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)
A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
Phosphoric acid esters of mannose.
A nucleoside diphosphate sugar which can be converted to the deoxy sugar GDPfucose, which provides fucose for lipopolysaccharides of bacterial cell walls. Also acts as mannose donor for glycolipid synthesis.
A lipophilic glycosyl carrier of the monosaccharide mannose in the biosynthesis of oligosaccharide phospholipids and glycoproteins.
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.
Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57.
An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC 5.3.1.8.
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins.
Polysaccharides consisting of mannose units.
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.
Hexosephosphates are sugar phosphate molecules, specifically those derived from hexoses (six-carbon sugars), such as glucose-6-phosphate and fructose-6-phosphate, which play crucial roles in various metabolic pathways including glycolysis, gluconeogenesis, and the pentose phosphate pathway.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
Compounds functioning as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. They include the polyisoprenyl pyrophosphates.
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with an alcohol to form an acetal. They include both alpha- and beta-mannosides.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
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)
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
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.
An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.
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.
Glucosamine is a naturally occurring amino sugar that plays a crucial role in the formation and maintenance of various tissues, particularly in the synthesis of proteoglycans and glycosaminoglycans, which are essential components of cartilage and synovial fluid in joints.
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 characteristic 3-dimensional shape of a carbohydrate.
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.
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.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Fucose is a deoxyhexose sugar, specifically a L-configuration 6-deoxygalactose, often found as a component of complex carbohydrates called glycans in various glycoproteins and glycolipids within the human body.
Phosphoric acid esters of dolichol.
Mannosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with methyl alcohol. They include both alpha- and beta-methylmannosides.
Hexoses are simple monosaccharides, specifically six-carbon sugars, which include glucose, fructose, and galactose, and play crucial roles in biological processes such as energy production and storage, and structural components of cells.
The N-acetyl derivative of glucosamine.
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.
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.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.
These compounds function as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. Include the pyrophosphates.
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.
An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity.
A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Glucuronidase is an enzyme (specifically, a glycosidase) that catalyzes the hydrolysis of glucuronic acid from various substrates, playing crucial roles in metabolic processes like detoxification and biotransformation within organisms.
Nucleoside Diphosphate Sugars (NDPs) are biomolecules consisting of a nucleoside monophosphate sugar molecule, which is formed from the condensation of a nucleotide and a sugar molecule through a pyrophosphate bond.
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.
Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)
Eicosamethyl octacontanonadecasen-1-o1. Polyprenol found in animal tissues that contains about 20 isoprene residues, the one carrying the alcohol group being saturated.
The rate dynamics in chemical or physical systems.
The bacterial sugar phosphotransferase system (PTS) that catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates (the PTS sugars) concomitant with the translocation of these sugars across the bacterial membrane. The phosphorylation of a given sugar requires four proteins, two general proteins, Enzyme I and HPr and a pair of sugar-specific proteins designated as the Enzyme II complex. The PTS has also been implicated in the induction of synthesis of some catabolic enzyme systems required for the utilization of sugars that are not substrates of the PTS as well as the regulation of the activity of ADENYLYL CYCLASES. EC 2.7.1.-.
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)
A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region.
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 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 genetically heterogeneous group of heritable disorders resulting from defects in protein N-glycosylation.
The sum of the weight of all the atoms in a molecule.
Five-carbon furanose sugars in which the OXYGEN is replaced by a NITROGEN atom.
An alpha-glucosidase inhibitor with antiviral action. Derivatives of deoxynojirimycin may have anti-HIV activity.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).
A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)
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)
Established cell cultures that have the potential to propagate indefinitely.
Indolizines are organic compounds that consist of a condensed pyridine and pyrrole ring structure, which can be found in certain natural and synthetic substances, and have been studied for their potential biological activities.
A well-characterized neutral peptide believed to be secreted by the LIVER and to circulate in the BLOOD. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on SOMATOTROPIN. It is believed to be a major fetal growth factor in contrast to INSULIN-LIKE GROWTH FACTOR I, which is a major growth factor in adults.
The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
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)
Compounds containing carbohydrate or glycosyl groups linked to phosphatidylinositols. They anchor GPI-LINKED PROTEINS or polysaccharides to cell membranes.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
Hexosamines are amino sugars that are formed by the substitution of an amino group for a hydroxyl group in a hexose sugar, playing crucial roles in various biological processes such as glycoprotein synthesis and protein folding.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Inborn errors of carbohydrate metabolism are genetic disorders that result from enzyme deficiencies or transport defects in the metabolic pathways responsible for breaking down and processing carbohydrates, leading to accumulation of toxic intermediates or energy deficits, and typically presenting with multisystem clinical manifestations.
An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. It requires the presence of more than two amino-acid residues in the substrate for activity. This enzyme was previously listed as EC 3.2.2.18.
A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.
The N-acetyl derivative of galactosamine.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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 lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A monosaccharide in sweet fruits and honey that is soluble in water, alcohol, or ether. It is used as a preservative and an intravenous infusion in parenteral feeding.
The aggregation of suspended solids into larger clumps.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
A plant genus in the family LILIACEAE (sometimes classified as Amaryllidaceae). Galanthus nivalis L. is the source of GALANTHAMINE.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A class of enzymes that catalyzes the phosphorylation of fructose in the presence of ATP. EC 2.7.1.-.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Transport proteins that carry specific substances in the blood or across cell membranes.
The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.
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 molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
Esters formed between the aldehydic carbon of sugars and the terminal phosphate of guanosine diphosphate.
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.
Glycoproteins found on the membrane or surface of cells.
Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.
A methylpentose whose L- isomer is found naturally in many plant glycosides and some gram-negative bacterial lipopolysaccharides.
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)
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.
Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.
Proteins prepared by recombinant DNA technology.
Xylose is a monosaccharide, a type of sugar, that is commonly found in woody plants and fruits, and it is used in medical testing to assess the absorptive capacity of the small intestine.
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.
Polyhydric alcohols having no more than one hydroxy group attached to each carbon atom. They are formed by the reduction of the carbonyl group of a sugar to a hydroxyl group.(From Dorland, 28th ed)
'Deoxy sugars' are monosaccharides or oligosaccharides that contain fewer hydroxyl groups than the corresponding hexose or pentose, with deoxyribose being a well-known example of a deoxy sugar.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
Phosphoric or pyrophosphoric acid esters of polyisoprenoids.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.
Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.
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)

Participation of a trisaccharide-lipid in glycosylation of oviduct membrane glycoproteins. (1/2363)

Preincubation of a hen oviduct membrane preparation with UDP-Nactyl[14C]glucosamine and bacitracin, followed by incubation with GDP-mannose, leads to formation of a chloroform/methanol (2/1)-extractable glycolipid. Treatment of the lipid with mild acid results in the release of a trisaccharide shown to have the structure beta-mannosyl-N-acetylglucosamineyl-N-acetylglucosamine. Incubation of purified trisaccharide-lipid with oviduct membranes in the presence of sodium deoxycholate, Mn2+, and GDP-mannose leads to formation of a labeled glycoprotein with an apparent molecular weight of 25,000...  (+info)

Mannose inhibits Arabidopsis germination via a hexokinase-mediated step. (2/2363)

Low concentrations of the glucose (Glc) analog mannose (Man) inhibit germination of Arabidopsis seeds. Man is phosphorylated by hexokinase (HXK), but the absence of germination was not due to ATP or phosphate depletion. The addition of metabolizable sugars reversed the Man-mediated inhibition of germination. Carbohydrate-mediated regulation of gene expression involving a HXK-mediated pathway is known to be activated by Glc, Man, and other monosaccharides. Therefore, we investigated whether Man blocks germination through this system. By testing other Glc analogs, we found that 2-deoxyglucose, which, like Man, is phosphorylated by HXK, also blocked germination; no inhibition was observed with 6-deoxyglucose or 3-O-methylglucose, which are not substrates for HXK. Since these latter two sugars are taken up at a rate similar to that of Man, uptake is unlikely to be involved in the inhibition of germination. Furthermore, we show that mannoheptulose, a specific HXK inhibitor, restores germination of seeds grown in the presence of Man. We conclude that HXK is involved in the Man-mediated repression of germination of Arabidopsis seeds, possibly via energy depletion.  (+info)

Glycosylation of asparagine-28 of recombinant staphylokinase with high-mannose-type oligosaccharides results in a protein with highly attenuated plasminogen activator activity. (3/2363)

The properties of recombinant staphylokinase (SakSTAR) expressed in Pichia pastoris cells have been determined. The single consensus N-linked oligosaccharide linkage site in SakSTAR (at Asn28 of the mature protein) was occupied in approximately 50% of the expressed protein with high-mannose-type oligosaccharides. The majority of these glycans ranged in polymerization state from Man8GlcNAc2 to Man14GlcNAc2, with the predominant species being Man10GlcNAc2 and Man11GlcNAc2. Glycosylated SakSTAR (SakSTARg) did not differ from its aglycosyl form in its aggregation state in solution, its thermal denaturation properties, its ability to form a complex with human plasmin (hPm), the amidolytic properties of the respective SakSTAR-hPm complexes, or its ability to liberate the amino-terminal decapeptide required for formation of a functional SakSTAR-hPm plasminogen activator complex. However, this latter complex with SakSTARg showed a greatly reduced ability to activate human plasminogen (hPg) as compared with the same complex with the aglycosyl form of SakSTAR. We conclude that glycosylation at Asn28 does not affect the structural properties of SakSTAR or its ability to participate in the formation of an active enzymatic complex with hPm, but it is detrimental to the ability of the SakSTAR-hPm complex to serve as a hPg activator. This is likely due to restricted access of hPg to the active site of the SakSTARg-hPm complex.  (+info)

Genetic evidence for the role of GDP-mannose in plant ascorbic acid (vitamin C) biosynthesis. (4/2363)

Vitamin C (L-ascorbic acid; AsA) acts as a potent antioxidant and cellular reductant in plants and animals. AsA has long been known to have many critical physiological roles in plants, yet its biosynthesis is only currently being defined. A pathway for AsA biosynthesis that features GDP-mannose and L-galactose has recently been proposed for plants. We have isolated a collection of AsA-deficient mutants of Arabidopsis thaliana that are valuable tools for testing of an AsA biosynthetic pathway. The best-characterized of these mutants (vtc1) contains approximately 25% of wild-type AsA and is defective in AsA biosynthesis. By using a combination of biochemical, molecular, and genetic techniques, we have demonstrated that the VTC1 locus encodes a GDP-mannose pyrophosphorylase (mannose-1-P guanyltransferase). This enzyme provides GDP-mannose, which is used for cell wall carbohydrate biosynthesis and protein glycosylation as well as for AsA biosynthesis. In addition to genetically defining the first locus involved in AsA biosynthesis, this work highlights the power of using traditional mutagenesis techniques coupled with the Arabidopsis Genome Initiative to rapidly clone physiologically important genes.  (+info)

Alteration of mannose transport in fibroblasts from type I carbohydrate deficient glycoprotein syndrome patients. (5/2363)

The aim of the present study was to explore how mannose enters fibroblasts derived from a panel of children suffering from different subtypes of type I carbohydrate deficient glycoprotein syndrome: seven carbohydrate deficient glycoprotein syndrome subtype Ia (phosphomannomutase deficiency), two carbohydrate deficient glycoprotein syndrome subtype Ib (phosphomannose isomerase deficiency) and two carbohydrate deficient glycoprotein syndrome subtype Ix (not identified deficiency). We showed that a specific mannose transport system exists in all the cells tested but has different characteristics with respect to carbohydrate deficient glycoprotein syndrome subtypes. Subtype Ia fibroblasts presented a mannose uptake equivalent or higher (maximum 1.6-fold) than control cells with a D-[2-3H]-mannose incorporation in nascent N-glycoproteins decreased up to 7-fold. Compared to control cells, the mannose uptake was greatly stimulated in subtype Ib (4.0-fold), due to lower Kuptake and higher Vmax values. Subtype Ib cells showed an increased incorporation of D-[2-3H]-mannose into nascent N-glycoproteins. Subtype Ix fibroblasts presented an intermediary status with mannose uptake equivalent to the control but with an increased incorporation of D-[2-3H]-mannose in nascent N-glycoproteins. All together, our results demonstrate quantitative and/or qualitative modifications in mannose transport of all carbohydrate deficient glycoprotein syndrome fibroblasts in comparison to control cells, with a relative homogeneity within a considered subtype of carbohydrate deficient glycoprotein syndrome. These results are consistent with the possible use of mannose as a therapeutic agent in carbohydrate deficient glycoprotein syndrome Ib and Ix.  (+info)

Sugars and sugar derivatives which inhibit the short-circuit current of the everted small intestine of the rat. (6/2363)

1. The short-circuit current of everted rat intestine supported on a perforated cannula proved to be stable for up to 3 hr and has been used to study competition between transportable and non-transportable sugars. 2. 4,6-O-Ethylidene-alpha-D-glucopyranose (ethylidene glucose) and 4,6-O-benzylidene-e alpha-D-glucopyranos (benzylinene glucose), two nontransportable inhibitors of the hexose transfer system in human erythrocytes, were found to reduce the short-circuit current generated by transportable sugars such as galactose or 3-O-methyl glucose. 3. These compounds were also found to reduce the basal short-circuit current established by the everted intestine in a sugar-free Krebs solution. Both types of inhibition approached saturation at the higher concentrations used. 4. Similar inhibitory properties were shown by mannose, a non-actively accumulated monosaccharide, and by the beta-disaccharides lactose and cellobiose. 5. It is suggested that this common pattern of behaviour is due to the ability of these compounds to react with the sites for active hexose transfer but without translocation by the system. The significance of the inhibition of the basal short-circuit current is briefly discussed in this context.  (+info)

Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis. (7/2363)

The human erythrocyte anion exchanger (AE1, Band 3) contains up to 14 transmembrane segments, with a single site of N-glycosylation at Asn642 in extracellular (EC) loop 4. Scanning and insertional N-glycosylation mutagenesis were used to determine the folding pattern of AE1 in the membrane. Full-length AE1, when expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells, retained a high-mannose oligosaccharide structure. Scanning N-glycosylation mutagenesis of EC loop 4 showed that N-glycosylation acceptor sites (Asn-Xaa-Ser/Thr) spaced 12 residues from the ends of adjacent transmembrane segments could be N-glycosylated. An acceptor site introduced at position 743 in intracellular (IC) loop 5 that could be N-glycosylated in a cell-free translation system was not N-glycosylated in transfected cells. Mutations designed to disrupt the folding of this loop enhanced the level of N-glycosylation at Asn743 in vitro. The results suggest that this loop might be transiently exposed to the lumen of the endoplasmic reticulum during biosynthesis but normally folds rapidly, precluding N-glycosylation. EC loop 4 insertions into positions 428, 484, 754 and 854 in EC loops 1, 2, 6 and 7 respectively were efficiently N-glycosylated, showing that these regions were extracellular. EC loop 4 insertions into positions 731 or 785 were poorly N-glycosylated, which was inconsistent with an extracellular disposition for these regions of AE1. Insertion of EC loop 4 into positions 599 and 820 in IC loops 3 and 6 respectively were not N-glycosylated in cells, which was consistent with a cytosolic disposition for these loops. Inhibitor-affinity chromatography with 4-acetamido-4'-isothiocyanostilbene-2,2'-disulphonate (SITS)-Affi-Gel was used to assess whether the AE1 mutants were in a native state. Mutants with insertions at positions 428, 484, 599, 731 and 785 showed impaired inhibitor binding, whereas insertions at positions 754, 820 and 854 retained binding. The results indicate that the folding of the C-terminal region of AE1 is more complex than originally proposed and that this region of the transporter might have a dynamic aspect.  (+info)

Recombinant human interleukin-12 is the second example of a C-mannosylated protein. (8/2363)

The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan. Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated. This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor. Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction. This shows that nonrecombinant IL-12 is potentially C-mannosylated as well. This is only the second report on a C-mannosylated protein. However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.  (+info)

Mannose is a simple sugar (monosaccharide) that is similar in structure to glucose. It is a hexose, meaning it contains six carbon atoms. Mannose is a stereoisomer of glucose, meaning it has the same chemical formula but a different structural arrangement of its atoms.

Mannose is not as commonly found in foods as other simple sugars, but it can be found in some fruits, such as cranberries, blueberries, and peaches, as well as in certain vegetables, like sweet potatoes and turnips. It is also found in some dietary fibers, such as those found in beans and whole grains.

In the body, mannose can be metabolized and used for energy, but it is also an important component of various glycoproteins and glycolipids, which are molecules that play critical roles in many biological processes, including cell recognition, signaling, and adhesion.

Mannose has been studied as a potential therapeutic agent for various medical conditions, including urinary tract infections (UTIs), because it can inhibit the attachment of certain bacteria to the cells lining the urinary tract. Additionally, mannose-binding lectins have been investigated for their potential role in the immune response to viral and bacterial infections.

Mannose-binding lectins (MBLs) are a group of proteins that belong to the collectin family and play a crucial role in the innate immune system. They are primarily produced by the liver and secreted into the bloodstream. MBLs have a specific affinity for mannose sugar residues found on the surface of various microorganisms, including bacteria, viruses, fungi, and parasites.

The primary function of MBLs is to recognize and bind to these mannose-rich structures, which triggers the complement system's activation through the lectin pathway. This process leads to the destruction of the microorganism by opsonization (coating the microbe to enhance phagocytosis) or direct lysis. MBLs also have the ability to neutralize certain viruses and inhibit the replication of others, further contributing to their antimicrobial activity.

Deficiencies in MBL levels or function have been associated with an increased susceptibility to infections, particularly in children and older adults. However, the clinical significance of MBL deficiency remains a subject of ongoing research.

IGF-2 (Insulin-like Growth Factor 2) receptor is a type of transmembrane protein that plays a role in cell growth, differentiation, and survival. Unlike other receptors in the insulin and IGF family, IGF-2 receptor does not mediate the activation of intracellular signaling pathways upon binding to its ligand (IGF-2). Instead, it acts as a clearance receptor that facilitates the removal of IGF-2 from circulation by transporting it to lysosomes for degradation.

The IGF-2 receptor is also known as cation-independent mannose-6-phosphate receptor (CI-M6PR) because it can also bind and transport mannose-6-phosphate-containing enzymes to lysosomes for degradation.

Mutations in the IGF-2 receptor gene have been associated with certain types of cancer, as well as developmental disorders such as Beckwith-Wiedemann syndrome.

I'm sorry for any confusion, but "Mannosephosphates" is not a widely recognized or established term in medicine or biochemistry. It seems that this term may be a combination of "mannose," which is a type of sugar (monosaccharide), and "phosphates," which are compounds containing phosphorus. However, without more context, it's difficult to provide an accurate medical definition for this term.

In biochemistry, mannose can be linked to phosphate groups in various ways, such as in the context of mannose-1-phosphate or mannose-6-phosphate, which are involved in different metabolic pathways. If you could provide more information about where you encountered this term, I might be able to give a more precise definition or explanation.

Guanosine diphosphate mannose (GDP-mannose) is a nucleotide sugar that plays a crucial role in the biosynthesis of various glycans, including those found on proteins and lipids. It is formed from mannose-1-phosphate through the action of the enzyme mannose-1-phosphate guanylyltransferase, using guanosine triphosphate (GTP) as a source of energy.

GDP-mannose serves as a donor substrate for several glycosyltransferases involved in the biosynthesis of complex carbohydrates, such as those found in glycoproteins and glycolipids. It is also used in the synthesis of certain polysaccharides, like bacterial cell wall components.

Defects in the metabolism or utilization of GDP-mannose can lead to various genetic disorders, such as congenital disorders of glycosylation (CDG), which can affect multiple organ systems and present with a wide range of clinical manifestations.

Dolichol monophosphate mannose (Dol-P-Man) is a type of glycosyl donor that plays a crucial role in the process of protein glycosylation within the endoplasmic reticulum (ER) of eukaryotic cells. Protein glycosylation is the enzymatic attachment of oligosaccharide chains to proteins, which can significantly affect their structure, stability, and function.

Dolichol monophosphate mannose consists of a dolichol molecule, a long-chain polyisoprenoid alcohol, linked to a mannose sugar via a phosphate group. The dolichol component serves as a lipid anchor, allowing Dol-P-Man to participate in the synthesis of oligosaccharides on the cytoplasmic side of the ER membrane.

In the first step of the process, mannose is transferred from a donor molecule, guanosine diphosphate mannose (GDP-Man), to dolichol phosphate (Dol-P) by the enzyme alpha-1,2-mannosyltransferase. This reaction forms Dol-P-Man, which then serves as a substrate for further glycosylation reactions in the ER lumen.

In summary, Dolichol monophosphate mannose is an essential intermediate in the biosynthesis of N-linked oligosaccharides, contributing to the proper folding and functioning of proteins within eukaryotic cells.

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

Mannosyltransferases are a group of enzymes that catalyze the transfer of mannose (a type of sugar) to specific acceptor molecules during the process of glycosylation. Glycosylation is the attachment of carbohydrate groups, or glycans, to proteins and lipids, which plays a crucial role in various biological processes such as protein folding, quality control, trafficking, and cell-cell recognition.

In particular, mannosyltransferases are involved in the addition of mannose residues to the core oligosaccharide structure of N-linked glycans in the endoplasmic reticulum (ER) and Golgi apparatus of eukaryotic cells. These enzymes use a donor substrate, typically dolichol-phosphate-mannose (DPM), to add mannose molecules to the acceptor substrate, which is an asparagine residue within a growing glycan chain.

There are several classes of mannosyltransferases, each responsible for adding mannose to specific positions within the glycan structure. Defects in these enzymes can lead to various genetic disorders known as congenital disorders of glycosylation (CDG), which can affect multiple organ systems and result in a wide range of clinical manifestations.

Mannose-6-Phosphate Isomerase (MPI) is an enzyme that catalyzes the interconversion between mannose-6-phosphate and fructose-6-phosphate, which are both key metabolites in the glycolysis and gluconeogenesis pathways. This enzyme plays a crucial role in maintaining the balance between these two metabolic pathways, allowing cells to either break down or synthesize glucose depending on their energy needs.

The gene that encodes for MPI is called MPI1 and is located on chromosome 4 in humans. Defects in this gene can lead to a rare genetic disorder known as Mannose-6-Phosphate Isomerase Deficiency or Congenital Disorder of Glycosylation Type IIm, which is characterized by developmental delay, intellectual disability, seizures, and various other neurological symptoms.

C-type lectins are a family of proteins that contain one or more carbohydrate recognition domains (CRDs) with a characteristic pattern of conserved sequence motifs. These proteins are capable of binding to specific carbohydrate structures in a calcium-dependent manner, making them important in various biological processes such as cell adhesion, immune recognition, and initiation of inflammatory responses.

C-type lectins can be further classified into several subfamilies based on their structure and function, including selectins, collectins, and immunoglobulin-like receptors. They play a crucial role in the immune system by recognizing and binding to carbohydrate structures on the surface of pathogens, facilitating their clearance by phagocytic cells. Additionally, C-type lectins are involved in various physiological processes such as cell development, tissue repair, and cancer progression.

It is important to note that some C-type lectins can also bind to self-antigens and contribute to autoimmune diseases. Therefore, understanding the structure and function of these proteins has important implications for developing new therapeutic strategies for various diseases.

Mannans are a type of complex carbohydrate, specifically a heteropolysaccharide, that are found in the cell walls of certain plants, algae, and fungi. They consist of chains of mannose sugars linked together, often with other sugar molecules such as glucose or galactose.

Mannans have various biological functions, including serving as a source of energy for microorganisms that can break them down. In some cases, mannans can also play a role in the immune response and are used as a component of vaccines to stimulate an immune response.

In the context of medicine, mannans may be relevant in certain conditions such as gut dysbiosis or allergic reactions to foods containing mannans. Additionally, some research has explored the potential use of mannans as a delivery vehicle for drugs or other therapeutic agents.

Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).

Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.

Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.

Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.

Hexose phosphates are organic compounds that consist of a hexose sugar molecule (a monosaccharide containing six carbon atoms, such as glucose or fructose) that has been phosphorylated, meaning that a phosphate group has been added to it. This process is typically facilitated by enzymes called kinases, which transfer a phosphate group from a donor molecule (usually ATP) to the sugar molecule.

Hexose phosphates play important roles in various metabolic pathways, including glycolysis, gluconeogenesis, and the pentose phosphate pathway. For example, glucose-6-phosphate is a key intermediate in both glycolysis and gluconeogenesis, while fructose-6-phosphate and fructose-1,6-bisphosphate are important intermediates in glycolysis. The pentose phosphate pathway, which is involved in the production of NADPH and ribose-5-phosphate, begins with the conversion of glucose-6-phosphate to 6-phosphogluconolactone by the enzyme glucose-6-phosphate dehydrogenase.

Overall, hexose phosphates are important metabolic intermediates that help regulate energy production and utilization in cells.

Mannosidases are a group of enzymes that catalyze the hydrolysis of mannose residues from glycoproteins, oligosaccharides, and glycolipids. These enzymes play a crucial role in the processing and degradation of N-linked glycans, which are carbohydrate structures attached to proteins in eukaryotic cells.

There are several types of mannosidases, including alpha-mannosidase and beta-mannosidase, which differ in their specificity for the type of linkage they cleave. Alpha-mannosidases hydrolyze alpha-1,2-, alpha-1,3-, alpha-1,6-mannosidic bonds, while beta-mannosidases hydrolyze beta-1,4-mannosidic bonds.

Deficiencies in mannosidase activity can lead to various genetic disorders, such as alpha-mannosidosis and beta-mannosidosis, which are characterized by the accumulation of unprocessed glycoproteins and subsequent cellular dysfunction.

Polyisoprenyl phosphate sugars are a type of glycosylated lipid that plays a crucial role in the biosynthesis of isoprenoid-derived natural products, including sterols and dolichols. These molecules consist of a polyisoprenyl phosphate group linked to one or more sugar moieties, such as glucose, mannose, or fructose. They serve as essential intermediates in the biosynthetic pathways that produce various isoprenoid-derived compounds, which have diverse functions in cellular metabolism and homeostasis.

The polyisoprenyl phosphate group is synthesized from isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP), the building blocks of isoprenoid biosynthesis, through a series of enzymatic reactions. The sugar moiety is then transferred to the polyisoprenyl phosphate group by specific glycosyltransferases, resulting in the formation of polyisoprenyl phosphate sugars.

These molecules are involved in various cellular processes, such as protein prenylation, where they serve as lipid anchors that facilitate the attachment of isoprenoid groups to proteins, thereby modulating their localization, stability, and activity. Additionally, polyisoprenyl phosphate sugars participate in the biosynthesis of bacterial cell wall components, such as peptidoglycan and lipopolysaccharides, highlighting their importance in both eukaryotic and prokaryotic organisms.

In summary, polyisoprenyl phosphate sugars are a class of glycosylated lipids that play a critical role in isoprenoid biosynthesis and related cellular processes, including protein prenylation and bacterial cell wall synthesis.

Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.

Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:

1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.

Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.

Mannosides are glycosylated compounds that consist of a mannose sugar molecule (a type of monosaccharide) linked to another compound, often a protein or lipid. They are formed when an enzyme called a glycosyltransferase transfers a mannose molecule from a donor substrate, such as a nucleotide sugar (like GDP-mannose), to an acceptor molecule.

Mannosides can be found on the surface of many types of cells and play important roles in various biological processes, including cell recognition, signaling, and protein folding. They are also involved in the immune response and have been studied as potential therapeutic targets for a variety of diseases, including infectious diseases and cancer.

It's worth noting that mannosides can be further classified based on the specific linkage between the mannose molecule and the acceptor compound. For example, an N-linked mannoside is one in which the mannose is linked to a nitrogen atom on the acceptor protein, while an O-linked mannoside is one in which the mannose is linked to an oxygen atom on the acceptor protein.

A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.

For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.

Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.

Monosaccharides are simple sugars that cannot be broken down into simpler units by hydrolysis. They are the most basic unit of carbohydrates and are often referred to as "simple sugars." Monosaccharides typically contain three to seven atoms of carbon, but the most common monosaccharides contain five or six carbon atoms.

The general formula for a monosaccharide is (CH2O)n, where n is the number of carbon atoms in the molecule. The majority of monosaccharides have a carbonyl group (aldehyde or ketone) and multiple hydroxyl groups. These functional groups give monosaccharides their characteristic sweet taste and chemical properties.

The most common monosaccharides include glucose, fructose, and galactose, all of which contain six carbon atoms and are known as hexoses. Other important monosaccharides include pentoses (five-carbon sugars) such as ribose and deoxyribose, which play crucial roles in the structure and function of nucleic acids (DNA and RNA).

Monosaccharides can exist in various forms, including linear and cyclic structures. In aqueous solutions, monosaccharides often form cyclic structures through a reaction between the carbonyl group and a hydroxyl group, creating a hemiacetal or hemiketal linkage. These cyclic structures can adopt different conformations, known as anomers, depending on the orientation of the hydroxyl group attached to the anomeric carbon atom.

Monosaccharides serve as essential building blocks for complex carbohydrates, such as disaccharides (e.g., sucrose, lactose, and maltose) and polysaccharides (e.g., starch, cellulose, and glycogen). They also participate in various biological processes, including energy metabolism, cell recognition, and protein glycosylation.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

Alpha-Mannosidase is an enzyme that belongs to the glycoside hydrolase family 47. It is responsible for cleaving alpha-1,3-, alpha-1,6-mannosidic linkages in N-linked oligosaccharides during the process of glycoprotein degradation. A deficiency or malfunction of this enzyme can lead to a lysosomal storage disorder known as alpha-Mannosidosis.

Polyisoprenyl phosphate monosaccharides are a type of glycosylated lipid intermediate molecule involved in the biosynthesis of isoprenoid-linked oligosaccharides, which are crucial for various cellular processes such as protein glycosylation and membrane trafficking.

These molecules consist of a polyisoprenyl phosphate tail, typically formed by the addition of multiple isoprene units (such as farnesyl or geranylgeranyl groups), which is attached to a single monosaccharide sugar moiety, such as glucose, mannose, or galactose.

The polyisoprenyl phosphate tail serves as a lipid anchor that helps tether the glycosylated molecule to cellular membranes during biosynthesis and transport. The monosaccharide component can be further modified by the addition of additional sugar residues, leading to the formation of more complex oligosaccharides that play important roles in various biological processes.

Glucosamine is a natural compound found in the body, primarily in the fluid around joints. It is a building block of cartilage, which is the tissue that cushions bones and allows for smooth joint movement. Glucosamine can also be produced in a laboratory and is commonly sold as a dietary supplement.

Medical definitions of glucosamine describe it as a type of amino sugar that plays a crucial role in the formation and maintenance of cartilage, ligaments, tendons, and other connective tissues. It is often used as a supplement to help manage osteoarthritis symptoms, such as pain, stiffness, and swelling in the joints, by potentially reducing inflammation and promoting cartilage repair.

There are different forms of glucosamine available, including glucosamine sulfate, glucosamine hydrochloride, and N-acetyl glucosamine. Glucosamine sulfate is the most commonly used form in supplements and has been studied more extensively than other forms. While some research suggests that glucosamine may provide modest benefits for osteoarthritis symptoms, its effectiveness remains a topic of ongoing debate among medical professionals.

Galactose is a simple sugar or monosaccharide that is a constituent of lactose, the disaccharide found in milk and dairy products. It's structurally similar to glucose but with a different chemical structure, and it plays a crucial role in various biological processes.

Galactose can be metabolized in the body through the action of enzymes such as galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-galactose 4'-epimerase. Inherited deficiencies in these enzymes can lead to metabolic disorders like galactosemia, which can cause serious health issues if not diagnosed and treated promptly.

In summary, Galactose is a simple sugar that plays an essential role in lactose metabolism and other biological processes.

Carbohydrate conformation refers to the three-dimensional shape and structure of a carbohydrate molecule. Carbohydrates, also known as sugars, can exist in various conformational states, which are determined by the rotation of their component bonds and the spatial arrangement of their functional groups.

The conformation of a carbohydrate molecule can have significant implications for its biological activity and recognition by other molecules, such as enzymes or antibodies. Factors that can influence carbohydrate conformation include the presence of intramolecular hydrogen bonds, steric effects, and intermolecular interactions with solvent molecules or other solutes.

In some cases, the conformation of a carbohydrate may be stabilized by the formation of cyclic structures, in which the hydroxyl group at one end of the molecule forms a covalent bond with the carbonyl carbon at the other end, creating a ring structure. The most common cyclic carbohydrates are monosaccharides, such as glucose and fructose, which can exist in various conformational isomers known as anomers.

Understanding the conformation of carbohydrate molecules is important for elucidating their biological functions and developing strategies for targeting them with drugs or other therapeutic agents.

Glycopeptides are a class of antibiotics that are characterized by their complex chemical structure, which includes both peptide and carbohydrate components. These antibiotics are produced naturally by certain types of bacteria and are effective against a range of Gram-positive bacterial infections, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE).

The glycopeptide antibiotics work by binding to the bacterial cell wall precursor, preventing the cross-linking of peptidoglycan chains that is necessary for the formation of a strong and rigid cell wall. This leads to the death of the bacteria.

Examples of glycopeptides include vancomycin, teicoplanin, and dalbavancin. While these antibiotics have been used successfully for many years, their use is often limited due to concerns about the emergence of resistance and potential toxicity.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Fucose is a type of sugar molecule that is often found in complex carbohydrates known as glycans, which are attached to many proteins and lipids in the body. It is a hexose sugar, meaning it contains six carbon atoms, and is a type of L-sugar, which means that it rotates plane-polarized light in a counterclockwise direction.

Fucose is often found at the ends of glycan chains and plays important roles in various biological processes, including cell recognition, signaling, and interaction. It is also a component of some blood group antigens and is involved in the development and function of the immune system. Abnormalities in fucosylation (the addition of fucose to glycans) have been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Dolichol phosphates are a type of lipid molecule that play a crucial role in the process of protein glycosylation within the endoplasmic reticulum of eukaryotic cells. Glycosylation is the attachment of carbohydrate groups, or oligosaccharides, to proteins and lipids.

Dolichol phosphates consist of a long, isoprenoid hydrocarbon chain that is attached to two phosphate groups. The hydrocarbon chain can vary in length but typically contains between 10 and 20 isoprene units. These molecules serve as the anchor for the oligosaccharides during the glycosylation process.

In the first step of protein glycosylation, an oligosaccharide is synthesized on a dolichol phosphate molecule through the sequential addition of sugar residues by a series of enzymes. Once the oligosaccharide is complete, it is transferred to the target protein in a process called "oligosaccharyltransferase" (OST)-mediated transfer. This transfer results in the formation of a glycoprotein, which can then undergo further modifications as it moves through the secretory pathway.

Defects in dolichol phosphate metabolism have been linked to various genetic disorders, such as congenital disorder of glycosylation (CDG) types Ib and Id, which are characterized by abnormal protein glycosylation and a wide range of clinical manifestations, including developmental delay, neurological impairment, and multi-systemic involvement.

Methylmannosides are not a recognized medical term or a specific medical condition. However, in biochemistry, methylmannosides refer to a type of glycosylation pattern where a methyl group (-CH3) is attached to a mannose sugar molecule. Mannose is a type of monosaccharide or simple sugar that is commonly found in various glycoproteins and glycolipids in the human body.

Methylmannosides can be formed through the enzymatic transfer of a methyl group from a donor molecule, such as S-adenosylmethionine (SAM), to the mannose sugar by methyltransferase enzymes. These modifications can play important roles in various biological processes, including protein folding, trafficking, and quality control, as well as cell-cell recognition and signaling.

It's worth noting that while methylmannosides have significant biochemical importance, they are not typically referred to in medical contexts unless discussing specific biochemical or molecular research studies.

Hexoses are simple sugars (monosaccharides) that contain six carbon atoms. The most common hexoses include glucose, fructose, and galactose. These sugars play important roles in various biological processes, such as serving as energy sources or forming complex carbohydrates like starch and cellulose. Hexoses are essential for the structure and function of living organisms, including humans.

Acetylglucosamine is a type of sugar that is commonly found in the body and plays a crucial role in various biological processes. It is a key component of glycoproteins and proteoglycans, which are complex molecules made up of protein and carbohydrate components.

More specifically, acetylglucosamine is an amino sugar that is formed by the addition of an acetyl group to glucosamine. It can be further modified in the body through a process called acetylation, which involves the addition of additional acetyl groups.

Acetylglucosamine is important for maintaining the structure and function of various tissues in the body, including cartilage, tendons, and ligaments. It also plays a role in the immune system and has been studied as a potential therapeutic target for various diseases, including cancer and inflammatory conditions.

In summary, acetylglucosamine is a type of sugar that is involved in many important biological processes in the body, and has potential therapeutic applications in various diseases.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Cathepsin D is a lysosomal aspartic protease that plays a role in intracellular protein degradation and turnover. It is produced as an inactive precursor and is activated by cleavage into two subunits within the acidic environment of the lysosome. Cathepsin D is also known to be secreted by certain cells, where it can contribute to extracellular matrix remodeling and tissue degradation. In addition, abnormal levels or activity of cathepsin D have been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

Mannose-Binding Lectin (MBL) is a protein that belongs to the collectin family and plays a crucial role in the innate immune system. It's primarily produced by the liver and secreted into the bloodstream. MBL binds to carbohydrate structures, such as mannose, found on the surface of various microorganisms, including bacteria, viruses, fungi, and parasites.

Once MBL binds to these microorganisms, it activates the complement system through the lectin pathway, which leads to the destruction of the pathogens by opsonization (marking for phagocytosis) or direct lysis. Additionally, MBL can also initiate other immune responses, such as inflammation and immune cell activation, helping to protect the host from infections.

Deficiencies in MBL have been associated with increased susceptibility to certain infectious diseases, autoimmune disorders, and allergies. However, more research is needed to fully understand the complex role of MBL in human health and disease.

Polyisoprenyl Phosphate Oligosaccharides are a type of molecule that play a role in the process of protein glycosylation, which is the attachment of sugar molecules to proteins. They consist of a polyisoprenyl phosphate molecule, which is a long-chain alcohol with isoprene units, linked to an oligosaccharide, which is a short chain of simple sugars. These molecules are involved in the transfer of the oligosaccharide to the protein during glycosylation, and they play a crucial role in the proper folding and functioning of many proteins in the body. They are found in various organisms, including bacteria, plants, and animals.

Hexosaminidases are a group of enzymes that play a crucial role in the breakdown of complex carbohydrates, specifically glycoproteins and glycolipids, in the human body. These enzymes are responsible for cleaving the terminal N-acetyl-D-glucosamine (GlcNAc) residues from these molecules during the process of glycosidase digestion.

There are several types of hexosaminidases, including Hexosaminidase A and Hexosaminidase B, which are encoded by different genes and have distinct functions. Deficiencies in these enzymes can lead to serious genetic disorders, such as Tay-Sachs disease and Sandhoff disease, respectively. These conditions are characterized by the accumulation of undigested glycolipids and glycoproteins in various tissues, leading to progressive neurological deterioration and other symptoms.

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

Beta-Mannosidase is an enzyme that breaks down complex carbohydrates known as glycoproteins. It does this by catalyzing the hydrolysis of beta-mannosidic linkages, which are specific types of chemical bonds that connect mannose sugars within glycoproteins.

This enzyme plays an important role in the normal functioning of the body, particularly in the breakdown and recycling of glycoproteins. A deficiency in beta-mannosidase activity can lead to a rare genetic disorder known as beta-Mannosidosis, which is characterized by the accumulation of mannose-rich oligosaccharides in various tissues and organs, leading to progressive neurological deterioration and other symptoms.

Swainsonine is not a medical condition or disease, but rather a toxin that can cause a medical condition known as "locoism" in animals. Swainsonine is produced by certain plants, including some species of the genera Swainsona and Astragalus, which are commonly known as locoweeds.

Swainsonine inhibits an enzyme called alpha-mannosidase, leading to abnormal accumulation of mannose-rich oligosaccharides in various tissues and organs. This can result in a range of clinical signs, including neurological symptoms such as tremors, ataxia (loss of coordination), and behavioral changes; gastrointestinal symptoms such as diarrhea, weight loss, and decreased appetite; and reproductive problems.

Locoism is most commonly seen in grazing animals such as cattle, sheep, and horses that consume large quantities of locoweeds over an extended period. It can be difficult to diagnose and treat, and prevention through management practices such as rotational grazing and avoiding the introduction of toxic plants into pastures is often the best approach.

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (MGNAG) is an enzyme that is involved in the breakdown and recycling of glycoproteins, which are proteins that contain oligosaccharide chains attached to them. The enzyme's primary function is to cleave the beta-N-acetylglucosaminyl linkages in the chitobiose core of N-linked glycans, which are complex carbohydrates that are attached to many proteins in eukaryotic cells.

MGNAG is a lysosomal enzyme, meaning it is located within the lysosomes, which are membrane-bound organelles found in the cytoplasm of eukaryotic cells. Lysosomes contain hydrolytic enzymes that break down various biomolecules, including glycoproteins, lipids, and nucleic acids, into their constituent parts for recycling or disposal.

Deficiency in MGNAG activity can lead to a rare genetic disorder known as alpha-mannosidosis, which is characterized by the accumulation of mannose-rich oligosaccharides in various tissues and organs throughout the body. This condition can result in a range of symptoms, including developmental delays, intellectual disability, coarse facial features, skeletal abnormalities, hearing loss, and immune dysfunction.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Glucuronidase is an enzyme that catalyzes the hydrolysis of glucuronic acid from various substrates, including molecules that have been conjugated with glucuronic acid as part of the detoxification process in the body. This enzyme plays a role in the breakdown and elimination of certain drugs, toxins, and endogenous compounds, such as bilirubin. It is found in various tissues and organisms, including humans, bacteria, and insects. In clinical contexts, glucuronidase activity may be measured to assess liver function or to identify the presence of certain bacterial infections.

Nucleoside diphosphate sugars (NDP-sugars) are essential activated sugars that play a crucial role in the biosynthesis of complex carbohydrates, such as glycoproteins and glycolipids. They consist of a sugar molecule linked to a nucleoside diphosphate, which is formed from a nucleotide by removal of one phosphate group.

NDP-sugars are created through the action of enzymes called nucleoside diphosphate sugars synthases or transferases, which transfer a sugar molecule from a donor to a nucleoside diphosphate, forming an NDP-sugar. The resulting NDP-sugar can then be used as a substrate for various glycosyltransferases that catalyze the addition of sugars to other molecules, such as proteins or lipids.

NDP-sugars are involved in many important biological processes, including cell signaling, protein targeting, and immune response. They also play a critical role in maintaining the structural integrity of cells and tissues.

Plant lectins are proteins or glycoproteins that are abundantly found in various plant parts such as seeds, leaves, stems, and roots. They have the ability to bind specifically to carbohydrate structures present on cell membranes, known as glycoconjugates. This binding property of lectins is reversible and non-catalytic, meaning it does not involve any enzymatic activity.

Lectins play several roles in plants, including defense against predators, pathogens, and herbivores. They can agglutinate red blood cells, stimulate the immune system, and have been implicated in various biological processes such as cell growth, differentiation, and apoptosis (programmed cell death). Some lectins also exhibit mitogenic activity, which means they can stimulate the proliferation of certain types of cells.

In the medical field, plant lectins have gained attention due to their potential therapeutic applications. For instance, some lectins have been shown to possess anti-cancer properties and are being investigated as potential cancer treatments. However, it is important to note that some lectins can be toxic or allergenic to humans and animals, so they must be used with caution.

Glycolipids are a type of lipid (fat) molecule that contain one or more sugar molecules attached to them. They are important components of cell membranes, where they play a role in cell recognition and signaling. Glycolipids are also found on the surface of some viruses and bacteria, where they can be recognized by the immune system as foreign invaders.

There are several different types of glycolipids, including cerebrosides, gangliosides, and globosides. These molecules differ in the number and type of sugar molecules they contain, as well as the structure of their lipid tails. Glycolipids are synthesized in the endoplasmic reticulum and Golgi apparatus of cells, and they are transported to the cell membrane through vesicles.

Abnormalities in glycolipid metabolism or structure have been implicated in a number of diseases, including certain types of cancer, neurological disorders, and autoimmune diseases. For example, mutations in genes involved in the synthesis of glycolipids can lead to conditions such as Tay-Sachs disease and Gaucher's disease, which are characterized by the accumulation of abnormal glycolipids in cells.

Dolichol is a type of lipid molecule that is involved in the process of protein glycosylation within the endoplasmic reticulum of eukaryotic cells. Glycosylation is the attachment of sugar molecules to proteins, and it plays a crucial role in various biological processes such as protein folding, trafficking, and cell-cell recognition.

Dolichols are long-chain polyisoprenoid alcohols that serve as carriers for the sugars during glycosylation. They consist of a hydrophobic tail made up of many isoprene units and a hydrophilic head group. The dolichol molecule is first activated by the addition of a diphosphate group to its terminal end, forming dolichyl pyrophosphate.

The sugars that will be attached to the protein are then transferred from their nucleotide sugar donors onto the dolichyl pyrophosphate carrier, creating a dolichol-linked oligosaccharide. This oligosaccharide is then transferred en bloc to the target protein in a process called "oligosaccharyltransferase" (OST) reaction.

Defects in dolichol biosynthesis or function can lead to various genetic disorders, such as congenital disorders of glycosylation (CDG), which are characterized by abnormal protein glycosylation and a wide range of clinical manifestations, including developmental delay, neurological impairment, and multi-systemic involvement.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

The Phosphoenolpyruvate (PEP) sugar phosphotransferase system (PTS) is not exactly a "sugar," but rather a complex molecular machinery used by certain bacteria for the transport and phosphorylation of sugars. The PTS system is a major carbohydrate transport system in many gram-positive and gram-negative bacteria, which allows them to take up and metabolize various sugars for energy and growth.

The PTS system consists of several protein components, including the enzyme I (EI), histidine phosphocarrier protein (HPr), and sugar-specific enzymes II (EII). The process begins when PEP transfers a phosphate group to EI, which then passes it on to HPr. The phosphorylated HPr then interacts with the sugar-specific EII complex, which is composed of two domains: the membrane-associated domain (EIIA) and the periplasmic domain (EIIC).

When a sugar molecule binds to the EIIC domain, it induces a conformational change that allows the phosphate group from HPr to be transferred to the sugar. This phosphorylation event facilitates the translocation of the sugar across the membrane and into the cytoplasm, where it undergoes further metabolic reactions.

In summary, the Phosphoenolpyruvate Sugar Phosphotransferase System (PEP-PTS) is a bacterial transport system that utilizes phosphoryl groups from phosphoenolpyruvate to facilitate the uptake and phosphorylation of sugars, allowing bacteria to efficiently metabolize and utilize various carbon sources for energy and growth.

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

Collectins are a group of proteins that belong to the collectin family, which are involved in the innate immune system. They are composed of a collagen-like region and a carbohydrate recognition domain (CRD), which allows them to bind to specific sugars on the surface of microorganisms, cells, and particles. Collectins play a crucial role in the defense against pathogens by promoting the clearance of microbes, modulating inflammation, and regulating immune responses.

Some examples of collectins include:

* Surfactant protein A (SP-A) and surfactant protein D (SP-D), which are found in the lungs and help to maintain the stability of the lung lining and protect against respiratory infections.
* Mannose-binding lectin (MBL), which is a serum protein that binds to mannose sugars on the surface of microorganisms, activating the complement system and promoting phagocytosis.
* Collectin liver 1 (CL-L1) and collectin kidney 1 (CL-K1), which are found in the liver and kidneys, respectively, and play a role in the clearance of apoptotic cells and immune complexes.

Deficiencies or mutations in collectins can lead to increased susceptibility to infections, autoimmune diseases, and other disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Tunicamycin is not a medical condition or disease, but rather a bacterial antibiotic and a research tool used in biochemistry and cell biology. It is produced by certain species of bacteria, including Streptomyces lysosuperificus and Streptomyces chartreusis.

Tunicamycin works by inhibiting the enzyme that catalyzes the first step in the biosynthesis of N-linked glycoproteins, which are complex carbohydrates that are attached to proteins during their synthesis. This leads to the accumulation of misfolded proteins and endoplasmic reticulum (ER) stress, which can ultimately result in cell death.

In medical research, tunicamycin is often used to study the role of N-linked glycoproteins in various biological processes, including protein folding, quality control, and trafficking. It has also been explored as a potential therapeutic agent for cancer and other diseases, although its use as a drug is limited by its toxicity to normal cells.

Congenital Disorders of Glycosylation (CDG) are a group of genetic disorders that affect the body's ability to add sugar molecules (glycans) to proteins and lipids. This process, known as glycosylation, is essential for the proper functioning of many cellular processes, including protein folding, trafficking, and signaling.

CDG can be caused by mutations in genes that are involved in the synthesis or transport of glycans. These genetic defects can lead to abnormal glycosylation patterns, which can result in a wide range of clinical manifestations, including developmental delay, intellectual disability, seizures, movement disorders, hypotonia, coagulation abnormalities, and multi-organ involvement.

CDG are typically classified into two main types: type I CDG, which involves defects in the synthesis of the lipid-linked oligosaccharide precursor used for N-glycosylation, and type II CDG, which involves defects in the processing and transfer of glycans to proteins.

The diagnosis of CDG is often based on clinical features, laboratory tests, and genetic analysis. Treatment is typically supportive and multidisciplinary, focusing on addressing specific symptoms and improving quality of life. In some cases, dietary modifications or supplementation with mannose or other sugars may be beneficial.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Imino furanoses are not a recognized medical term, but they may be referred to in the field of biochemistry and carbohydrate research. In this context, imino furanoses are a type of sugar ring structure that contains an imine group (-C=N-) instead of the usual oxygen atom in the furanose form of sugars. Imino furanoses can be formed under certain conditions during chemical reactions involving carbohydrates, but they are not typically found in biological systems.

1-Deoxynojirimycin (DNJ) is an antagonist of the enzyme alpha-glucosidase, which is involved in the digestion of carbohydrates. DNJ is a naturally occurring compound found in some plants, including mulberry leaves and the roots of the African plant Moringa oleifera. It works by binding to the active site of alpha-glucosidase and inhibiting its activity, which can help to slow down the digestion and absorption of carbohydrates in the small intestine. This can help to reduce postprandial glucose levels (the spike in blood sugar that occurs after a meal) and may have potential benefits for the management of diabetes and other metabolic disorders. DNJ is also being studied for its potential anti-cancer effects.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

Paper chromatography is a type of chromatography technique that involves the separation and analysis of mixtures based on their components' ability to migrate differently upon capillary action on a paper medium. This simple and cost-effective method utilizes a paper, typically made of cellulose, as the stationary phase. The sample mixture is applied as a small spot near one end of the paper, and then the other end is dipped into a developing solvent or a mixture of solvents (mobile phase) in a shallow container.

As the mobile phase moves up the paper by capillary action, components within the sample mixture separate based on their partition coefficients between the stationary and mobile phases. The partition coefficient describes how much a component prefers to be in either the stationary or mobile phase. Components with higher partition coefficients in the mobile phase will move faster and further than those with lower partition coefficients.

Once separation is complete, the paper is dried and can be visualized under ultraviolet light or by using chemical reagents specific for the components of interest. The distance each component travels from the origin (point of application) and its corresponding solvent front position are measured, allowing for the calculation of Rf values (retardation factors). Rf is a dimensionless quantity calculated as the ratio of the distance traveled by the component to the distance traveled by the solvent front.

Rf = (distance traveled by component) / (distance traveled by solvent front)

Paper chromatography has been widely used in various applications, such as:

1. Identification and purity analysis of chemical compounds in pharmaceuticals, forensics, and research laboratories.
2. Separation and detection of amino acids, sugars, and other biomolecules in biological samples.
3. Educational purposes to demonstrate the principles of chromatography and separation techniques.

Despite its limitations, such as lower resolution compared to high-performance liquid chromatography (HPLC) and less compatibility with volatile or nonpolar compounds, paper chromatography remains a valuable tool for quick, qualitative analysis in various fields.

Mucolipidoses are a group of inherited metabolic disorders characterized by the accumulation of complex carbohydrates (muco-) and fatty substances (lipids) in various tissues and cells (-oses). This is due to deficiency in enzymes that help break down these substances within lysosomes, which are organelles responsible for recycling and breaking down waste materials inside the cell.

There are four main types of mucolipidoses (I, II, III, and IV), each resulting from specific genetic mutations affecting different enzymes or proteins involved in the lysosomal degradation pathway. The symptoms, severity, and age of onset can vary widely among these types, ranging from mild to severe and including developmental delays, bone abnormalities, vision and hearing loss, heart problems, and coarse facial features.

Mucolipidoses are typically inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the condition. However, mucolipidosis II is caused by X-linked inheritance, where a single copy of the mutated gene on the X chromosome is enough to cause the disorder.

Early diagnosis and management of mucolipidoses can help improve quality of life and slow disease progression. Treatment options include physical therapy, occupational therapy, speech therapy, medications for symptom management, and in some cases, enzyme replacement therapy or bone marrow transplantation.

Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.

The process typically involves the following steps:

1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.

Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

I'm sorry for any confusion, but "Indolizines" is not a medical term. It is a chemical term that refers to a class of heterocyclic organic compounds which contain a seven-membered ring with two nitrogen atoms and a carbon-carbon double bond. They are used in the synthesis of various pharmaceuticals and natural products, but they are not a medical condition or diagnosis.

Insulin-like Growth Factor II (IGF-II) is a growth factor that is structurally and functionally similar to insulin. It is a single-chain polypeptide hormone, primarily produced by the liver under the regulation of growth hormone. IGF-II plays an essential role in fetal growth and development, and continues to have important functions in postnatal life, including promoting cell growth, proliferation, and differentiation in various tissues.

IGF-II binds to and activates the IGF-I receptor and the insulin receptor, leading to intracellular signaling cascades that regulate metabolic and mitogenic responses. Dysregulation of IGF-II expression and signaling has been implicated in several pathological conditions, such as cancer, growth disorders, and diabetes.

It is important to note that IGF-II should not be confused with Insulin-like Growth Factor I (IGF-I), which is another hormone with structural and functional similarities to insulin but has distinct roles in growth and development.

Macrophages are a type of white blood cell that are an essential part of the immune system. They are large, specialized cells that engulf and destroy foreign substances, such as bacteria, viruses, parasites, and fungi, as well as damaged or dead cells. Macrophages are found throughout the body, including in the bloodstream, lymph nodes, spleen, liver, lungs, and connective tissues. They play a critical role in inflammation, immune response, and tissue repair and remodeling.

Macrophages originate from monocytes, which are a type of white blood cell produced in the bone marrow. When monocytes enter the tissues, they differentiate into macrophages, which have a larger size and more specialized functions than monocytes. Macrophages can change their shape and move through tissues to reach sites of infection or injury. They also produce cytokines, chemokines, and other signaling molecules that help coordinate the immune response and recruit other immune cells to the site of infection or injury.

Macrophages have a variety of surface receptors that allow them to recognize and respond to different types of foreign substances and signals from other cells. They can engulf and digest foreign particles, bacteria, and viruses through a process called phagocytosis. Macrophages also play a role in presenting antigens to T cells, which are another type of immune cell that helps coordinate the immune response.

Overall, macrophages are crucial for maintaining tissue homeostasis, defending against infection, and promoting wound healing and tissue repair. Dysregulation of macrophage function has been implicated in a variety of diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Asparagine is an organic compound that is classified as a naturally occurring amino acid. It contains an amino group, a carboxylic acid group, and a side chain consisting of a single carbon atom bonded to a nitrogen atom, making it a neutral amino acid. Asparagine is encoded by the genetic codon AAU or AAC in the DNA sequence.

In the human body, asparagine plays important roles in various biological processes, including serving as a building block for proteins and participating in the synthesis of other amino acids. It can also act as a neurotransmitter and is involved in the regulation of cellular metabolism. Asparagine can be found in many foods, particularly in high-protein sources such as meat, fish, eggs, and dairy products.

Glycosylphosphatidylinositols (GPIs) are complex glycolipids that are attached to the outer leaflet of the cell membrane. They play a role in anchoring proteins to the cell surface by serving as a post-translational modification site for certain proteins, known as GPI-anchored proteins.

The structure of GPIs consists of a core glycan backbone made up of three mannose and one glucosamine residue, which is linked to a phosphatidylinositol (PI) anchor via a glycosylphosphatidylinositol anchor addition site. The PI anchor is composed of a diacylglycerol moiety and a phosphatidylinositol headgroup.

GPIs are involved in various cellular processes, including signal transduction, protein targeting, and cell adhesion. They have also been implicated in several diseases, such as cancer and neurodegenerative disorders.

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Hexosamines are amino sugars that are formed by the substitution of an amino group (-NH2) for a hydroxyl group (-OH) in a hexose sugar. The most common hexosamine is N-acetylglucosamine (GlcNAc), which is derived from glucose. Other hexosamines include galactosamine, mannosamine, and fucosamine.

Hexosamines play important roles in various biological processes, including the formation of glycosaminoglycans, proteoglycans, and glycoproteins. These molecules are involved in many cellular functions, such as cell signaling, cell adhesion, and protein folding. Abnormalities in hexosamine metabolism have been implicated in several diseases, including diabetes, cancer, and neurodegenerative disorders.

Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.

Inborn errors of carbohydrate metabolism refer to genetic disorders that affect the body's ability to break down and process carbohydrates, which are sugars and starches that provide energy for the body. These disorders are caused by defects in enzymes or transport proteins that play a critical role in the metabolic pathways involved in carbohydrate metabolism.

There are several types of inborn errors of carbohydrate metabolism, including:

1. Galactosemia: This disorder affects the body's ability to metabolize the sugar galactose, which is found in milk and other dairy products. It is caused by a deficiency of the enzyme galactose-1-phosphate uridylyltransferase.
2. Glycogen storage diseases: These disorders affect the body's ability to store and break down glycogen, which is a complex carbohydrate that serves as a source of energy for the body. There are several types of glycogen storage diseases, each caused by a deficiency in a different enzyme involved in glycogen metabolism.
3. Hereditary fructose intolerance: This disorder affects the body's ability to metabolize the sugar fructose, which is found in fruits and sweeteners. It is caused by a deficiency of the enzyme aldolase B.
4. Pentose phosphate pathway disorders: These disorders affect the body's ability to metabolize certain sugars and generate energy through the pentose phosphate pathway. They are caused by defects in enzymes involved in this pathway.

Symptoms of inborn errors of carbohydrate metabolism can vary widely depending on the specific disorder and its severity. Treatment typically involves dietary restrictions, supplementation with necessary enzymes or cofactors, and management of complications. In some cases, enzyme replacement therapy or even organ transplantation may be considered.

Beta-N-Acetylhexosaminidases are a group of enzymes that play a role in the breakdown and recycling of complex carbohydrates in the body. Specifically, they help to break down gangliosides, which are a type of molecule found in cell membranes.

There are several different isoforms of beta-N-Acetylhexosaminidases, including A, B, and S. These isoforms are formed by different combinations of subunits, which can affect their activity and substrate specificity.

Mutations in the genes that encode for these enzymes can lead to a variety of genetic disorders, including Tay-Sachs disease and Sandhoff disease. These conditions are characterized by an accumulation of gangliosides in the brain, which can cause progressive neurological deterioration and death.

Treatment for these conditions typically involves managing symptoms and providing supportive care, as there is currently no cure. Enzyme replacement therapy has been explored as a potential treatment option, but its effectiveness varies depending on the specific disorder and the age of the patient.

Acetylgalactosamine (also known as N-acetyl-D-galactosamine or GalNAc) is a type of sugar molecule called a hexosamine that is commonly found in glycoproteins and proteoglycans, which are complex carbohydrates that are attached to proteins and lipids. It plays an important role in various biological processes, including cell-cell recognition, signal transduction, and protein folding.

In the context of medical research and biochemistry, Acetylgalactosamine is often used as a building block for synthesizing glycoconjugates, which are molecules that consist of a carbohydrate attached to a protein or lipid. These molecules play important roles in many biological processes, including cell-cell recognition, signaling, and immune response.

Acetylgalactosamine is also used as a target for enzymes called glycosyltransferases, which add sugar molecules to proteins and lipids. In particular, Acetylgalactosamine is the acceptor substrate for a class of glycosyltransferases known as galactosyltransferases, which add galactose molecules to Acetylgalactosamine-containing structures.

Defects in the metabolism of Acetylgalactosamine have been linked to various genetic disorders, including Schindler disease and Kanzaki disease, which are characterized by neurological symptoms and abnormal accumulation of glycoproteins in various tissues.

Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.

Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.

Endosomes are membrane-bound compartments within eukaryotic cells that play a critical role in intracellular trafficking and sorting of various cargoes, including proteins and lipids. They are formed by the invagination of the plasma membrane during endocytosis, resulting in the internalization of extracellular material and cell surface receptors.

Endosomes can be classified into early endosomes, late endosomes, and recycling endosomes based on their morphology, molecular markers, and functional properties. Early endosomes are the initial sorting stations for internalized cargoes, where they undergo sorting and processing before being directed to their final destinations. Late endosomes are more acidic compartments that mature from early endosomes and are responsible for the transport of cargoes to lysosomes for degradation.

Recycling endosomes, on the other hand, are involved in the recycling of internalized cargoes back to the plasma membrane or to other cellular compartments. Endosomal sorting and trafficking are regulated by a complex network of molecular interactions involving various proteins, lipids, and intracellular signaling pathways.

Defects in endosomal function have been implicated in various human diseases, including neurodegenerative disorders, developmental abnormalities, and cancer. Therefore, understanding the mechanisms underlying endosomal trafficking and sorting is of great importance for developing therapeutic strategies to treat these conditions.

Thin-layer chromatography (TLC) is a type of chromatography used to separate, identify, and quantify the components of a mixture. In TLC, the sample is applied as a small spot onto a thin layer of adsorbent material, such as silica gel or alumina, which is coated on a flat, rigid support like a glass plate. The plate is then placed in a developing chamber containing a mobile phase, typically a mixture of solvents.

As the mobile phase moves up the plate by capillary action, it interacts with the stationary phase and the components of the sample. Different components of the mixture travel at different rates due to their varying interactions with the stationary and mobile phases, resulting in distinct spots on the plate. The distance each component travels can be measured and compared to known standards to identify and quantify the components of the mixture.

TLC is a simple, rapid, and cost-effective technique that is widely used in various fields, including forensics, pharmaceuticals, and research laboratories. It allows for the separation and analysis of complex mixtures with high resolution and sensitivity, making it an essential tool in many analytical applications.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Fructose is a simple monosaccharide, also known as "fruit sugar." It is a naturally occurring carbohydrate that is found in fruits, vegetables, and honey. Fructose has the chemical formula C6H12O6 and is a hexose, or six-carbon sugar.

Fructose is absorbed directly into the bloodstream during digestion and is metabolized primarily in the liver. It is sweeter than other sugars such as glucose and sucrose (table sugar), which makes it a popular sweetener in many processed foods and beverages. However, consuming large amounts of fructose can have negative health effects, including increasing the risk of obesity, diabetes, and heart disease.

Flocculation is not a term that has a specific medical definition. However, it is a term that is used in various scientific and medical contexts to refer to the process of forming flocs or clumps. Flocs are aggregates of small particles that come together to form larger, visible clumps.

In medical contexts, flocculation may be used to describe the formation of clumps in biological samples such as urine or blood. For example, the presence of flocculent material in urine may indicate the presence of a protein abnormality or kidney disease. Similarly, flocculation of red blood cells may occur in certain medical conditions such as paroxysmal nocturnal hemoglobinuria (PNH), where red blood cells are susceptible to complement-mediated lysis and can form clumps in the blood.

Overall, while flocculation is not a term with a specific medical definition, it is a process that can have implications for various medical diagnoses and conditions.

"Galanthus" is not a medical term. It is the genus name for snowdrops, a type of small, white flowering plant that typically blooms in early spring. The name "Galanthus" comes from the Greek words "gala," meaning milk, and "anthos," meaning flower, referring to the plant's white, milk-like flowers.

Snowdrops have been used in traditional medicine in some cultures, but there is limited scientific evidence to support their effectiveness for any specific medical purpose. Some studies suggest that certain compounds found in snowdrops may have potential therapeutic benefits, such as anti-inflammatory and neuroprotective effects, but more research is needed before any definitive conclusions can be drawn.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Fructokinase is an enzyme that phosphorylates fructose into fructose-1-phosphate in the metabolism of dietary sugars. It plays a crucial role in fructose metabolism, particularly in the liver, kidneys, and intestines. In humans, there are several isoforms of fructokinase, including ketohexokinase (KHK-A and KHK-C) and liver fructokinase (KHK-B). Disorders in fructose metabolism, such as hereditary fructose intolerance, can result from mutations in the gene encoding for fructokinase.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

A cell wall is a rigid layer found surrounding the plasma membrane of plant cells, fungi, and many types of bacteria. It provides structural support and protection to the cell, maintains cell shape, and acts as a barrier against external factors such as chemicals and mechanical stress. The composition of the cell wall varies among different species; for example, in plants, it is primarily made up of cellulose, hemicellulose, and pectin, while in bacteria, it is composed of peptidoglycan.

The trans-Golgi network (TGN) is a structure in the cell's endomembrane system that is involved in the sorting and distribution of proteins and lipids to their final destinations within the cell or for secretion. It is a part of the Golgi apparatus, which consists of a series of flattened, membrane-bound sacs called cisternae. The TGN is located at the trans face (or "exit" side) of the Golgi complex and is the final stop for proteins that have been modified as they pass through the Golgi stacks.

At the TGN, proteins are sorted into different transport vesicles based on their specific targeting signals. These vesicles then bud off from the TGN and move to their respective destinations, such as endosomes, lysosomes, the plasma membrane, or secretory vesicles for exocytosis. The TGN also plays a role in the modification of lipids and the formation of primary lysosomes.

In summary, the trans-Golgi network is a crucial sorting and distribution center within the cell that ensures proteins and lipids reach their correct destinations to maintain proper cellular function.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

A ligand, in the context of biochemistry and medicine, is a molecule that binds to a specific site on a protein or a larger biomolecule, such as an enzyme or a receptor. This binding interaction can modify the function or activity of the target protein, either activating it or inhibiting it. Ligands can be small molecules, like hormones or neurotransmitters, or larger structures, like antibodies. The study of ligand-protein interactions is crucial for understanding cellular processes and developing drugs, as many therapeutic compounds function by binding to specific targets within the body.

Guanosine diphosphate sugars (GDP-sugars) are nucleotide sugars that play a crucial role in the biosynthesis of complex carbohydrates, such as glycoproteins and proteoglycans. Nucleotide sugars are formed by the attachment of a sugar molecule to a nucleoside diphosphate, in this case, guanosine diphosphate (GDP).

GDP-sugars serve as activated donor substrates for glycosyltransferases, enzymes that catalyze the transfer of sugar moieties onto various acceptor molecules, including proteins and lipids. The GDP-sugar synthesis pathway involves several enzymatic steps, starting with the conversion of nucleoside triphosphate (NTP) to nucleoside diphosphate (NDP), followed by the attachment of a sugar moiety from a donor molecule, such as UDP-glucose or TDP-rhamnose.

Examples of GDP-sugars include:

1. GDP-mannose: A nucleotide sugar that serves as a donor substrate for the addition of mannose residues to glycoproteins and proteoglycans.
2. GDP-fucose: A nucleotide sugar that is involved in the biosynthesis of fucosylated glycoconjugates, which have important functions in cell recognition, signaling, and development.
3. GDP-rhamnose: A nucleotide sugar that plays a role in the synthesis of rhamnosylated glycoconjugates, found in bacterial cell walls and some plant polysaccharides.
4. GDP-glucose: A nucleotide sugar that is used as a donor substrate for the addition of glucose residues to various acceptors, including proteins and lipids.

Dysregulation of GDP-sugar metabolism has been implicated in several diseases, such as cancer, neurodegenerative disorders, and bacterial and viral infections. Therefore, understanding the synthesis, regulation, and function of GDP-sugars is crucial for developing novel therapeutic strategies to target these conditions.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

Uridine Diphosphate N-Acetylglucosamine (UDP-GlcNAc) is not a medical term per se, but rather a biochemical term. It is a form of nucleotide sugar that plays a crucial role in several biochemical processes in the human body.

To provide a more detailed definition: UDP-GlcNAc is a nucleotide sugar that serves as a donor substrate for various glycosyltransferases involved in the biosynthesis of glycoproteins, proteoglycans, and glycolipids. It is a key component in the process of N-linked and O-linked glycosylation, which are important post-translational modifications of proteins that occur within the endoplasmic reticulum and Golgi apparatus. UDP-GlcNAc also plays a role in the biosynthesis of hyaluronic acid, a major component of the extracellular matrix.

Abnormal levels or functioning of UDP-GlcNAc have been implicated in various disease states, including cancer and diabetes. However, it is not typically used as a diagnostic marker or therapeutic target in clinical medicine.

Rhamnose is a naturally occurring sugar or monosaccharide, that is commonly found in various plants and some fruits. It is a type of deoxy sugar, which means it lacks one hydroxyl group (-OH) compared to a regular hexose sugar. Specifically, rhamnose has a hydrogen atom instead of a hydroxyl group at the 6-position of its structure.

Rhamnose is an essential component of various complex carbohydrates and glycoconjugates found in plant cell walls, such as pectins and glycoproteins. It also plays a role in bacterial cell wall biosynthesis and is used in the production of some antibiotics.

In medical contexts, rhamnose may be relevant to research on bacterial infections, plant-derived medicines, or the metabolism of certain sugars. However, it is not a commonly used term in clinical medicine.

The endoplasmic reticulum (ER) is a network of interconnected tubules and sacs that are present in the cytoplasm of eukaryotic cells. It is a continuous membranous organelle that plays a crucial role in the synthesis, folding, modification, and transport of proteins and lipids.

The ER has two main types: rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). RER is covered with ribosomes, which give it a rough appearance, and is responsible for protein synthesis. On the other hand, SER lacks ribosomes and is involved in lipid synthesis, drug detoxification, calcium homeostasis, and steroid hormone production.

In summary, the endoplasmic reticulum is a vital organelle that functions in various cellular processes, including protein and lipid metabolism, calcium regulation, and detoxification.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

A cation is a type of ion, which is a charged particle, that has a positive charge. In chemistry and biology, cations are formed when a neutral atom loses one or more electrons during chemical reactions. The removal of electrons results in the atom having more protons than electrons, giving it a net positive charge.

Cations are important in many biological processes, including nerve impulse transmission, muscle contraction, and enzyme function. For example, sodium (Na+), potassium (K+), calcium (Ca2+), and magnesium (Mg2+) are all essential cations that play critical roles in various physiological functions.

In medical contexts, cations can also be relevant in the diagnosis and treatment of various conditions. For instance, abnormal levels of certain cations, such as potassium or calcium, can indicate specific diseases or disorders. Additionally, medications used to treat various conditions may work by altering cation concentrations or activity within the body.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Xylose is a type of sugar that is commonly found in plants and wood. In the context of medical definitions, xylose is often used in tests to assess the function of the small intestine. The most common test is called the "xylose absorption test," which measures the ability of the small intestine to absorb this sugar.

In this test, a patient is given a small amount of xylose to drink, and then several blood and/or urine samples are collected over the next few hours. The amount of xylose that appears in these samples is measured and used to determine how well the small intestine is absorbing nutrients.

Abnormal results on a xylose absorption test can indicate various gastrointestinal disorders, such as malabsorption syndromes, celiac disease, or bacterial overgrowth in the small intestine.

Concanavalin A (Con A) is a type of protein known as a lectin, which is found in the seeds of the plant Canavalia ensiformis, also known as jack bean. It is often used in laboratory settings as a tool to study various biological processes, such as cell division and the immune response, due to its ability to bind specifically to certain sugars on the surface of cells. Con A has been extensively studied for its potential applications in medicine, including as a possible treatment for cancer and viral infections. However, more research is needed before these potential uses can be realized.

Sugar alcohols, also known as polyols, are carbohydrates that are chemically similar to sugar but have a different molecular structure. They occur naturally in some fruits and vegetables, but most sugar alcohols used in food products are manufactured.

The chemical structure of sugar alcohols contains a hydroxyl group (-OH) instead of a hydrogen and a ketone or aldehyde group, which makes them less sweet than sugar and have fewer calories. They are not completely absorbed by the body, so they do not cause a rapid increase in blood glucose levels, making them a popular sweetener for people with diabetes.

Common sugar alcohols used in food products include xylitol, sorbitol, mannitol, erythritol, and maltitol. They are often used as sweeteners in sugar-free and low-sugar foods such as candy, chewing gum, baked goods, and beverages.

However, consuming large amounts of sugar alcohols can cause digestive symptoms such as bloating, gas, and diarrhea, due to their partial absorption in the gut. Therefore, it is recommended to consume them in moderation.

Deoxy sugars, also known as deoxyriboses, are sugars that have one or more hydroxyl (-OH) groups replaced by a hydrogen atom. The most well-known deoxy sugar is deoxyribose, which is a component of DNA (deoxyribonucleic acid).

Deoxyribose is a pentose sugar, meaning it has five carbon atoms, and it differs from the related sugar ribose by having a hydrogen atom instead of a hydroxyl group at the 2' position. This structural difference affects the ability of DNA to form double-stranded helices through hydrogen bonding between complementary base pairs, which is critical for the storage and replication of genetic information.

Other deoxy sugars may also be important in biology, such as L-deoxyribose, a component of certain antibiotics, and various deoxyhexoses, which are found in some natural products and bacterial polysaccharides.

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Polyisoprenyl phosphates are a type of organic compound that play a crucial role in the biosynthesis of various essential biomolecules in cells. They are formed by the addition of isoprene units, which are five-carbon molecules with a branched structure, to a phosphate group.

In medical terms, polyisoprenyl phosphates are primarily known for their role as intermediates in the biosynthesis of dolichols and farnesylated proteins. Dolichols are long-chain isoprenoids that function as lipid carriers in the synthesis of glycoproteins, which are proteins that contain carbohydrate groups attached to them. Farnesylated proteins, on the other hand, are proteins that have been modified with a farnesyl group, which is a 15-carbon isoprenoid. This modification plays a role in the localization and function of certain proteins within the cell.

Abnormalities in the biosynthesis of polyisoprenyl phosphates and their downstream products have been implicated in various diseases, including cancer, neurological disorders, and genetic syndromes. Therefore, understanding the biology and regulation of these compounds is an active area of research with potential therapeutic implications.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Mitogen receptors are a type of cell surface receptor that become activated in response to the binding of mitogens, which are substances that stimulate mitosis (cell division) and therefore promote growth and proliferation of cells. The activation of mitogen receptors triggers a series of intracellular signaling events that ultimately lead to the transcription of genes involved in cell cycle progression and cell division.

Mitogen receptors include receptor tyrosine kinases (RTKs), G protein-coupled receptors (GPCRs), and cytokine receptors, among others. RTKs are transmembrane proteins that have an intracellular tyrosine kinase domain, which becomes activated upon ligand binding and phosphorylates downstream signaling molecules. GPCRs are seven-transmembrane domain proteins that activate heterotrimeric G proteins upon ligand binding, leading to the activation of various intracellular signaling pathways. Cytokine receptors are typically composed of multiple subunits and activate Janus kinases (JAKs) and signal transducer and activator of transcription (STAT) proteins upon ligand binding.

Abnormal activation of mitogen receptors has been implicated in the development and progression of various diseases, including cancer, autoimmune disorders, and inflammatory conditions. Therefore, understanding the mechanisms underlying mitogen receptor signaling is crucial for the development of targeted therapies for these diseases.

Immunologic receptors are specialized proteins found on the surface of immune cells that recognize and bind to specific molecules, known as antigens, on the surface of pathogens or infected cells. This binding triggers a series of intracellular signaling events that activate the immune cell and initiate an immune response.

There are several types of immunologic receptors, including:

1. T-cell receptors (TCRs): These receptors are found on the surface of T cells and recognize antigens presented in the context of major histocompatibility complex (MHC) molecules.
2. B-cell receptors (BCRs): These receptors are found on the surface of B cells and recognize free antigens in solution.
3. Pattern recognition receptors (PRRs): These receptors are found inside immune cells and recognize conserved molecular patterns associated with pathogens, such as lipopolysaccharides and flagellin.
4. Fc receptors: These receptors are found on the surface of various immune cells and bind to the constant region of antibodies, mediating effector functions such as phagocytosis and antibody-dependent cellular cytotoxicity (ADCC).

Immunologic receptors play a critical role in the recognition and elimination of pathogens and infected cells, and dysregulation of these receptors can lead to immune disorders and diseases.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Pinocytosis is a type of cellular process involving the ingestion and absorption of extracellular fluid and dissolved substances into a cell. It is a form of endocytosis, where the cell membrane surrounds and engulfs the extracellular fluid to form a vesicle containing the fluid and its contents within the cell cytoplasm.

In pinocytosis, the cell membrane invaginates and forms small vesicles (pinocytotic vesicles) that contain extracellular fluid and dissolved substances. These vesicles then detach from the cell membrane and move into the cytoplasm, where they fuse with endosomes or lysosomes to break down and digest the contents of the vesicle.

Pinocytosis is a non-selective process that allows cells to take up small amounts of extracellular fluid and dissolved substances from their environment. It plays an important role in various physiological processes, including nutrient uptake, cell signaling, and the regulation of extracellular matrix composition.

Glycoconjugates are a type of complex molecule that form when a carbohydrate (sugar) becomes chemically linked to a protein or lipid (fat) molecule. This linkage, known as a glycosidic bond, results in the formation of a new molecule that combines the properties and functions of both the carbohydrate and the protein or lipid component.

Glycoconjugates can be classified into several categories based on the type of linkage and the nature of the components involved. For example, glycoproteins are glycoconjugates that consist of a protein backbone with one or more carbohydrate chains attached to it. Similarly, glycolipids are molecules that contain a lipid anchor linked to one or more carbohydrate residues.

Glycoconjugates play important roles in various biological processes, including cell recognition, signaling, and communication. They are also involved in the immune response, inflammation, and the development of certain diseases such as cancer and infectious disorders. As a result, understanding the structure and function of glycoconjugates is an active area of research in biochemistry, cell biology, and medical science.

... mannose to prevent or treat UTIs. Mannose differs from glucose by inversion of the C-2 chiral center. Mannose displays a 4 C 1 ... α-Mannosidase Mannose receptor Mannan oligosaccharide-based nutritional supplements Rhamnose, 6-deoxy-L-mannose PTS Mannose- ... Mannose is a sugar monomer of the aldohexose series of carbohydrates. It is a C-2 epimer of glucose. Mannose is important in ... Mannose provides 2-5 kcal/g. It is partially excreted in the urine. The root of both "mannose" and "mannitol" is manna, which ...
Despite the similarities in mannose-binding between the mannose receptor and MBL, these differences suggest that mannose- ... As opposed to macrophages that use the mannose receptors for phagocytosis of particulate matter >200 nm, the mannose receptor ... binding by the mannose receptor evolved separately to that of other C-type lectins. Individually, the CRDs bind mannose with ... The mannose receptor is the only member of the family in which this domain is functional. The fibronectin type II repeat domain ...
In enzymology, a mannose isomerase (EC 5.3.1.7) is an enzyme that catalyzes the chemical reaction D-mannose ⇌ {\displaystyle \ ... The systematic name of this enzyme class is D-mannose aldose-ketose-isomerase. Other names in common use include D-mannose ... This enzyme participates in fructose and mannose metabolism. Palleroni NJ, Doudoroff M (January 1956). "Mannose isomerase of ... rightleftharpoons } D-fructose Hence, this enzyme has one substrate, D-mannose, and one product, D-fructose. This enzyme ...
... is a chemical compound involved in glycosylation. Maeda, Yusuke; Kinoshita, Taroh (2008). " ... "Dolichol-phosphate mannose synthase: Structure, function and regulation". Biochimica et Biophysica Acta (BBA) - General ...
The enzyme dolichylphosphate-mannose phosphodiesterase (EC 3.1.4.49) catalyzes the reaction dolichyl β-D-mannosyl phosphate + ... H2O ⇌ {\displaystyle \rightleftharpoons } dolichyl phosphate + D-mannose This enzyme belongs to the family of hydrolases, ...
I-cell disease Insulin-like growth factor 2 receptor Mannose Mannose 1-phosphate Alberts, Bruce; et al. (2002). Molecular ... Mannose-6-phosphate (M6P) is a molecule bound by lectin in the immune system. M6P is converted to fructose 6-phosphate by ... Mannose-6-Phosphate+Receptor at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Role of M6P in protein ... There, the M6P moiety is recognized and bound by mannose 6-phosphate receptor (MPR) proteins at pH 6.5-6.7. The M6P-tagged ...
GDP-mannose is essential in eukaryotes. GDP-mannose is produced from GTP and mannose-6-phosphate by the enzyme mannose-1- ... Guanosine diphosphate mannose or GDP-mannose is a nucleotide sugar that is a substrate for glycosyltransferase reactions in ... One of the enzymes from the family of nucleootidyl-transferases, GDP-Mannose Pyrophosphorylase (GDP-MP) is an pervasive enzyme ... Pomel, Sébastien; Mao, Wei; Ha-Duong, Tâp; Cavé, Christian; Loiseau, Philippe M. (2019-05-31). "GDP-Mannose Pyrophosphorylase: ...
... and mannose-6-phosphate (M6P). Mannose-6-phosphate isomerase may also enable the synthesis of GDP-mannose in eukaryotic ... Because mannose and glucose are stereoisomers at C2, which is crucial to the mechanism for both enzymes, PMI must allow extra ... Mannose-6 phosphate isomerase (MPI), alternately phosphomannose isomerase (PMI) (EC 5.3.1.8) is an enzyme which facilitates the ... MPI must convert an aldose (mannose) to a ketose (fructose), in addition to opening and closing the rings for these sugars. In ...
... diphospho-D-mannose, pyrophosphorylase), GDP-mannose pyrophosphorylase, guanosine 5'-diphospho-D-mannose pyrophosphorylase, ... GDP-mannose Thus, the two substrates of this enzyme are GTP and alpha-D-mannose 1-phosphate, whereas its two products are ... alpha-D-mannose-1-phosphate guanylyltransferase. Other names in common use include GTP-mannose-1-phosphate guanylyltransferase ... and mannose 1-phosphate guanylyltransferase (guanosine triphosphate). This enzyme participates in fructose and mannose ...
In enzymology, a GDP-mannose 6-dehydrogenase (EC 1.1.1.132) is an enzyme that catalyzes the chemical reaction GDP-D-mannose + 2 ... and guanosine diphospho-D-mannose dehydrogenase. This enzyme participates in fructose and mannose metabolism. This protein may ... The systematic name of this enzyme class is GDP-D-mannose:NAD+ 6-oxidoreductase. Other names in common use include guanosine ... 2 H+ The 3 substrates of this enzyme are GDP-D-mannose, NAD+, and H2O, whereas its 3 products are GDP-D-mannuronate, NADH, and ...
... mannose 6-phosphate) or phosphodiester (Man-phosphate-GlcNAc) Number of mannose 6-phosphate tags Location of the mannose 6- ... Domains 3, 5 and 9 have been found to bind to mannose 6-phosphate. Domains 3 and 9 can bind to mannose 6-phosphate with high ... Each monomer forms a 9 stranded β-barrel which can bind to a single mannose 6-phosphate residue. The CI-MPR and CD-MPR bind ... Mannose 6-phosphate receptors bind newly synthesized lysosomal hydrolases in the trans-Golgi network (TGN) and deliver them to ...
... is a protein that in humans is encoded by the MRC1 gene. The recognition of complex carbohydrate ... "Entrez Gene: Mannose receptor C-type 1". Retrieved 2018-10-15. DesJardin LE, Kaufman TM, Potts B, Kutzbach B, Yi H, Schlesinger ... Le Cabec V, Emorine LJ, Toesca I, Cougoule C, Maridonneau-Parini I (June 2005). "The human macrophage mannose receptor is not a ... The protein has been shown to bind high-mannose structures on the surface of potentially pathogenic viruses, bacteria, and ...
The systematic name of this enzyme class is GDP-mannose 3,5-epimerase. Other names in common use include GDP-D-mannose:GDP-L- ... In enzymology, a GDP-mannose 3,5-epimerase (EC 5.1.3.18) is an enzyme that catalyzes the chemical reaction GDP-mannose ⇌ {\ ... GDP-mannose, and two products, GDP-L-galactose and GDP-L-gulose Since only GDP-L-gulose (the C5-epimer of GDP-D-mannose) was ... Gevaert O, Van Overtveldt S, Da Costa M, Beerens K, Desmet T (2020). "GDP-altrose as novel product of GDP-mannose 3,5-epimerase ...
The chemical reaction of GDP-Mannose 4, 6-Dehydratase is as shown: GDP-mannose ↔ GDP-4-dehydro-6-deoxy-D-mannose + H2O The ... GDP-D-mannose dehydratase, GDP-D-mannose 4,6-dehydratase, GMD, and GDP-mannose 4,6-hydro-lyase. The enzyme is a part of the GDP ... GDP-D-mannose dehydratase, GDP-D-mannose 4,6-dehydratase, Gmd, and GDP-mannose 4,6-hydro-lyase. This enzyme participates in ... The enzyme GDP-Mannose 4, 6-Dehydratase is only present in one pathway that we know of. This pathway is the GDP-mannose- ...
GDP mannose phosphorylase Mannose 1-phosphate (guanosine diphosphate) guanylyltransferase GDP mannose phosphorylase GDP-mannose ... GDP-mannose Thus, the two substrates of this enzyme are GDP and alpha-D-mannose 1-phosphate, whereas its two products are ... alpha-D-mannose-1-phosphate guanylyltransferase. This enzyme participates in fructose and mannose metabolism. ... In enzymology, a mannose-1-phosphate guanylyltransferase (GDP) (EC 2.7.7.22) is an enzyme that catalyzes the chemical reaction ...
The mannose porter of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N ... The PTS Mannose-Fructose-Sorbose (Man) Family (TC# 4.A.6) is a group of multicomponent PTS systems that are involved in sugar ... As of this edit, this article uses content from "4.A.6 The PTS Mannose-Fructose-Sorbose (Man) Family", which is licensed in a ... Huber, F.; Erni, B. (1996-08-01). "Membrane topology of the mannose transporter of Escherichia coli K12". European Journal of ...
Other names in common use include NADPH-dependent mannose 6-phosphate reductase, mannose-6-phosphate reductase, 6- ... In enzymology, a mannose-6-phosphate 6-reductase (EC 1.1.1.224) is an enzyme that catalyzes the chemical reaction D-mannitol 1- ... and NADPH-mannose-6-P reductase. Rumpho ME, Edwards GE, Loescher WH (1983). "A pathway for photosynthetic carbon flow to ... whereas its 3 products are D-mannose 6-phosphate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, ...
The systematic name of this enzyme class is dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase. Other names in common ... In enzymology, a dolichyl-phosphate-mannose-protein mannosyltransferase (EC 2.4.1.109) is an enzyme that catalyzes the chemical ... the two substrates of this enzyme are dolichyl phosphate D-mannose and protein, whereas its two products are dolichyl phosphate ... "Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and ...
... are serine proteases involved in the complement system. Types include: MASP1 ... "The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond ... "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding ...
cation-dependent+mannose-6-phosphate+receptor at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e ( ... Kölsch H, Ptok U, Majores M, Schmitz S, Rao ML, Maier W, Heun R (2004). "Putative association of polymorphism in the mannose 6- ... The CD-MPR is one of two transmembrane proteins that bind mannose-6-phosphate (M6P) tags on acid hydrolase precursors in the ... Ghosh P, Dahms NM, Kornfeld S (March 2003). "Mannose 6-phosphate receptors: new twists in the tale". Nat. Rev. Mol. Cell Biol. ...
GDP-mannose:cellobiosyl-diphosphopolyprenol+alpha-mannosyltransferase at the U.S. National Library of Medicine Medical Subject ... GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase (EC 2.4.1.252, GumH, AceA, alpha1,3-mannosyltransferase ... Petroni EA, Ielpi L (August 1996). "Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-diphosphopolyprenol alpha- ... This enzyme catalyses the following chemical reaction GDP-mannose + D-Glc-beta-(1->4)-Glc-alpha-1-diphospho-ditrans,octacis- ...
GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+ The 3 substrates of this enzyme are GDP-6-deoxy-D-mannose, NAD+, and NADP+, ... In enzymology, a GDP-4-dehydro-6-deoxy-D-mannose reductase (EC 1.1.1.281) is an enzyme that catalyzes the chemical reaction GDP ... The systematic name of this enzyme class is GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming). Other names in ... This enzyme participates in fructose and mannose metabolism. Messner P; Graninger, M; Adam, G; Puchberger, M; Kosma, P; Zayni, ...
... the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum The activity of the intersecting mannose ... High-mannose-oligosaccharide+beta-1,4-N-acetylglucosaminyltransferase at the U.S. National Library of Medicine Medical Subject ... High-mannose-oligosaccharide beta-1,4-N-acetylglucosaminyltransferase (EC 2.4.1.197), uridine diphosphoacetylglucosamine- ... high-mannose-oligosaccharide beta-1,4-N-acetylglucosaminyltransferase) is an enzyme with systematic name UDP-N-acetyl-D- ...
Fischer, Emil; Hirschberger, Josef (1 January 1889). "Ueber Mannose. II". Berichte der Deutschen Chemischen Gesellschaft. 22 (1 ...
Another potential characterization of the CLRs can be into mannose receptors and asialoglycoprotein receptors. The mannose ... Specifically, mannose binding triggers recruitment of MBL-associated serine proteases (MASPs). The serine proteases activate ... It recognizes and binds to repeated mannose units on the surfaces of infectious agents and its activation triggers endocytosis ... Dommett RM, Klein N, Turner MW (September 2006). "Mannose-binding lectin in innate immunity: past, present and future". Tissue ...
"Mannose-binding lectin deficiency". Genetics Home Reference. U.S. National Library of Medicine. v t e (Articles with short ...
... cation-independent mannose-6-phosphate receptor; mannose receptor of macrophages; 180 Kd secretory phospholipase A2 receptor; ... Drickamer K, Taylor ME, Conary JT, Lennartz MR, Stahl PD (1990). "Primary structure of the mannose receptor contains multiple ... Kornfeld S (1992). "Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors". Annu. Rev. ...
Irvine, James Colquhoun; Moodie, Agnes Marion (1905). "CXLIV.-The alkylation of mannose". J. Chem. Soc., Trans. 87: 1462-1468. ...
... cation-independent mannose-6-phosphate receptor) and CD-MPR (cation-dependent mannose-6-phosphate receptor). In eukaryotes, O- ... Five mannose residues are then added to this structure. At this point, the partially finished core glycan is flipped across the ... The modification of an N-linked glycan with a mannose-6-phosphate residue serves as a signal that the protein to which this ... This core structure of N-linked glycans, thus, consists of 14 residues (3 glucose, 9 mannose, and 2 N-acetylglucosamine). Image ...
... mannose receptor), CD301, CD103. The mesoderm gives rise to myeloid progenitor cells, which further differentiate into ...
... mannose to prevent or treat UTIs. Mannose differs from glucose by inversion of the C-2 chiral center. Mannose displays a 4 C 1 ... α-Mannosidase Mannose receptor Mannan oligosaccharide-based nutritional supplements Rhamnose, 6-deoxy-L-mannose PTS Mannose- ... Mannose is a sugar monomer of the aldohexose series of carbohydrates. It is a C-2 epimer of glucose. Mannose is important in ... Mannose provides 2-5 kcal/g. It is partially excreted in the urine. The root of both "mannose" and "mannitol" is manna, which ...
Structure of PslG from Pseudomonas aeruginosa in complex with mannose ... Composed of a pentameric repeating unit of mannose, glucose, and rhamnose, the biosynthesis of Psl is proposed to occur via a ... PslG formed a complex with two mannose monosaccharides in this groove, consistent with binding data obtained from intrinsic ... and its complex with mannose were determined to 2.0 and 1.9 Å resolution, respectively. Despite a domain architecture and ...
Biosynthesis of mammalian O-mannosyl glycans is initiated by the transfer of mannose from mannose-P-Dol to serine or threonine ... Mannose type O-glycan biosynthesis - Reference pathway [ Pathway menu , Organism menu , Pathway entry , Show description , ... N00698 Mannose type O-glycan biosynthesis, Rib-ol-5P to CDP-Rib-ol ... N00627 Mannose type O-glycan biosynthesis, POMT to POMK * ...
FimH adhesin Q133N mutant-FimC chaperone complex with methyl-alpha-D-mannose ... All but one of the mutants examined had greatly diminished mannose-binding activity and had also lost the ability to bind human ... The binding activity of the mono-saccharide D-mannose was delineated from this of mannotriose (Man(alpha 1-3)[Man(alpha 1-6)] ... The residues in the FimH mannose-binding pocket were sequenced and found to be invariant in over 200 uropathogenic strains of E ...
CIL) offers product CLM-9394-PK D-Mannose (4-¹³C, 99%) ... Mannose; (+)-Mannose; D-(+)-Mannose; (3S,4S,5S,6R)-6-( ... SynonymsD-Mannose-1,2,3,4,5,6-13C6; Mannose; (+)-Mannose; D-(+)-Mannose; (3S,4S,5S,6R)-6-(Hydroxymethyl)oxane-2,3,4,5-tetrol; ( ...
D-Mannose Market. D-Mannose Market (Type - Powder, Tablet, and Capsule; Application - Dietary Supplements, Functional Food, ...
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D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a ... NOW® Pure D-Mannose has a caloric value of four calories per gram, which is similar to other sugars. Mannose exists in two ... Technically known as D-mannose, this is a simple, six-carbon sugar. Mannose naturally occurs as a monosaccharide, or a simple ... D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a ...
Daily Dietary Supplement Chewable with D-Mannose, Berry, 60 Count B00XNZQNTQ; Upc: 072959015404; Ean: 007295901540; ASIN: ... The Camels are taking you to the Uricalm Cranberry, Daily Dietary Supplement Chewable with D-Mannose, Berry, 60 Count ... Uricalm Cranberry, Daily Dietary Supplement Chewable with D-Mannose, Berry, 60 Count B00XNZQNTQ at Amazon , camelcamelcamel.com ...
METHODS: In 663 patients with RPL in whom we had results for HLA-DRB1 typing and plasma mannose-binding lectin (p-MBL) ... Dive into the research topics of A combination of the HLA-DRB1*03 phenotype and low plasma mannose-binding lectin predisposes ... T1 - A combination of the HLA-DRB1*03 phenotype and low plasma mannose-binding lectin predisposes to autoantibody formation in ... A combination of the HLA-DRB1*03 phenotype and low plasma mannose-binding lectin predisposes to autoantibody formation in women ...
Saunders, K., Nicely, N. I., Wiehe, K., (2017), Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against ... Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in ... Env immunizations elicited plasma antibodies that neutralized HIV-1 expressing only high-mannose glycans-a characteristic ... Thus, HIV-1 Env vaccination induced mannose-dependent antibodies with characteristics of V3-glycan bnAb precursors. ...
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... several other related mannose-specific plant lectins, and the monoclonal antibody 2G12, modestly resistant to the mannose- ... Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of ... Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of ... Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of ...
Simultaneous and rate-coordinated conversion of lignocellulose derived glucose, xylose, arabinose, mannose, and galactose into ... mannose, and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification ... mannose, and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification ... mannose, and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification ...
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Home » Molecular and computational analyses of genes involved in mannose 6-phosphate independent trafficking ... Molecular and computational analyses of genes involved in mannose 6-phosphate independent trafficking ... Molecular and computational analyses of genes involved in mannose 6-phosphate independent trafficking. ...
Protocol For Life Balance D-Mannose 500 mg supports a healthy urinary tract and bladder by maintaining a balanced mucosal ... D-Mannose 500 mg may be beneficial in providing normal urinary tract health when taken on a regular basis. ... Be the first to review "Protocol For Life Balance D-Mannose 500 mg, 90 Vegetable Capsules" Cancel reply. Your email address ... Protocol For Life Balance D-Mannose 500 mg assists with the support of a healthy environment inside the bladder by maintaining ...
Absorption of D-mannose Targets the Urinary Tract. D-mannose or mannose is the sugar, carbohydrate part of the plant that when ... D-mannose specifically rids the body of E.coli. The results of a Pub Med study done at NIH indicate that D-mannose can ... Best Uses of D-mannose. D-mannose is best used to treat UTIs when taken orally. You should take ½ teaspoon every two hours for ... D-mannose does not readily enter the blood stream. Some preliminary research has shown that 90% of mannose taken orally is ...
6 Probiotics Strains, Organic Prebiotics, D-Mannose and Cranberry. ... D-Mannose and proanthocyanadins from Pro Cran dOr™ - a pure, concentrated whole cranberry fruit powder - help protect a ... D-mannose is a monosaccharide (sugar) that naturally occurs in fruits including apples, blueberries, and cranberries. In ... ProCran is a potent, pure powder made from cranberry extract - an effective accompaniment to D-Mannose in helping prevent UTIs. ...
The cation-independent mannose 6-phosphate receptor and the low density lipoprotein receptor, both rapidly internalized from ... SA Green, RB Kelly; Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from ... Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to ...
Cranberry/d-Mannose combines cranberry extract and d-mannose for urinary tract functionality and health to help you find ... Cranberry/d-Mannose combines cranberry extract made from 100% cranberry fruit solids and d-mannose for both time-tested and ... Cranberry/d-Mannose combines cranberry extract and d-mannose for urinary tract functionality and health to help you find ... Cranberry-d-Mannose has been added to your list successfully. See all your saved products in your account. ...
Why Utiva D-Mannose?. *D-Mannose is trusted by healthcare practitioners as an effective option to help stop infections before ...
D-Mannose is a simple sugar with a low glycemic index which, once taken, is eliminated through the kidneys, concentrating ... Thanks to its protective action on uroepithelial cells, D-mannose represents a natural and safe alternative for the control of ...
... Name:D(+)-Mannose. CAS NO. :3458-28-4. 【Pre】 1,2,4-Butanetriol 【Next】6-deoxy-L-mannose. ...
These species were identified in the process of characterizing mannose 6-phosphate/insulin-like growth factor II (M-6-P/IGF-II ... We have identified a novel class of peptides bound to MHC class II: mannose 6- phosphate (Man-6-P) containing glycopeptides ... A mannose 6-phosphate-containing N-linked glycopeptide derived from lysosomal acid lipase is bound to MHC class II in B ... A mannose 6-phosphate-containing N-linked glycopeptide derived from lysosomal acid lipase is bound to MHC class II in B ...
2014, Institute for Systems Biology, All Rights Reserved ...
D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a ... D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a ... D-mannose promotes normal urinary tract function by cleansing and maintaining the health of the bladder lining.* ...
  • Now D-Mannose Powder Reviews - Is This Product Legit & Worth? (consumerhealthdigest.com)
  • Now, D-Mannose Powder is a supplement created to support the health of your urinary tract. (consumerhealthdigest.com)
  • Now D-Mannose Powder is a product which is intended to help you with the functioning of your urinary tract. (consumerhealthdigest.com)
  • Now D-Mannose Powder Review - Does It Really Work? (consumerhealthdigest.com)
  • Now D-Mannose Powder Ingredients - Are they Safe & Effective? (consumerhealthdigest.com)
  • ProCran is a potent, pure powder made from cranberry extract - an effective accompaniment to D-Mannose in helping prevent UTIs. (physicianschoice.com)
  • D-Mannose and proanthocyanadins from Pro Cran d'Or™ - a pure, concentrated whole cranberry fruit powder - help protect a healthy urinary tract. (physicianschoice.com)
  • Available in powder form, D‑Mannose & Cranberry is formulated as a way to help prevent urinary tract infections (UTIs). (thepeanutmill.com)
  • Mannose One is an unflavored d-mannose powder to support urinary tract health. (theralogix.com)
  • citation needed] While much of the mannose used in glycosylation is believed to be derived from glucose, in cultured hepatoma cells (cancerous cells from the liver), most of the mannose for glycoprotein biosynthesis comes from extracellular mannose, not glucose. (wikipedia.org)
  • Mannose-6-phosphate is converted to fructose-6-phosphate, by the enzyme phosphomannose isomerase, and then enters the glycolytic pathway or is converted to glucose-6-phosphate by the gluconeogenic pathway of hepatocytes. (wikipedia.org)
  • Glucose is hydrolyzed on fully folded protein and the mannose moieties are hydrolyzed by ER and Golgi-resident mannosidases. (wikipedia.org)
  • Mannose differs from glucose by inversion of the C-2 chiral center. (wikipedia.org)
  • Composed of a pentameric repeating unit of mannose, glucose, and rhamnose, the biosynthesis of Psl is proposed to occur via a Wzx/Wzy-dependent mechanism. (rcsb.org)
  • This study showed a simultaneous and rate-coordinated conversion of lignocellulose derived glucose, xylose, arabinose, mannose, and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification and co-fermentation (SSCF) of wheat straw. (lu.se)
  • D-mannose is a simple sugar, similar to glucose, that is derived naturally from fruits and some plants. (healthfully.com)
  • The body uses only small amounts of D-mannose for metabolism, the rest of it is rapidly excreted in the urine, leaving the blood glucose levels unaffected. (herbal.ee)
  • Although d-mannose is a type of sugar, it is metabolized differently than glucose, so it does not raise blood sugar levels. (theralogix.com)
  • The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. (ntu.edu.sg)
  • Each serving contains 2,000 mg of D-Mannose. (drvitaminsolutions.com)
  • Contains 2,000 mg of d-mannose, the research-backed dose to flush bacteria from the urinary tract. (theralogix.com)
  • citation needed] Mannose is a dominant monosaccharide in N-linked glycosylation, which is a post-translational modification of proteins. (wikipedia.org)
  • Our structure/function analysis demonstrated that the binding of the monosaccharide alpha-D-mannose is the primary bladder cell receptor for uropathogenic E. coli and that this event requires a highly conserved FimH binding pocket. (rcsb.org)
  • Mannose naturally occurs as a monosaccharide, or a simple sugar, in fruits such as blueberries and cranberries, as well as in other plants and fungi. (healthy.co.nz)
  • D-mannose is a monosaccharide (sugar) that naturally occurs in fruits including apples, blueberries, and cranberries. (physicianschoice.com)
  • I started the D-mannose and cranberry capsules after Thumper had his second round of a UTI. (shoppettest.com)
  • Relieve urinary tract discomfort and boost your immune system with Organic D-Mannose & Cranberry Capsules. (cnpusa.com)
  • NOW® Pure D-Mannose has a caloric value of four calories per gram, which is similar to other sugars. (healthy.co.nz)
  • Well, the sugars in D-mannose are the specific components in cranberry juice that act as antibacterial agents. (healthfully.com)
  • Therefore, D-mannose is not metabolized like other sugars in the body, it does not alter blood sugar levels and the plant components are filtered directly into the bladder. (healthfully.com)
  • The sugars in D-mannose coat the lining of the urinary tract and bladder as they pass through the body. (healthfully.com)
  • citation needed] Mannose (D-mannose) is used as a dietary supplement to prevent recurrent urinary tract infections (UTIs). (wikipedia.org)
  • As of 2022[update], one review found that taking mannose was as effective as antibiotics to prevent UTIs, while another review found that clinical trial quality was too low to allow any conclusion about using D‐mannose to prevent or treat UTIs. (wikipedia.org)
  • D-mannose is best used to treat UTIs when taken orally. (healthfully.com)
  • A bundle with the 2 main active ingredients to help prevent UTIs - Cranberry PACs & D-Mannose. (utivahealth.ca)
  • D-Mannose helps target E. coli effectively to promote natural flushing and prevent trigger-associated UTIs. (utivahealth.ca)
  • PetTest D-Mannose is a dietary supplement used for preventing urinary tract infections (UTIs). (shoppettest.com)
  • Coby started using D-mannose and, to her surprise and relief, discovered it managed to keep UTIs at bay. (dmannose.info)
  • Mannose XYZ permease is a member of the family, with this distinct method being used by bacteria for sugar uptake particularly exogenous hexoses in the case of mannose XYZ to release the phosphate esters into the cell cytoplasm in preparation for metabolism primarily through the route of glycolysis. (wikipedia.org)
  • Only enterohaemorrhagic E. coli (EHEC) possess a sequence variation within the mannose-binding pocket of FimH, suggesting a naturally occurring mechanism of attenuation in EHEC bacteria that would prevent them from being targeted to the urinary tract. (rcsb.org)
  • The results of a Pub Med study done at NIH indicate that D-mannose can significantly reduce bacteria in the urine within one day of use. (healthfully.com)
  • In addition, D-mannose is the food for lactic acid bacteria, therefore promoting the growth of colonies of beneficial bacteria in the gut. (herbal.ee)
  • Cranberry PACs are understood to address a variety of bacteria and D-Mannose is known to target E.coli. (utivahealth.ca)
  • Utiva provides a pure source of D-Mannose that has shown benefits in maintaining a healthy urinary tract by stopping bacteria from sticking. (utivahealth.ca)
  • D‑Mannose & Cranberry will help rebuild a proper intestinal fauna, which will help keep harmful bacteria from colonizing the gastrointestinal tract. (thepeanutmill.com)
  • Each convenient packet of Mannose One provides 2000 mg of d-mannose, the research-backed dose to flush bacteria from the urinary tract. (theralogix.com)
  • Both cranberry proanthocyanidins (PACs) in TheraCran One and d-mannose in Mannose One prevent certain bacteria from sticking to the urinary tract. (theralogix.com)
  • The plant lectins from Hippeastrum hybrid (HHA) and Galanthus nivalis (GNA) are 50,000-D tetramers showing specificity for α-(1,3) and/or α-(1,6)-mannose oligomers. (aspetjournals.org)
  • Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) and Langerin are C-type lectins of dendritic cells (DCs) that share a specificity for mannose and are involved in pathogen recognition. (uea.ac.uk)
  • Mannose-Binding Lectins as Potent Antivirals against SARS-CoV-2. (bvsalud.org)
  • Here, we evaluated the in vitro anti- SARS-CoV-2 activity of two mannose-binding lectins isolated from the Brazilian plants Canavalia brasiliensis and Dioclea violacea (ConBR and DVL). (bvsalud.org)
  • d-Mannose, a simple sugar found in cranberries and other fruit, is included in this formula to provide concentrated support. (pureprescriptions.com)
  • Cranberries have been used as a medicinal agent for centuries to promote health but recently the scientific literature has proven that proanthocyanidins contained in cranberries as well as a simple sugar ᴅ‑mannose specifically inhibit the adhesion and proliferation of E. coli in the urinary tract. (vitamintree.ca)
  • D-Mannose is a simple sugar found naturally in cranberries, pineapple, and other plant sources. (abundantvitamins.com)
  • Dus wil jij jouw lichaam met cranberries wat extra's geven, dan is Solaray D-Mannose met CranActin wat voor jou! (solaray.co.uk)
  • d-Mannose is a simple sugar found naturally in cranberries and pineapples, which can now be consumed from an easily dissolvable powdered form to help support a healthy urinary tract. (yourholisticdoc.com)
  • Cranberry/d-Mannose combines cranberry extract made from 100% cranberry fruit solids and d-mannose for both time-tested and concentrated support of urinary tract comfort. (pureprescriptions.com)
  • Cranberry/d-Mannose combines cranberry extract and d-mannose for urinary tract functionality and health to help you find urinary tract comfort. (drhyman.com)
  • The first step in the colonization of the human urinary tract by pathogenic Escherichia coli is the mannose-sensitive binding of FimH, the adhesin present at the tip of type 1 pili, to the bladder epithelium. (rcsb.org)
  • The residues in the FimH mannose-binding pocket were sequenced and found to be invariant in over 200 uropathogenic strains of E. coli. (rcsb.org)
  • D-mannose specifically rids the body of E.coli. (healthfully.com)
  • If you are suffering from a UTI D-mannose can effectively be used as a natural antibiotic against E.coli. (healthfully.com)
  • Thanks to its protective action on uroepithelial cells, D-mannose represents a natural and safe alternative for the control of urinary tract infections and infectious cystitis, inhibiting the adhesion of Escherichia coli, the main bacterium responsible for urinary infections, on uroepithelial cells. (rialpharma.it)
  • Cranberry extracts and ᴅ‑mannose each independently inhibit one of two adhesion methods utilized by E. coli. (vitamintree.ca)
  • Combined together in a synergistic and novel formula D‑Mannose SAP addresses both type-1 (FimH) and P-type fimbrial-mediated adhesion by E. coli to the urinary tract mucosa. (vitamintree.ca)
  • D‑Mannose SAP is specifically targeted for the treatment and prevention of E. coli UTI. (vitamintree.ca)
  • D-Mannose With Cranberry and Probiotics provides relief from urinary tract infections often caused by E. coli infection. (thepeanutmill.com)
  • We show here for the first time that glycomimetics based on a mannose anchor can be tuned to selectively inhibit DC-SIGN over Langerin. (uea.ac.uk)
  • The particular components in D-mannose and its method of absorption in the body make it beneficial in treating infections in the bladder and urinary tract. (healthfully.com)
  • Drink eight to ten glasses of water a day when taking D-mannose for a UTI to increase flushing through the bladder and urinary tract. (healthfully.com)
  • D-mannose is a natural sugar that helps keep the bladder and urinary tract healthy. (herbal.ee)
  • D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a healthy bladder lining. (healthy.co.nz)
  • Made purely of organic d-mannose and cranberry, they help flush and cleanse your urinary tract, promoting a healthier overall urinary system. (cnpusa.com)
  • How is Mannose One different than other d-mannose supplements? (theralogix.com)
  • Does Mannose One interact with any dietary supplements or prescription medications? (theralogix.com)
  • Typically, mature human glycoproteins only contain three mannose residues buried under sequential modification by GlcNAc, galactose, and sialic acid. (wikipedia.org)
  • This is important, as the innate immune system in mammals is geared to recognise exposed mannose residues. (wikipedia.org)
  • This activity is due to the prevalence of mannose residues, in the form of mannans, on the surfaces of yeasts. (wikipedia.org)
  • The human immunodeficiency virus displays considerable amount of mannose residues due to the tight clustering of glycans in its viral spike. (wikipedia.org)
  • These mannose residues are the target for broadly neutralizing antibodies. (wikipedia.org)
  • Clinical studies have demonstrated that, when taken regularly, D-mannose promotes normal urinary tract function by cleansing and maintaining the health of the bladder lining. (healthy.co.nz)
  • D-Mannose 500 mg may be beneficial in providing normal urinary tract health when taken on a regular basis. (drvitaminsolutions.com)
  • Although small amounts of D-Mannose are metabolized by the human body, most of it is rapidly excreted in the urine. (vitaminlife.com)
  • Some preliminary research has shown that 90% of mannose taken orally is excreted in the urine unchanged within 30-60 minutes. (healthfully.com)
  • One study examining the effect of d-mannose on epithelial cells suggested that it may play a role in supporting healthy genitourinary function by maintaining a healthy mucosal surface. (pureprescriptions.com)
  • Protocol For Life Balance D-Mannose 500 mg assists with the support of a healthy environment inside the bladder by maintaining a balanced mucosal lining and encouraging proper disposal. (drvitaminsolutions.com)
  • As it is flushed out of the body, D-Mannose maintains a healthy environment for the mucosal surface of the urinary tract. (abundantvitamins.com)
  • It is initiated by the en bloc transfer on Glc3Man9GlcNAc2 to nascent glycoproteins in the endoplasmic reticulum in a co-translational manner as the protein entered through the transport system. (wikipedia.org)
  • To understand the function of this protein, the apo-structure of the periplasmic domain of PslG (PslG(31-442)) and its complex with mannose were determined to 2.0 and 1.9 Å resolution, respectively. (rcsb.org)
  • The cation-independent mannose 6-phosphate receptor and the low density lipoprotein receptor, both rapidly internalized from the cell surface, and the synaptic vesicle membrane protein synaptophysin, were transported to the Golgi apparatus with equivalent, nonlinear kinetics. (rupress.org)
  • it occurs when mannose-binding lectin (MBL), a serum protein, binds to mannose, fucose, or N -acetylglucosamine groups on bacterial cell walls, yeast walls, or viruses. (msdmanuals.com)
  • They are activated when complexed with the MANNOSE-BINDING LECTIN, therefore also known as Mannose-binding protein-Associated Serine Proteases (MASPs). (bvsalud.org)
  • To determine whether immunization could induce antibodies to the V3-glycan bnAb binding site, we repetitively immunized macaques over a 4-year period with an Env expressing V3-high mannose glycans. (ku.edu)
  • Env immunizations elicited plasma antibodies that neutralized HIV-1 expressing only high-mannose glycans-a characteristic shared by early bnAb B cell lineage members. (ku.edu)
  • A structure of the antibody bound to glycan revealed that the three variable heavy-chain complementarity-determining regions formed a cavity into which glycan could insert and neutralized multiple HIV-1 isolates with high-mannose glycans. (ku.edu)
  • D-Mannose is a simple sugar that occurs naturally in some plants. (vitaminlife.com)
  • We have identified a novel class of peptides bound to MHC class II: mannose 6- phosphate (Man-6-P) containing glycopeptides from lysosomal enzymes. (ox.ac.uk)
  • It galactose, Dcarabinose, Dcxylose and Dc should be made clear to the public that swalc mannose. (who.int)
  • Mannose is a sugar monomer of the aldohexose series of carbohydrates. (wikipedia.org)
  • citation needed] The digestion of many polysaccharides and glycoproteins yields mannose, which is phosphorylated by hexokinase to generate mannose-6-phosphate. (wikipedia.org)
  • A mannose 6-phosphate-containing N-linked glycopeptide derived from lysosomal acid lipase is bound to MHC class II in B lymphoblastoid cell lines. (ox.ac.uk)
  • These species were identified in the process of characterizing mannose 6-phosphate/insulin-like growth factor II (M-6-P/IGF-II) receptor binding to the surface of B lymphoblasts. (ox.ac.uk)
  • Mannose is important in human metabolism, especially in the glycosylation of certain proteins. (wikipedia.org)
  • Several congenital disorders of glycosylation are associated with mutations in enzymes involved in mannose metabolism. (wikipedia.org)
  • Thus, HIV-1 Env vaccination induced mannose-dependent antibodies with characteristics of V3-glycan bnAb precursors. (ku.edu)
  • Met D-Mannose, een suikervorm die natuurlijk voorkomt in fruit, en toegevoegde vitamine C. En dan is Solaray D-Mannose met CranActin ook nog eens vegan en glutenvrij! (solaray.co.uk)
  • Research shows that d-mannose helps flush the urinary tract and supports overall urinary tract health. (theralogix.com)
  • D-Mannose defends the UT lining, aids digestive support, and encourages healthy urine flow & inflammation relief. (shoppettest.com)
  • D-Mannose is a simple sugar with a low glycemic index which, once taken, is eliminated through the kidneys, concentrating selectively in the urinary tract. (rialpharma.it)
  • Plus, Mannose One is the only d-mannose supplement certified by NSF International for content accuracy and purity. (theralogix.com)
  • D-mannose or mannose is the sugar, carbohydrate part of the plant that when ingested is not well absorbed by the human body. (healthfully.com)
  • The only d-mannose supplement independently tested and certified by NSF International. (theralogix.com)
  • The product promises to handle all this through using nothing but D-Mannose, which is nothing but a sugar. (consumerhealthdigest.com)
  • Technically known as D-mannose, this is a simple, six-carbon sugar. (healthy.co.nz)
  • Because insubstantial amounts of D-Mannose are used by the body, it does not interfere with healthy blood sugar regulation. (vitaminlife.com)
  • D-mannose is a natural sugar (also known as gluco-nutrient, i.e. healthy sugar). (herbal.ee)
  • D-mannose is a sugar found in fruits and vegetables, and it's also naturally occurring within the body. (theralogix.com)
  • When taken at the recommended daily dose, Mannose One should not affect blood sugar levels. (theralogix.com)
  • Many of the glycoproteins produced in the liver are secreted into the bloodstream, so dietary mannose is distributed throughout the body. (wikipedia.org)
  • The natural manufacturing methods for mannose result in a mixture of these two forms, yielding a product that is mildly sweet with a slight bitter aftertaste. (healthy.co.nz)
  • Cranberry D-Mannose for dogs and cats is a natural solution to help support and maintain the healthy and normal function of the urinary tract system. (shoppettest.com)
  • JerdaPharma Glucosamine is composed of 100% natural D-Mannose. (pharmahorse.eu)