factor receptor (FGFR)-specific adaptor protein, which impairs FGFR-dependent migration of mesodermal and tracheal cells.. ...
The current study highlights a novel glycosylation-dependent mechanism that confers gemcitabine resistance by preventing DNA damage. Experimental procedures Cell culture MiaPaCa-2 and BxPC-3 cell lines were obtained from ATCC. increased gemcitabine sensitivity ratio, an indication of gemcitabine toxicity. Gemcitabine-resistant MiaPaCa-2 cells display higher ST6Gal-I levels than treatment-na?ve WEHI-9625 cells along with a reduced gemcitabine sensitivity ratio, suggesting that WEHI-9625 chronic chemotherapy selects for clonal variants with more abundant ST6Gal-I. Finally, we examined Suit2 PDAC cells and Suit2 derivatives with enhanced metastatic potential. Intriguingly, three metastatic and chemoresistant subclones, S2-CP9, S2-LM7AA, and S2-013, exhibit up-regulated ST6Gal-I relative to parental Suit2 cells. ST6Gal-I KD in S2-013 cells increases gemcitabine-mediated DNA damage, indicating that suppressing ST6Gal-I activity sensitizes inherently resistant cells to gemcitabine. Together, these ...
TY - JOUR. T1 - N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL. AU - van Sorge, N.M.. AU - Bleumink, N.M.C.. AU - van Vliet, S.J.. AU - Saeland, E.. AU - van der Pol, W.L.. AU - van Kooyk, Y.. AU - van Putten, J.W.. PY - 2009. Y1 - 2009. U2 - 10.1111/j.1462-5822.2009.01370.x. DO - 10.1111/j.1462-5822.2009.01370.x. M3 - Article. C2 - 19681908. VL - 11. SP - 1768. EP - 1781. JO - Cellular Microbiology. JF - Cellular Microbiology. SN - 1462-5814. IS - 12. ER - ...
The addition of specific monosaccharides to the oligosaccharide can mask the special sequence and prevent its recognition by microbial toxins or antibodies. Intracellular targeting of proteins may also depend on the glycan structure associated with the protein as was demonstrated for lyosomal enzymes. 5). Expression of specific types of glycosylation on different glycoconjugates in different tissues at different times during development imply that these structures have diverse roles in the same organism. Further, each potential glycosylation site in a given glycoprotein population is fully, partially, or not at all occupied. In fact, an eukaryotic glycoprotein is not isolated as a single structural entity, but rather as a set of glycosylated variants of a common polypeptide, which are referred to as glycoforms [11, 13]. The particular glycosylation pattern of a protein is not random and uncontrolled and reflects the balance of all activities of that glycoprotein in a particular physiological ...
Berg, Tore Julsrud; Dahl-Jørgensen, Knut; Torjesen, Peter A.; Bucala, Richard & Hanssen, Kristian Folkvord (1996). Increased serum levels of Advanced glycosylation end products (AGEs) in children and adolescents with IDDM. Show summary Increased Serum levels of Advanced Glycosylation End products (AGEs) in Children and Adolescents with IDDM. TORE J. BERG, KNUT DAHL-JØRGENSEN*, PETER A. TORJESEN, RICK BUCALA*4, KRISTIAN F. HANSSEN, Oslo, Norway and Manhasset, NY.We have developed a sandwich fluoremetric-immunoassay for measuring AGEs in serum utilizing polyclonal antibodies made from rabbit immunized with AGE-RNase. Using this assay we have earlier shown that AGEs in serum predict the progression of morphological pathology in the kidney of diabetic patients with microalbuminuria. In the present study we aimed to investigate whether the serum levels of AGEs in a cohort of diabetic adolescent patients were different from normal subjects. IDDM patients (n=69) were compared with healthy ...
糖腎病是一種常見的慢性糖尿病併發症,也是造成末期腎臟衰竭的原因之一,伴隨的尿毒症狀更是讓洗腎人口數向上攀升。約有20-30%的糖尿病患者會發展成糖腎病,其中第一型糖尿病在10-15年內會演變成糖腎病,並具有50%的機會進展到末期腎病變;而第二型糖尿病則有20%-40%的糖腎病進程,然而20年後僅有20%的機率形成末期腎病變。根據美國腎臟資料系統的末期腎臟病年報中顯示,台灣糖腎病患者的盛行率位居世界第二,發生率則居全球之冠,在國人十大死因裡更是排名第五,為此研發出延緩或改善糖尿病腎病變的治療方法是極其迫切的議題。 糖尿病患者體內的高血糖環境會促進最終糖化蛋白的合成 (Advanced Glycosylation End Products, AGEs) ,進而引發體內細胞產生有害的活性氧物 (Reactive oxygen species, ROS) 以及釋放促發炎因子,造成內皮細胞受損並吸引巨噬細胞前來浸潤
Results We discovered that ACPA-IgG from RA patients have a higher apparent molecular weight as compared to other IgG molecules including antibodies against recall antigens and other autoantibodies. This higher molecular weight was explained by the overrepresentation of N-linked glycans in the variable domain (Fab region) of ACPA-IgG. Detailed structural analysis of these glycans demonstrated that ACPA-IgG linked Fab glycans are complex-type biantennary N-glycans that differ from the conventional Fc-linked N-glycans by a high degree of sialylation, galactosylation, and fucosylation together with the presence of bisecting N-acetylglucosamine. Using recombinant ACPA-IgG monoclonal antibodies with and without Fab-glycans, we found that Fab-glycans modulate binding affinity of ACPA-IgG for citrullinated antigens. Finally, lectin-immunoblotting showed that ACPA Fab-glycans can bind to sialic acid-binding immunoglobulin-type lectins.. ...
Most subtypes of CDG are classified as disorders of N-glycosylation, which involves carbohydrates called N-linked oligosaccharides. These oligosaccharides are created in a specific order to create specific sugar trees, which are then attached to proteins on various cells. Disorders of N-glycosylation are due to an enzyme deficiency or other malfunction somewhere along the N-glycosylation pathway.. As long as the defect is not identified, disorders of N-glycosylation are subdivided into defects of oligosaccharide assembly and transfer (CDG-Ix) and defects in oligosaccharide trimming and processing that occur after they are bound to proteins (CDG-IIx). As soon as the defect in an individual patient is clarified, a CDG name is given according to the current nomenclature.. Disorders of N-glycosylation include:. PMM2-CDG - This disorder is the most common type of CDG. More than 700 individuals have been identified. The disorder can be broken down into three stages: infantile multisystem, ...
To determine whether the N-terminal hydrophobic sequence is also responsible for retention, the N-terminal 29 amino acids of cytochrome P450 2C1, with and without an additional 29 amino acids containing an N-glycosylation site, were fused to a soluble cytoplasmic protein, Escherichia coli $\beta$-galactosidase, or to a secreted protein, Escherichia coli alkaline phosphatase, and the hybrid proteins were expressed in COS1 cells and cellular localization was determined by subcellular fractionation, immunolocalization and the glycosylation state of the proteins. Both the $\beta$-galactosidase and alkaline phosphatase hybrid proteins were retained in the endoplasmic reticulum establishing that a specific sequence or property in the N-terminal 29 amino acids is responsible for ER retention. To further examine the possibility that retention of proteins with a large cytoplasmic domain is the default pathway, the cellular distributions of a series of P450 2C1 and EGFR chimeric proteins were examined. ...
Autor: Guillard, Mailys et al.; Genre: Zeitschriftenartikel; Im Druck veröffentlicht: 2009-09; Keywords: Glycosylation; Cutis laxa; V-ATPase; Congenital disorders of glycosylation; OMIM 219200; Apolipoprotein C III; Titel: Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa
TY - JOUR. T1 - Role of glycosylation in the H-2-restricted cytolysis of virus-infected cells. AU - Black, P. L.. AU - Vitetta, E. S.. AU - Forman, J.. AU - Kang, C. Y.. AU - May, R. D.. AU - Uhr, J. W.. PY - 1981. Y1 - 1981. N2 - The role of the oligosaccharide portions of cell surface glycoproteins in the susceptibility of virus-infected cells to H-2-restricted cytolysis was investigated by using the antibiotic tunicamycin (TM). TM inhibits the addition of sugars to the polypeptides of glycoproteins. TM treatment of P 815 cells before and during infection with vesicular stomatitis virus (VSV) inhibited glycosylation of proteins and reduced by about 50% the lysis of infected P 815 cells by VSV-immune, H-2-identical killer cells. In contrast, TM treatment had a modest inhibitory effect on cytolysis of P 815 cells by alloimmune effector cells. TM treatment did not inhibit the surface expression of either H-2 or VSV glycoprotein. Thus, glycosylation of H-2 and/or viral glycoprotein is a ...
C-type lectins are important molecules of the innate immune system. These molecules, like surfactant protein D (SP-D) can recognize glycans on pathogens and neutralize these. Also influenza viruses are recognized by SP-D and their susceptibility to neutralization by SP-D is dependent on the number of N-linked glycosylation sites in the hemagglutinin in particular. Porcine SP-D displayed stronger neutralizing activity to human influenza A viruses than to swine influenza A viruses. Although viruses from these species differ with regard to the number of glycosylation sites in the hemagglutinin, the mechanism underlying the differential recognition by porcine SP-D is poorly understood. Here we investigated the molecular basis for the differential recognition of a seasonal H1N1 and a 2009 pandemic H1N1 virus by porcine SP-D. We demonstrated that the number and position of glycosylation sites determine viral susceptibility to the neutralizing activity of porcine SP-D. However, predicting the effect ...
TY - JOUR. T1 - Killing of Trypanosoma brucei by Concanavalin A. T2 - Structural basis of resistance in glycosylation mutants. AU - Acosta-Serrano, Alvaro. AU - Cole, Robert N. AU - Englund, Paul T.. PY - 2000/12/8. Y1 - 2000/12/8. N2 - Concanavalin A (Con A) kills procyclic (insect) forms of Trypanosoma brucei by binding to N-glycans on EP-procyclin, a major surface glycosyl phosphatidylinositol (GPI)-anchored protein which is rich in Glu-Pro repeats. We have previously isolated and studied two procyclic mutants (ConA 1-1 and ConA 4-1) that are more resistant than wild-type (WT) to Con A killing. Although both mutants express the same altered oligosaccharides compared to WT cells, ConA 4-1 is considerably more resistant to lectin killing than is ConA 1-1. Thus, we looked for other alterations to account for the differences in sensitivity. Using mass spectrometry, together with chemical and enzymatic treatments, we found that both mutants express types of EP-procyclin that are either poorly ...
BACKGROUND: Mesangial IgA1 deposition is characteristic of IgA nephropathy (IgAN). Structural abnormalities of the IgA1 glycoprotein may play a key role in its mesangial deposition, particularly the recently described abnormalities of O-glycosylation of the IgA1 hinge region. The mechanism of abnormal O-glycosylation has not yet been elucidated; it is not clear whether there is an alteration in the amino acid sequence of the hinge region, modifying the number of O-glycosylation sites available, or whether there is a post-translational defect in the glycosylation process. METHODS: The O-glycosylation of serum IgA1 from a series of patients with IgAN and matched controls was assessed by lectin binding assay. We then used dideoxy-sequencing of the PCR-amplified hinge region of the alpha1 heavy chain gene to compare the hinge region nucleotide sequence in IgAN and controls. We also compared cDNA transcripts of alpha1 hinge region mRNA to look for evidence for a transcriptional abnormality in IgAN. ...
I have a recombinant protein produced in the yeast Pichia pastoris that is partially glycosylated with O-linked sugar (it must be O-linked - there are no N-linked sites). I wish to remove the glycosylated protein from the non-glycosylated. I have tried using ConA-Sepharose (Pharmacia) and Glycine-Max (Sigma). Neither of these has appeared to bind. The ConA comes with instructions that have been followed. No instructions could be found for Gycine-MAx and Sigma were not forthcoming. Has anyone has experience with trying to purify O-linked sugars, with either of the above lectins, or using any other reagents, I would very much like to hear from you. Please reply to me by e-mail as I do not regularly read this newsgroup. Tim -- Tim Dudgeon British Biotech Phone: 0865 748747 FAX: 0865 717598 email: dudgeon at ...
N-glycans or asparagine-linked glycans are major constituents of glycoproteins in eukaryotes. N-glycans are covalently attached to asparagine with the consensus sequence of Asn-X-Ser/Thr by an N-glycosidic bond, GlcNAc b1- Asn. Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol. After sequential addition of monosaccharides by ALG glycosyltransferases [MD:M00055], the N-glycan precursor is attached by the OST (oligosaccharyltransferase) complex to the polypeptide chain that is being synthesized and translocated through the ER membrane. The protein-bound N-glycan precursor is subsequently trimmed, extended, and modified in the ER and Golgi by a complex series of reactions catalyzed by membrane-bound glycosidases and glycosyltransferases. N-glycans thus synthesized are classified into three types: high-mannose type, complex type, and hybrid type. ...
Should you be thinking more about glycosylation? Glycosylation, which is the addition of carbohydrates to proteins or other molecules, plays a huge part in protein folding, protein stability, cell adhesion, cellular function and protection, recognition of self, pathogen invasion, and much more. From bacteria to yeast to mammals, it happens everywhere and it happens a lot. Yet in the light of biological research, it is often overlooked or even disregarded. This blog discusses a few of the many important roles for glycosylation in biology.
Traumatic spinal cord injury (SCI) results in disruption of tissue integrity leading to a loss of function. There has been minimal success in treating these injuries clinically, due to the inhibitory environment which develops over time. In this work, we study the glycosylation response to SCI in two models: Xenopus laevis is used to compare successful to failed regeneration, by comparing the response to injury pre- and post-metamorphosis, while we use a rat model to understand the pathophysiology of the injury and how this may be modified by treatment with an aligned collagen hydrogel. We hypothesise that glycosylation is altered in response to injury, that it has a role in determining the success of regeneration, and that biomaterial treatment can influence this glycosylation response. Complete transection was used to model SCI in pre- and post-metamorphic stages of Xenopus laevis and in adult rat. Collagen hydrogels with aligned or non-aligned fibres were placed at the transection site in the ...
To help the researchers and pharmaceutical partners with discovering the most effective therapeutic glycoprotein, Creative Biolabs provides solutions on glycosylation, the most widely applied posttranslational modification (PTM) approach to change protein function and measure the recombinant biopharmaceutical immunogenicity. Based upon the efficient glycoengineered expression platforms (glyco-engineered mammalian cell expression system, glyco-engineered pichia pastoris expression system, and glyco-engineered plant-based expression system), Creative Biolabs is fully competent to handle the requests of therapeutic glycoprotein development and glycoengineering of antibody/cell line.. Creative Biolabs has updated the generally applied mammalian cell expression with glyco-engineered Chinese hamster ovary (CHO) cells and glyco-engineered human embryonic kidney 293 (HEK293) cells for glycoprotein production, which can guarantee the natural folding and sugar chain composition of glycoprotein, and ...
IgG glycosylation is skewed toward proinflammatory G0 variants in healthy children, in particular during the first few years of life. This deviation is exaggerated in patients with JIA. The role for IgG glycan variation in immune function in children, including the predilection of JIA for early chil …
Sriram Neelamegham received grants to fund his research focused on developing a systems level understanding of cellular glycosylation processes, using a combination of mathematical modeling methods and experiments. Such work is important since glycans, or carbohydrates expressed on cells, either absolutely control or finely tune a number of biological processes in human during health and disease. The studies being pursued are thus important for biotechnology and medical research. Collaborators on the awards include Professor Jun Qu (Pharmaceutical Sciences), Michael Buck (Biochemistry), G. Ekin Atilla-Gokcumen (Chemistry) and Lara Mahal (Chemistry, New York University). ...
Sigma-Aldrich offers abstracts and full-text articles by [Erandi Lira-Navarrete, Matilde de Las Rivas, Ismael Compañón, María Carmen Pallarés, Yun Kong, Javier Iglesias-Fernández, Gonçalo J L Bernardes, Jesús M Peregrina, Carme Rovira, Pau Bernadó, Pierpaolo Bruscolini, Henrik Clausen, Anabel Lostao, Francisco Corzana, Ramon Hurtado-Guerrero].
CD24, also known as heat-stable antigen (HSA) in mice, is a small heavily glycosylated cell-surface protein that is linked to the membrane by a glycosyl-phosphatidylinositol (GPI-) anchor (Pierres et al., 1987; Kay et al., 1990; Alterman et al., 1990). Mouse CD24 has a protein core of 27 amino acids with seven potential glycosylation sites, whereas human CD24 consists of 31 amino acids with 16 potential O- and N-glycosylation sites. Owing to this extensive glycosylation, CD24 has mucin-like characteristics (reviewed by Kristiansen et al., 2004b).. CD24 is expressed in mouse hematopoietic cell subpopulations including B lymphocytes, the majority of thymocytes, erythrocytes and neutrophils. Because of its lineage-specific and developmentally regulated expression, CD24 was traditionally used as a differentiation marker for B- and T-cell ontogeny (Poncet et al., 1996; Egerton et al., 1990; Lu et al., 1998). Later studies revealed that CD24 is not exclusively expressed by hematopoietic cells but is ...
Freeze HH, Hart GW, Schnaar RL (2015). "Glycosylation Precursors". In Varki A, Cummings RD, Esko JD, Stanley P (eds.). ...
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): ...
Drake RR, Jones EE, Powers TW, Nyalwidhe JO (2015). "Altered glycosylation in prostate cancer". In Drake RR, Ball LE (eds.). ... Glycosylation and Cancer. Advances in Cancer Research Vol. 126. Vol. 126. pp. 345-82. doi:10.1016/bs.acr.2014.12.001. ISBN ...
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 ...
Dedera DA, Gu RL, Ratner L (March 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 ... Feizi T, Larkin M (September 1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID ... 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. doi:10.1128/jvi.63.6.2452-2456.1989. ...
Fluorine directed glycosylations represent an encouraging handle for both B selectivity and introduction of a non-natural ... In addition one of the most intriguing aspects thereof is the capability of O-glycosylation to extend half life, decrease ... The overall specificity of the glycosylation can be improved by utilizing approaches which take into account the relative ... The full mOR agonist pentapeptide DAMGO is also CNS penetrant upon introduction of glycosylation. DNA molecules contain 5- ...
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 ... GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview v t e (Genes on human chromosome, All stub ... Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17-23. doi:10.1093/glycob/1.1.17. PMID 2136376. Land A ...
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. PMID 19150496. "Ferritin: Reference Range ...
... hydroxylation on the P residues and subsequent glycosylation and in many cases addition of a GPI-anchor. Glycosylation of the ... These events occur prior to prolyl hydroxylation and glycosylation. The core glycan structure of GPI anchors is Man-α-1,2-Man-α ... Sequences that direct AG glycosylation (SO, TO, AO, VO) are called AGP glycomotifs. All AGP protein backbones contain a minimum ... Taken together, these studies provide evidence that proper glycosylation of AGPs is important to AGP function in plant growth ...
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". Archived from the original on 2004-03- ...
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 ...
"Congenital Disorders of Glycosylation". NORD (National Organization for Rare Disorders). Retrieved 2019-08-01. "Mito Info". ... Placental insufficiency Craniosynostosis Genetic Inborn errors of metabolism Congenital disorder of glycosylation Mitochondrial ...
To this end, paucimannosylation is therefore now considered to be a distinct type of N-glycosylation that adds diversity to the ... Recently, granule-specific glycosylation was shown in neutrophils featuring prominent paucimannosylation in the azurophilic ... Mortimer, Nathan T.; Kacsoh, Balint Z.; Keebaugh, Erin S.; Schlenke, Todd A. (2012-07-19). "Mgat1-dependent N-glycosylation of ... Recently, paucimannosylation was reported to form an unconventional type of protein N-glycosylation in vertebrates. It has been ...
Mutations in the gene have been shown to cause defects in the protein glycosylation pathway which manifest as the congenital ... GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview GeneReviews/NIH/NCBI/UW entry on PMM2-CDG (CDG- ... Jaeken J, Matthijs G (2002). "Congenital disorders of glycosylation". Annual Review of Genomics and Human Genetics. 2: 129-51. ... Congenital Disorder of Glycosylation Type 1a; Jaeken Syndrome v t e (Articles with short description, Short description matches ...
Marth, Jamey David (2020). "Glycosylation in a Common Mechanism of Colitis and Sepsis". The FASEB Journal. 34 (S1): 1. doi: ... His research has largely focused on how protein glycosylation contributes to the origins of common diseases and syndromes ... Marth's early studies of glycosylation and glycan linkages revealed a profound effect on immunity and contributed to the ... Marth, J.D.; Grewal, P.K. (2008). "Mammalian glycosylation in immunity". Nat. Rev. Immunol. 8 (11): 874-887. doi:10.1038/ ...
Dong DL, Xu ZS, Chevrier MR, Cotter RJ, Cleveland DW, Hart GW (August 1993). "Glycosylation of mammalian neurofilaments. ...
Congenital disorder of glycosylation MPI-CDG EBI Database, IPRO16305 Mannose-6-phosphate Isomerase. "1pmi". PDBe. Gao H, Yu Y, ... GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview Mannose-6-Phosphate+Isomerase at the US ... Jaeken J, Matthijs G (2001). "Congenital disorders of glycosylation". Annual Review of Genomics and Human Genetics. 2: 129-51. ...
0-Beta-GlcNAc is presumably the only type of glycosylation occurring in the nucleus and/or cytoplasm of cells. There is a ... NetNGlyc predicted glycosylation sites; however, these sites were excluded because the protein is likely nuclear and would not ... undergo this form of glycosylation. There were no predicted acetylation sites at the N-terminus of the protein. This is unusual ... notable link between antigen activation by lymphocytes and dynamic 0-B-Glycosylation in nuclear proteins (Hart and Akimoto). ...
James N Arnold; Mark R Wormald; Robert B. Sim; Pauline M Rudd; Raymond A Dwek (1 January 2007). "The impact of glycosylation on ... Van den Steen P; Rudd PM; Dwek RA; Opdenakker G (1 January 1998). "Concepts and principles of O-linked glycosylation". Critical ... "Glycosylation and the immune system". Science. 291 (5512): 2370-2376. doi:10.1126/SCIENCE.291.5512.2370. ISSN 0036-8075. PMID ... where she developed new processes for protein glycosylation in an attempt to characterise recombinant protein drugs. Elected a ...
glucose to haemoglobin Chemical glycosylation Glycosyl halide Armed and disarmed saccharides Carbohydrate chemistry Van Der ... "Acceptor reactivity in glycosylation reactions". Chemical Society Reviews. 48 (17): 4688-4706. doi:10.1039/C8CS00369F. PMID ...
The most important of these to note are N-linked glycosylation and disulfide bond formation. N-linked glycosylation occurs as ... tunicamycin inhibits N-linked glycosylation. Dengue virus induces PERK dependent ER stress as part of virus induced response in ... targeting it for identification and re-glycosylation by the enzyme UGGT (UDP-glucose:glycoprotein glucosyltransferase). If this ...
His thesis was entitled Glycosylation in Mice and Rats. After graduation he helped establish the first commercially focused ... He conducted research on the structure-function relationships of glycosylation. These specific efforts focused on evolution, ... Dennis, Jim W; Granovsky, Maria; Warren, Charles E (1999). "Glycoprotein glycosylation and cancer progression". Biochim Biophys ... ". "Dr Jim Dennis". Dennis, Jim W; Granovsky, Maria; Warren, Charles E (1999). "Protein glycosylation in development and ...
Reily C, Stewart TJ, Renfrow MB, Novak J (June 2019). "Glycosylation in health and disease". Nature Reviews. Nephrology. 15 (6 ... 4-galactosyltransferase I causes the congenital disorder of glycosylation type IId". The Journal of Clinical Investigation. 109 ...
The two types of glycosylation events in the Golgi are N-linked glycosylation and O-linked glycosylation. Glycosylation of ... investigated glycosylation of serum proteins with individuals with WSS and found that they had defects in N-glycosylation at ... In order to retain the enzymes responsible for protein glycosylation in the correct regions of the Golgi, there must be ... "Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa." Biochimica et Biophysica Acta (BBA) - Molecular Basis of ...
1993). "Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on ...
2007). "Down-regulation of N-acetylglucosaminyltransferase-V induces ER stress by changing glycosylation and function of GLUT1 ... "Glycoprotein glycosylation and cancer progression". Biochim. Biophys. Acta. 1473 (1): 21-34. doi:10.1016/s0304-4165(99)00167-1 ... induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original ...
Initial glycosylation as assembly continues. This is N-linked (O-linking occurs in the Golgi). N-linked glycosylation: If the ...
... glycosylation is a site-specific modification. N-linked glycosylation is a very prevalent form of glycosylation and is ... disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No ... O-linked glycosylation is a form of glycosylation that occurs in eukaryotes in the Golgi apparatus, but also occurs in archaea ... Glycosylation can also module the thermodynamic and kinetic stability of the proteins. Glycosylation increases diversity in the ...
... also known as congenital disorder of glycosylation type Ia) is an inherited condition that affects many parts of the body. ... 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 ...
glycosylation Sorry, no results found.. We tried our best, but we couldnt find any articles relating to . ...
An Effective Approach for Glycan Structure De Novo Sequencing From HCD Spectra 556 235 Transactions on NanoBioscience (TNB) Transactions on NanoBioscience (TNB) // ...
IgA1 Glycosylation Is Heritable in Healthy Twins Hannah J. Lomax-Browne, Alessia Visconti, Charles D. Pusey, H. Terence Cook, ... O- and N-Glycosylation of Serum Immunoglobulin A is Associated with IgA Nephropathy and Glomerular Function Viktoria Dotz, ... On the Importance of Considering Glycosylation When Evaluating Biologic Therapies Mathieu Lemaire ...
Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains ... Development and application of mass spectrometric methods for the analysis of progranulin N-glycosylation J Proteomics. 2010 ... PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains. A ... In-gel tryptic digestion was further applied to the gel pieces containing deglycosylated protein, for N-glycosylation site ...
Re: Schmidt glycosylation problems « Reply #1 on: April 01, 2022, 02:16:24 AM » ... Re: Schmidt glycosylation problems « Reply #2 on: April 01, 2022, 11:02:00 AM » ... Re: Schmidt glycosylation problems « Reply #3 on: April 01, 2022, 02:53:23 PM » ... Re: Schmidt glycosylation problems « Reply #4 on: April 21, 2022, 08:47:32 AM » ...
Proteolytic processing of human host cell factor 1 (HCF-1) to its mature form was recently shown, unexpectedly, to occur in a UDP-GlcNAc-dependent fashion within the transferase active site of O-GlcNAc-transferase (OGT) (Lazarus, M. B., Jiang, J., Kapuria, V., Bhuiyan, T., Janetzko, J., Zandberg, W. F., Vocadlo, D. J., Herr, W., and Walker, S. (2013) Science 342, 1235-1239). An interesting mechanism involving formation and then intramolecular rearrangement of a covalent glycosyl ester adduct of the HCF-1 polypeptide was proposed to account for this unprecedented proteolytic activity. However, the key intermediate remained hypothetical. Here, using a model enzyme system for which the formation of a glycosyl ester within the enzyme active site has been shown unequivocally, we show that ester formation can indeed lead to proteolysis of the adjacent peptide bond, thereby providing substantive support for the mechanism of HCF-1 processing proposed.. ...
Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site ... Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. ... Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation ... Synthetic glycosylation of proteins using N-(beta-saccharide) iodoacetamides: applications in site-specific glycosylation and ...
Glycosylation of a model proto-RNA nucleobase with non-ribose sugars: implications for the prebiotic synthesis of nucleosides† ... Glycosylation of a model proto-RNA nucleobase with non-ribose sugars: implications for the prebiotic synthesis of nucleosides D ... were found to be β-pyranosides with the glycosylation site on TAP varying with sugar identity. Our results suggest that ...
Through site directed mutagenesis of N-glycosylation sites we have generated forms of SNS and Duf/Kirre lacking all N-glycans. ... Analysis of these mutants in S2 cell aggregation assays demonstrate a specific requirement for N-glycosylation of SNS in SNS- ... Roles of N-linked glycosylation in SNS-Duf/Kirre mediated cell-cell adhesion. ... Since rescue experiments using SNS N-glycosylation mutants show only mild defects, it is apparent that, although the presence ...
Protein glycosylation is a widespread post-translational modification. The first committed step to the lipid-linked glycan used ... N2 - Protein glycosylation is a widespread post-translational modification. The first committed step to the lipid-linked glycan ... AB - Protein glycosylation is a widespread post-translational modification. The first committed step to the lipid-linked glycan ... abstract = "Protein glycosylation is a widespread post-translational modification. The first committed step to the lipid-linked ...
FUT1 genetic variants impact protein glycosylation of porcine intestinal mucosa. Marianne O. Hesselager, Arun V. Everest-Dass, ... FUT1 genetic variants impact protein glycosylation of porcine intestinal mucosa. Glycobiology. 2016 Jun 7;26(6):607-622. https ... These results provide insight into the role of FUT1 on intestinal glycosylation, improve our understanding of how variation in ... These results provide insight into the role of FUT1 on intestinal glycosylation, improve our understanding of how variation in ...
Massive cancer cell death was observed in glycosylation deficient cancer cells, suggesting glycosylation of PD-L1 is required ... Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity. Presented at: Dimension of Time: From ... Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity. Presented at: Dimension of Time: From ... The essence of PD-L1 N192, N200 and N219 glycosylation suggests it antagonizes GSK3beta binding. In this regard, only non- ...
To probe the scope of DBDMH/TfOH-mediated 1,2-cis-glycosylation, perbenzylated galactosyl donor 12 [41] (Table 3, entries 1-4) ... Preactivation-based chemoselective glycosylations: A powerful strategy for oligosaccharide assembly Weizhun Yang, Bo Yang, ... 1,3-Dibromo-5,5-dimethylhydantoin as promoter for glycosylations using thioglycosides. * Fei-Fei Xu1,2, ... Table 2: 1,2-Trans-glycosylation activated by DBDMH with a variety of building blocks. ...
From Stereocontrolled Glycosylation to Early-Stage Automation: Adventures in Deoxy Sugar Oligosaccharide Synthesis. Clay ...
Comprehensive Characterization of Glycosylation Alterations in Alzheimers Disease ... 3.4M NIH grant funded over five years to study the comprehensive characterization of glycosylation alterations in Alzheimers ... Zivkovic and colleagues receive $3.4M NIH grant to study glycosylation alterations in Alzheimers Disease *September 27, 2018 ... Zivkovic and colleagues receive $3.4M NIH grant to study glycosylation alterations in Alzheimers Disease ...
Abstract 3351: Differential glycosylation of extracellular matrix specifically modulates lung cancer initiating cells subsets ... Our results suggest that differential collagen glycosylation could play an essential role in the creation of a niche favorable ... Differential glycosylation of extracellular matrix specifically modulates lung cancer initiating cells subsets. [abstract]. In ... The relevance of collagen glycosylation, a fundamental post-translational modification controlling several biological processes ...
Transferrin glycosylation in hypoxia Academic Article ...
"The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59." In Advances in Experimental Medicine and ... "The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59." Advances in Experimental Medicine and Biology ... The glycosylation of the complement regulatory protein, human erythrocyte CD59. Advances in Experimental Medicine and Biology, ...
Yang, S., Nikodem, D., Davidson, E. A., & Gowda, D. C. (1999). Glycosylation and proteolytic processing of 70 kDa C-terminal ... Yang, S, Nikodem, D, Davidson, EA & Gowda, DC 1999, Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant ... T1 - Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite ... Glycosylation and proteolytic processing of 70 kDa C-terminal recombinant polypeptides of Plasmodium falciparum merozoite ...
Congenital disorders of glycosylation (CDG) are a growing group of rare genetic disorders. The most common CDG is ... Congenital disorders of glycosylation (CDG) are a growing family of rare diseases that affect the synthesis and attachment of ... Congenital disorders of glycosylation (CDG) are a growing group of rare genetic disorders. The most common CDG is ... P Lipiński A Tylki-Szymańska 2021 Congenital disorders of glycosylation: what clinicians need to know? Front Pediatr 9 926 ...
It is concluded (i) that the glycosylation of AGP was not dependent on its genetic expression and (ii) that both the variants ... in relation to changes in glycosylation was studied in sera of patients with burn injury, media of cytokine-treated primary ...
autosomal recessive disease congenital disorder of glycosylation type II autosomal recessive disease congenital disorder of ... A congenital disorder of glycosylation type II that has_material_basis_in an autosomal recessive mutation of COG2 on chromosome ...
Congenital Disorders of Glycosylation (CDG) are a group of genetic diseases that are caused by defects in protein glycosylation ... A treatable Congenital Disorder of Glycosylation with no central nervous system involvement.. By: Fiona Waddell, journalist and ... View the story "PGM1-CDG (formerly CDG-It): A treatable Congenital Disorder of Glycosylation " on Storify]. ... Keywords:Phosphoglucomutase-1 deficiency, PGM1-CDG, Tulane PGM1-CDG Rating Scale, TPCRS, Congenital Disorders of Glycosylation ...
... reveals conservation of potential O-glycosylation sites, transmembrane, and cytoplasmic domains and a loss of minisatellite- ... reveals conservation of potential O-glycosylation sites, transmembrane, and cytoplasmic domains and a loss of minisatellite- ...
Yoshimi M, Sekiguchi T, Hara N, Nishimoto T. Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 cells. ... Yoshimi, M., Sekiguchi, T., Hara, N., & Nishimoto, T. (2000). Inhibition of N-linked glycosylation causes apoptosis in hamster ... Yoshimi, M, Sekiguchi, T, Hara, N & Nishimoto, T 2000, Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 ... Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 cells. Michihiro Yoshimi, Takeshi Sekiguchi, Nobuyuki ...
  • In-gel tryptic digestion was further applied to the gel pieces containing deglycosylated protein, for N-glycosylation site determination. (
  • Protein glycosylation is a widespread post-translational modification. (
  • The glycosylation of the complement regulatory protein, human erythrocyte CD59. (
  • Congenital Disorders of Glycosylation (CDG) are a group of genetic diseases that are caused by defects in protein glycosylation. (
  • High throughput screening for compounds that alter muscle cell glycosylation identifies new role for N-glycans in regulating sarcolemmal protein abundance and laminin binding. (
  • B3GNT5 enhances SSEA-1 expression and CSCs properties of breast cancer cells through B3GNT5 overexpression and its glycosylation-mediated protein stabilization, promoting tumorigenesis. (
  • Glycosylation is affected by several factors, including: movement of the protein through the ER and Golgi apparatus, environmental factors, and sugar availability. (
  • Protein glycosylation is a frequent posttranslational modification, highly responsive to inflammation and ageing. (
  • Protein glycosylation can be further divided into two main categories, N-linked and O-linked protein glycosylation , depending on how sugars are added to proteins. (
  • O-linked protein glycosylation (or O-glycosylation) is the process by which glycans are added to specific amino acids, such as serine and threonine, in proteins. (
  • O-glycosylation requires a variety of different enzymes to activate, modify and attach sugars to proteins and can be classified by the first sugar that is attached to the amino acid in the protein. (
  • O-linked protein glycosylation (or O-glycosylation) is a process where sugars are attached to the oxygen atom of certain amino acid residues in proteins - mainly serine and threonine, as well as others, such as tyrosine and hydroxylysine 1-3 . (
  • Mutations in the genes involved in O-glycosylation can lead to CDG, which are classified as disorders of O-linked protein glycosylation. (
  • There are seven different types of O-glycosylation which are classified based on initial monosaccharide that is attached to amino acid residue in the protein (Figure 1). (
  • O-glycosylation can be classified by the first monosaccharide attached to the protein: O-mannosylation (mannose), O-xylosylation (xylose), O-fucosylation (fucose), O-GalNAcylation (GalNAc), O-GlcNAcylation (GlcNAc), O-glucosylation (glucose) and O-galactosylation (galactose). (
  • During O-glycosylation, a monosaccharide is attached onto specific amino acids of a protein, either serine (S), threonine (T) and lysine (K). (
  • Glycosylation is an important and highly regulated mechanism of secondary protein processing within cells and it plays a crucial role in modulating the stability of proteins, as carbohydrates are important in achieving the proper three-dimensional conformation of glycoproteins. (
  • All the proteins involved in β-amyloid (Aβ) precursor protein metabolism have been identified as candidates of glycosylation highlighting the possibility that Aβ metabolism could be regulated by their glycosylation. (
  • The hexosamine biosynthetic pathway (HBP) is a branch of the glycolysis that is responsible for the production of UDP-GlcNAc, a key substrate for protein glycosylation. (
  • Protein glycosylation and advanced glycosylated endproducts (AGEs) accumulation: an avian solution? (
  • A protein expressed by yeast system could be modificated such as glycosylation, acylation, phosphorylation and so on to ensure the native protein conformation. (
  • Microbial and fungi/yeast hosts for r ecombinant protein production were limited in their ability to provide complete glycosylation. (
  • Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result. (
  • PMM2 -congenital disorder of glycosylation ( PMM2 -CDG, also known as congenital disorder of glycosylation type Ia) is an inherited condition that affects many parts of the body. (
  • A congenital disorder of glycosylation type II that has_material_basis_in an autosomal recessive mutation of COG2 on chromosome 1q42.2. (
  • The PMM2 enzyme is involved in a process called glycosylation, which attaches groups of sugar molecules (oligosaccharides) to proteins. (
  • Glycosylation modifies proteins so they can perform a wider variety of functions. (
  • The extensive glycosylation of HIV-1 envelope proteins (Envs), gp120/gp41, is known to play an important role in evasion of host immune response by masking key neutralization epitopes and presenting the Env glycosylation as "self" to the host immune system. (
  • IMSEAR at SEARO: Glycosylation of proteins: relevance to diabetes mellitus. (
  • Hyperglycemia causes excessive amounts of irreversible advanced glycosylation end products (AGEPs) to accumulate on long-lived extracellular matrix proteins and probably also on DNA in tissues that develop diabetic complications. (
  • Initial diagnostic testing involves screening of proteins for abnormal glycosylation patterns and analysis of muscle cells, but definitive diagnosis typically relies on genetic testing. (
  • During O-glycosylation, enzymes transfer monosaccharides from the activated sugars to amino acids (serine, threonine or lysine) on proteins, typically in the cytosol, Golgi, ER or nucleus. (
  • 1 N -glycosylation sequons not glycosylated in native hPGHS proteins. (
  • We used high throughput screening with the plant lectin Wisteria floribunda agglutinin (WFA) to identify compounds that altered muscle cell surface glycosylation, with the goal of finding compounds that increase abundance of α-DG and associated sarcolemmal glycoproteins, increase utrophin usage, and increase laminin binding. (
  • Glycan analysis demonstrated a general increase in N-glycans on lobeline-treated cells rather than specific alterations in cell surface glycosylation, consistent with increased abundance of multiple sarcolemmal glycoproteins. (
  • Here, we describe a mass spectrometry-based approach to characterize the glycosylation profiles of two rVV-expressed clade C Envs by identifying the glycan motifs on each glycosylation site and determining the degree of glycosylation site occupancy. (
  • Extensive weight loss reduces glycan age by altering IgG N-glycosylation. (
  • CONCLUSIONS: Altogether, these findings highlight that weight loss substantially affects IgG N-glycosylation, resulting in reduced glycan and biological age. (
  • N-glycosylation of mannose receptor (CD206) regulates glycan binding by C-type lectin domains. (
  • Previous studies indicated that self - glycosylation of MR regulates its glycan binding. (
  • The construct was expressed in different glycosylation -mutant cell lines to study the influence of differential glycosylation on receptor glycan -binding properties. (
  • We conducted site-specific N- and O- glycosylation analysis and glycosylation site characterization using mass spectrometry by which several novel O- glycosylation sites were identified in mouse MR and confirmed in human full-length MR. This information guided experiments evaluating the receptor functionality by glycan microarray analysis in combination with glycan -modifying enzymes . (
  • These results suggest that N-glycosylation alone is not sufficient for the efficient extracellular transport of the recombinant MSP-1 polypeptides through the secretory pathway in mammalian cells. (
  • In response to different growth conditions, changes in the transcription profile of aglM mirrored changes in the transcription profiles of aglF, aglG and aglI, genes encoding confirmed participants in the H. volcanii N-glycosylation pathway, thus offering support to the hypothesis that in H. volcanii, N-glycosylation serves an adaptive role. (
  • Our results indicate that the transport modality across the Golgi complex is a key determinant for the glycosylation pattern of a cargo and establish a new paradigm for the branching of the glycosphingolipid synthetic pathway. (
  • To date, almost 50 different types of congenital disorders of glycosylation (CDG) are caused by defects in the O-glycosylation pathway. (
  • Overview of the O-glycosylation pathway. (
  • Within this framework, the present review aims to summarize the current understanding on the role of glycosylation in the etiopathology of AD, emphasizing the idea that the glucose metabolic pathway may represent an alternative therapeutic option for targeting AD. (
  • The glycosylation patterns of B3GNT5 and associated functions were determined by Western blotting, quantitative real-time PCR and flow cytometry. (
  • In your description, you mention that Cell-Ess improves the consistency of glycosylation patterns. (
  • The prospect of biological age reduction, by changing glycosylation patterns through metabolic intervention, opens many possibilities. (
  • It impacts extracellular and intracellular pH and can directly and indirectly impact glycosylation patterns and molecule stability. (
  • The method developed was applied to progranulin (PGRN) to characterize the structures of the released glycans and to identify the sites of glycosylation. (
  • Through site directed mutagenesis of N-glycosylation sites we have generated forms of SNS and Duf/Kirre lacking all N-glycans. (
  • This demonstrates the feasibility of high throughput screening with plant lectins to identify compounds that alter muscle cell glycosylation and identifies a novel role for N-glycans in regulating muscle cell function. (
  • O-glycosylation is initiated by seven different monosaccharides that can be further extended to form longer sugar chains called O-glycans 6 . (
  • Aberrant glycosylation has been demonstrated in many cancers including CCA. (
  • Antibody recognition of aberrant glycosylation on the surface of cancer cells. (
  • Results: We found sGal-3 preferentially binds to b1 integrin on the surface of tumor cells due to aberrant N-glycosylation resulting from cancer-associated upregulation of several glycosyltransferases. (
  • Together, our results link ubiquitination and glycosylation pathways with stringent regulation of PD-L1, proposing a new therapeutic strategy to enhance cancer immune therapy efficacy. (
  • abstract = "Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. (
  • β-DG can also associate with utrophin, and this differential association correlates with specific glycosylation changes on α-DG. (
  • Since rescue experiments using SNS N-glycosylation mutants show only mild defects, it is apparent that, although the presence SNS is required for founder-fusion competent myoblast recognition, it is not the only molecule involved in proper execution of this process. (
  • To approach this problem, we determined high-resolution structures of Notch receptor-ligand complexes, which provided insight into the roles of molecular tension and receptor glycosylation as regulatory mechanisms. (
  • Without a properly functioning PMM2 enzyme, glycosylation cannot proceed normally. (
  • Michelakakis H, Moraitou M, Mavridou I, Dimitriou E. Plasma lysosomal enzyme activities in congenital disorders of glycosylation, galactosemia and fructosemia. (
  • PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains. (
  • Inflammation-induced changes in expression and glycosylation of genetic variants of alpha 1-acid glycoprotein. (
  • The relevance of collagen glycosylation, a fundamental post-translational modification controlling several biological processes, remains however largely unexplored. (
  • Missense DPAGT1 variants cause congenital myasthenic syndrome and congenital disorders of glycosylation. (
  • Here, we report the engineering and expression of variants of the murine TCR 2B4 in which many of the potential N-linked glycosylation sites were eliminated. (
  • Before O-glycosylation can occur, cells must generate high-energy (reactive) forms of monosaccharides, called activated sugars 7 . (
  • Nucleotide sugars are the activated form of monosaccharides used by glycosyltransferases during glycosylation. (
  • 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. (
  • Here, using mouse and cell models, we clarify the molecular mechanisms underlying the intra-Golgi vectorial transfer of GlcCer by FAPP2 and show that GlcCer is channelled by vesicular and non-vesicular transport to two topologically distinct glycosylation tracks in the Golgi cisternae and the trans-Golgi network, respectively. (
  • The apparent molecular mass of hFc-mNKG2D is approximately 35-55 kDa due to glycosylation. (
  • Biologics, on the other hand, are very large molecules with less defined structures, due to, inter alia, the effects of post-translational modifications such as glycosylation. (
  • therefore, it was thought that an inhibition of N-linked glycosylation induced apoptosis. (
  • However, tunicamycin, a potent inhibitor of N-linked glycosylation, had not caused apoptosis in wild-type BHK21 cells. (
  • Thus, we concluded that loss of N-linked glycosylation causes apoptosis. (
  • The polypeptides were studied with respect to the nature of glycosylation, localization, and proteolytic processing. (
  • The structures of the eight TAP glycosides formed with glucose and two of its derivatives, glucose-6-phosphate and N -acetylglucosamine, were found to be β-pyranosides with the glycosylation site on TAP varying with sugar identity. (
  • A site-directed mutagenesis verified a single glycosylation site in UT-A3 at Asn279. (
  • The results show that, at least in frog oocytes, the first potential N-glycosylation site (Asn45) is utilized exclusively. (
  • Lynne is a Senior Nurse Practitioner, the Undiagnosed Diseases Network NIH-UDP Site Coordinator, and the Principal Investigator for the Congenital Disorders of Glycosylation protocol. (
  • Moreover, glycosylation acts as a metabolic sensor that links glucose metabolism to normal neuronal functioning. (
  • In this study, we investigated UT-A3 regulation by glycosylation modification. (
  • Massive cancer cell death was observed in glycosylation deficient cancer cells, suggesting glycosylation of PD-L1 is required for its immunosuppression. (
  • In diabetes, endothelial cells are damaged by advance glycosylation end-products. (
  • Disorders of O-glycosylation present varied clinical features. (
  • Contrary to the complex N- and O-linked glycosylation, which requires several enzymes, O-GlcNAcylation is regulated by the concerted action of only two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). (
  • Figure 1: Different types of O-glycosylation in humans. (
  • From this perspective, the pharmacological modulation of glycosylation levels may represent a 'sweet approach' to treat AD targeting new mechanisms independent of the amyloid cascade and with comparable impacts in familial and sporadic AD. (
  • The Env glycosylation is mostly conserved but continues to evolve to modulate viral infectivity. (
  • It stands for Congenital Disorders of Glycosylation and these are a group of metabolic disorders with over 100 different types. (
  • Her areas of research include congenital disorders of glycosylation, mitochondrial disease/dysfunction, treatment of rare diseases, nutrition and supplement support for metabolic and mitochondrial diseases, and transitional care, all areas she has also published in. (
  • Optimization of glycosylation conditions using DBDMH as promoter. (
  • In many cases scientists will focus optimization efforts on either titer or glycosylation first, but find that both titer and glycosylation are affected by any one change. (
  • Two of the observed glycosylation sites occur within granulin domains, which may have important implications for understanding the structural basis of PGRN action. (
  • O-glycosylation can occur in different locations in the cell, such as the ER and Golgi, which are compartments surrounded by membranes that nucleotide sugars cannot pass through. (
  • Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains undetermined), with one of the four observed to be partially occupied. (
  • Analysis of these mutants in S2 cell aggregation assays demonstrate a specific requirement for N-glycosylation of SNS in SNS-Duf/Kirre mediated aggregation, and for Duf/Kirre in Duf/Kirre-Duf/Kirre mediated aggregation. (
  • If not depicted, the glycosylation state of the sequon was the same among all the glycoforms subjected to analysis. (
  • these features mimic the glycosylation profile of a Group M consensus immunogen, CON-S. Our results also reveal a clade-specific glycosylation pattern. (
  • These results provide insight into the role of FUT1 on intestinal glycosylation, improve our understanding of how variation in FUT1 can modulate host-microbe interactions, and suggest that the FUT1 genetic variant may help to improve pig gut health. (
  • Finally, lot-to-lot variation in commercially available supplements and feeds also introduce variation in glycosylation. (