Mannose
Mannose-Binding Lectins
Receptor, IGF Type 2
Guanosine Diphosphate Mannose
Dolichol Monophosphate Mannose
Oligosaccharides
Mannosyltransferases
Mannose-6-Phosphate Isomerase
Lectins, C-Type
Carbohydrates
Polyisoprenyl Phosphate Sugars
Receptors, Cell Surface
Mannosides
Carbohydrate Sequence
Monosaccharides
Glycoproteins
Glycosylation
alpha-Mannosidase
Polyisoprenyl Phosphate Monosaccharides
Galactose
Glycopeptides
Lectins
Lysosomes
Methylmannosides
Molecular Sequence Data
Phosphotransferases (Phosphomutases)
Cathepsin D
Carbohydrate Metabolism
Mannose-Binding Lectin
Polyisoprenyl Phosphate Oligosaccharides
Hexosaminidases
beta-Mannosidase
Swainsonine
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Endocytosis
Plant Lectins
Glycolipids
Dolichol
Phosphoenolpyruvate Sugar Phosphotransferase System
Golgi Apparatus
Collectins
Amino Acid Sequence
Tunicamycin
Congenital Disorders of Glycosylation
1-Deoxynojirimycin
Glucose
Chromatography, Paper
Mucolipidoses
Chromatography, Affinity
Insulin-Like Growth Factor II
Macrophages
Chromatography, Gel
Asparagine
Glycosylphosphatidylinositols
Acetylglucosaminidase
Electrophoresis, Polyacrylamide Gel
Biological Transport
Cricetinae
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
beta-N-Acetylhexosaminidases
alpha-Glucosidases
Endosomes
Chromatography, Thin Layer
Protein Processing, Post-Translational
Cell Membrane
Fructose
Transferases (Other Substituted Phosphate Groups)
Galanthus
Amino Acids
Fructokinases
Liver
Carrier Proteins
Cell Wall
trans-Golgi Network
Cells, Cultured
Ligands
Guanosine Diphosphate Sugars
Protein Binding
Uridine Diphosphate N-Acetylglucosamine
Rhamnose
Endoplasmic Reticulum
Mutation
Cations
Concanavalin A
Sugar Alcohols
Fibroblasts
Binding Sites
Substrate Specificity
Cattle
Magnetic Resonance Spectroscopy
Receptors, Mitogen
Receptors, Immunologic
Chromatography, Ion Exchange
Pinocytosis
Glycoconjugates
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)CDGs are caused by mutations in genes that code for enzymes involved in glycosylation, a process that adds sugars to proteins and lipids to form glycoproteins and glycolipids. These molecules play important roles in cell signaling, protein folding, and the immune response. Without proper glycosylation, these molecules cannot function properly, leading to a wide range of symptoms and complications.
Symptoms of CDGs can vary depending on the specific disorder and the organs affected. Common symptoms include developmental delays, intellectual disability, seizures, poor muscle tone, and liver problems. Some children with CDGs may also experience failure to thrive, diarrhea, and vomiting.
There is currently no cure for CDGs, but various treatments are available to manage the symptoms and prevent complications. These may include enzyme replacement therapy, nutritional supplements, and medications to control seizures and other symptoms. In some cases, a bone marrow transplant may be necessary to replace the defective cells with healthy ones.
The diagnosis of CDG is based on a combination of clinical symptoms, laboratory tests, and genetic analysis. Newborn screening is increasingly being used to identify CDGs in infants, allowing for early intervention and treatment.
Overall, congenital disorders of glycosylation are rare and complex conditions that require specialized care and management. With advances in medical technology and research, there is hope for improved treatments and outcomes for individuals with CDGs.
The term "mucolipidoses" was coined by the American pediatrician and medical geneticist Dr. Victor A. McKusick in the 1960s to describe this group of diseases. The term is derived from the Greek words "muco-," meaning mucus, and "-lipido-," meaning fat, and "-osis," meaning condition or disease.
There are several types of mucolipidoses, including:
1. Mucolipidosis type I (MLI): This is the most common form of the disorder and is caused by a deficiency of the enzyme galactocerebrosidase (GALC).
2. Mucolipidosis type II (MLII): This form of the disorder is caused by a deficiency of the enzyme sulfatases, which are necessary for the breakdown of sulfated glycosaminoglycans (sGAGs).
3. Mucolipidosis type III (MLIII): This form of the disorder is caused by a deficiency of the enzyme acetyl-CoA:beta-glucoside ceramide beta-glucosidase (CERBGL), which is necessary for the breakdown of glycosphingolipids.
4. Mucolipidosis type IV (MLIV): This form of the disorder is caused by a deficiency of the enzyme glucocerebrosidase (GUCB), which is necessary for the breakdown of glucocerebroside, a type of glycosphingolipid.
Mucolipidoses are usually diagnosed by measuring the activity of the enzymes involved in glycosphingolipid metabolism in white blood cells or fibroblasts, and by molecular genetic analysis to identify mutations in the genes that code for these enzymes. Treatment is typically focused on managing the symptoms and may include physical therapy, speech therapy, and other supportive care measures. Bone marrow transplantation has been tried in some cases as a potential treatment for mucolipidosis, but the outcome has been variable.
Prognosis: The prognosis for mucolipidoses is generally poor, with most individuals with the disorder dying before the age of 10 years due to severe neurological and other complications. However, with appropriate management and supportive care, some individuals with milder forms of the disorder may survive into adulthood.
Epidemiology: Mucolipidoses are rare disorders, with an estimated prevalence of 1 in 100,000 to 1 in 200,000 births. They affect both males and females equally, and there is no known geographic or ethnic predilection.
Clinical features: The clinical features of mucolipidoses vary depending on the specific type of disorder and the severity of the mutation. Common features include:
* Delayed development and intellectual disability
* Seizures
* Vision loss or blindness
* Hearing loss or deafness
* Poor muscle tone and coordination
* Increased risk of infections
* Coarsening of facial features
* Enlarged liver and spleen
* Abnormalities of the heart, including ventricular septal defect and atrial septal defect
Diagnosis: Diagnosis of mucolipidoses is based on a combination of clinical features, laboratory tests, and genetic analysis. Laboratory tests may include measurement of enzyme activity in white blood cells, urine testing, and molecular genetic analysis.
Treatment and management: There is no cure for mucolipidoses, but treatment and management strategies can help manage the symptoms and improve quality of life. These may include:
* Physical therapy to improve muscle tone and coordination
* Speech therapy to improve communication skills
* Occupational therapy to improve daily living skills
* Anticonvulsant medications to control seizures
* Supportive care to manage infections and other complications
* Genetic counseling to discuss the risk of inheritance and options for family planning.
Prognosis: The prognosis for mucolipidoses varies depending on the specific type and severity of the condition. In general, the prognosis is poor for children with more severe forms of the disorder, while those with milder forms may have a better outlook. With appropriate management and supportive care, some individuals with mucolipidoses can lead relatively normal lives, while others may require ongoing medical care and assistance throughout their lives.
Examples of inborn errors of carbohydrate metabolism include:
1. Phosphofructokinase (PFK) deficiency: This is a rare genetic disorder that affects the body's ability to break down glucose-6-phosphate, a type of sugar. Symptoms can include seizures, developmental delays, and metabolic acidosis.
2. Galactosemia: This is a group of genetic disorders that affect the body's ability to process galactose, a type of sugar found in milk and other dairy products. Untreated, galactosemia can lead to serious health problems, including liver disease, kidney damage, and cognitive impairment.
3. Glycogen storage disease type II (GSDII): This is a rare genetic disorder that affects the body's ability to store and use glycogen, a complex carbohydrate found in the liver and muscles. Symptoms can include low blood sugar, fatigue, and muscle weakness.
4. Pompe disease: This is a rare genetic disorder that affects the body's ability to break down glycogen. Symptoms can include muscle weakness, breathing problems, and heart problems.
5. Mucopolysaccharidoses (MPS): These are a group of genetic disorders that affect the body's ability to break down sugar molecules. Symptoms can include joint stiffness, developmental delays, and heart problems.
Inborn errors of carbohydrate metabolism can be diagnosed through blood tests, urine tests, and other diagnostic procedures. Treatment depends on the specific disorder and may involve a combination of dietary changes, medication, and other therapies.
Mannose
Mannose receptor
Mannose isomerase
Dolichylphosphate-mannose phosphodiesterase
Mannose 6-phosphate
Guanosine diphosphate mannose
Mannose phosphate isomerase
Mannose-1-phosphate guanylyltransferase
GDP-mannose 6-dehydrogenase
Mannose 6-phosphate receptor
Mannose receptor C-type 1
GDP-mannose 3,5-epimerase
GDP-mannose 4,6-dehydratase
Mannose-1-phosphate guanylyltransferase (GDP)
PTS Mannose-Fructose-Sorbose Family
Mannose-6-phosphate 6-reductase
Dolichyl-phosphate-mannose-protein mannosyltransferase
Mannose-binding protein-associated serine protease
Cation-dependent mannose-6-phosphate receptor
GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase
GDP-4-dehydro-6-deoxy-D-mannose reductase
High-mannose-oligosaccharide beta-1,4-N-acetylglucosaminyltransferase
Enantioselective synthesis
Pattern recognition receptor
MBL deficiency
Fibronectin type II domain
Agnes Marion Moodie
Glycan
Pancreatic islet macrophage
Congenital disorder of glycosylation
Mannose-binding lectin deficiency: MedlinePlus Genetics
RCSB PDB - 6DDU: mouse beta-mannosidase bound to beta-D-mannose (MANBA)
Dietary sugars inhibit biologic functions of the pattern recognition molecule, mannose-binding lectin
Pages that link to "Mannose" - wikidoc
D-Mannose Special
Translocation of the yeast dolichol-phosphate-mannose synthase into microsomal membranes
Association between Mannose-Binding Lectin Polymorphisms and Wuchereria bancrofti Infection in Two Communities in North-Eastern...
Women's Probiotics with Prebiotics, D-Mannose & Cranberry | Physician's Choice
Expression of the two mannose 6-phosphate receptors is spatially and temporally different during mouse embryogenesis |...
D Mannose
First small molecular inhibitors of T. brucei dolicholphosphate mannose synthase (DPMS), a validated drug target in African...
GDP-Mannose pyrophosphorylase | Chemily Glycoscience
Network Portal - Function mannose-phosphate guanylyltransferase activity
Solaray D-Mannose with CranActin - 120 Capsules
D-Mannose with Cranberry- (60 Capsules) | Sprout Supplements
D-mannose - for a healthy bladder with Vagiflor® cystimed
Cranberry & D Mannose - Biotex Life | Invest in your life!
D-Mannose & Cranberry Extract Capsules | Complete UT Health - HR Supplements
Now D-Mannose 500mg - The Water Bug Health Food Store
Regulatory effect of Pseudomonas aeruginosa mannose-sensitive hemagglutinin on inflammation and immune function in percutaneous...
UT Answer Cranberry with D-Mannose, 90 Vegetarian Capsules, Nature's Answer
Finding step glcP for D-mannose catabolism in Pseudomonas simiae WCS417
The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1-|2 mannose...
Mouse Mbl2 / Mannose-binding Protein C ELISA Kit | Merck Life Science Indonesia
5 FAQ: D-mannose For UTI: Dosage, Frequency, And More - Stop UTI Forever
Prevention D Mannose And Cranberry pills | UTI Prevention Supplement | Viva-Nutra
- Viva Nutra
NHANES 2013-2014:
Dietary Supplement Use 30-Day - Total Dietary Supplements Data Documentation, Codebook, and...
Mannose-binding lectin genotypes: lack of association with susceptibility to thoracic empyema. - Experimental Medicine Division
1kwz.1 | SWISS-MODEL Template Library
Capsules6
- Our D-Mannose cranberry capsules use only natural ingredients, Purest Vantage D-Mannose is the obvious choice. (purestvantage.com)
- NOW's D-Mannose veg capsules deliver the convenience of a pill delivery form. (waterbug.ca)
- Click Buy Now below to get UT Answer Cranberry with D-Mannose, 90 Vegetarian Capsules, Nature's Answer. (dailyhealthexchange.com)
- Purchase UT Answer Cranberry with D-Mannose, 90 Vegetarian Capsules, Nature's Answer from VitaSprings.com through links and I may recieve a commission. (dailyhealthexchange.com)
- Our highly powerful D-Mannose capsules combine the healthy properties of D-mannose, Cranberry, Hibiscus flower, and Dandelion root extract to help flush out toxins, cleanse the urinary tract, and maintain a healthy bladder lining. (viva-nutra.com)
- Contains 120 capsules - 2000mg of D-mannose, 300mg of Cranberry Juice Powder, 200mg of Hibiscus Flower Extract, and 200mg of Dandelion Root Extract. (viva-nutra.com)
Urinary tract10
- D-Mannose supports the health of the entire urinary tract: the urethra, bladder, ureter, renal pelvis and the renal parenchyma. (baar.com)
- D-Mannose and proanthocyanadins from Pro Cran d'Or™ - a pure, concentrated whole cranberry fruit powder - show evidence of the ability to inhibit the adherence of E. coli bacteria in the urinary tract. (physicianschoice.com)
- As part of a balanced response, a physician may suggest the use of D Mannose to help a healthy urinary tract expel unwanted organisms. (purestvantage.com)
- D-Mannose is a type of sugar that has been shown to help prevent UTIs by sticking to harmful bacteria and flushing them out of the urinary tract. (sproutsupps.com)
- Complete with Vitamin C, Vitamin B6, D-Mannose, Cranberry 4:1 Extract, Uva Ursi, and Dandelion Extract, Complete UT Health is designed to promote urinary tract health with antioxidants. (hrsupplements.com)
- D-Mannose works by sticking to E. Coli bacteria in the urinary tract and removing it from the body through urination, commonly used as a preventative measure for urinary tract infections. (hrsupplements.com)
- D-mannose is a naturally occurring simple sugar that your body utilizes to help cleanse the urinary tract and maintain a healthy bladder lining. (waterbug.ca)
- 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. (waterbug.ca)
- Regulatory effect of Pseudomonas aeruginosa mannose-sensitive hemagglutinin on inflammation and immune function in percutaneous nephrolithotomy patients with upper urinary tract calculi complicated with infection. (bvsalud.org)
- To study the effect of an injection of Pseudomonas aeruginosa mannose -sensitive hemagglutinin (PA-MSHA) on inflammation and immune function in patients with upper urinary tract calculi complicated by infection who have undergone percutaneous nephrolithotomy . (bvsalud.org)
LECTIN DEFICIENCY7
- Mannose-binding lectin deficiency is a condition that affects the immune system. (medlineplus.gov)
- People with mannose-binding lectin deficiency can develop infections of the upper respiratory tract and other body systems. (medlineplus.gov)
- Infants and young children with mannose-binding lectin deficiency seem to be more susceptible to infections than affected adults, but adults can also develop recurrent infections. (medlineplus.gov)
- Relatively common mutations in the MBL2 gene can lead to mannose-binding lectin deficiency. (medlineplus.gov)
- Researchers believe that a number of factors, including other genetic and environmental factors, are involved in the development of mannose-binding lectin deficiency and susceptibility to infection. (medlineplus.gov)
- The inheritance pattern of mannose-binding lectin deficiency is unclear. (medlineplus.gov)
- It is important to note that people inherit an increased risk of developing mannose-binding lectin deficiency, not the condition itself. (medlineplus.gov)
MBL25
- Functional mannose-binding lectins are made up of two to six protein groups called trimers, which are each composed of three of the protein pieces (subunits) produced from the MBL2 gene. (medlineplus.gov)
- Mutations in the MBL2 gene can reduce the production of the mannose-binding lectin subunit or eliminate the subunit's ability to assemble into functional mannose-binding lectin. (medlineplus.gov)
- However, not everyone with a change in the MBL2 gene has decreased levels of mannose-binding lectin, and not everyone with decreased protein levels is prone to infection. (medlineplus.gov)
- Mannose-binding lectin 2 (MBL2) gene polymorphism in asthma and atopy among adults. (cdc.gov)
- Mannose-binding lectin concentrations, MBL2 polymorphisms, and susceptibility to respiratory tract infections in young men. (cdc.gov)
Mammalian3
- Here, we present the first structures of a mammalian β-mannosidase in both the apo- and mannose-bound forms. (rcsb.org)
- Mannose-binding lectin (MBL), a mammalian lectin, is a pattern recognition molecule of the innate immune system and recognizes carbo-hydrates that are exposed on pathogens. (scirp.org)
- Mammalian cells express two mannose 6-phosphate receptors, MPR46 and MPR300, both of which mediate the targeting of lysosomal enzymes to lysosomes. (biologists.com)
Susceptibility2
Residues3
- The receptors recognize mannose 6-phosphate residues which are specifically added to lysosomal enzymes during their passage through the Golgi apparatus. (biologists.com)
- 2 mannose residues on the outer face of gp120. (lji.org)
- The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120. (lji.org)
Monosaccharide2
- D-Mannose is a monosaccharide hexose sugar, naturally found in some trees, berries and fruits, such as cranberry. (baar.com)
- D-mannose is a monosaccharide (sugar) that naturally occurs in fruits including apples, blueberries, and cranberries. (physicianschoice.com)
Molecule1
- Catalysis of the transfer of a phosphate group from GTP or GDP to a mannose molecule. (systemsbiology.net)
UTIs4
- ProCran is a potent, pure powder made from cranberry extract - an effective accompaniment to D-Mannose in helping prevent UTIs. (physicianschoice.com)
- This incredible supplement combines the powerful benefits of two natural extracts, D-Mannose and Cranberry, to give you a one-two punch against UTIs. (sproutsupps.com)
- Start fighting UTIs the natural way with D-Mannose Cranberry + today! (sproutsupps.com)
- E. coli bacteria are responsible for causing 90% of UTIs and are not easy to get rid of unless through intervention by our healthy D-mannose punch. (viva-nutra.com)
Ligands3
- Two MPRs are known, both of which mediate the transport of newly synthesized mannose 6-phosphate-containing ligands from the Golgi apparatus to prelysosomal structures of the endocytic pathway. (biologists.com)
- Furthermore, the larger of the two receptors with an apparent M T of 300 ×10 3 (MPR300) mediates the endocjlosis of mannose 6-phosphate-containing ligands, while the smaller of the two receptors with an apparent M r of 46 ×10 3 (MPR46) mediates the secretion of part of its ligands. (biologists.com)
- Orientation of bound ligands in mannose-binding proteins. (expasy.org)
Polymorphisms3
- Mannose binding lectin gene polymorphisms and asthma. (cdc.gov)
- Mannose-binding lectin gene polymorphisms in infants with bronchiolitis and post-bronchiolitis wheezing. (cdc.gov)
- Mannose-binding lectin 2 gene polymorphisms and predisposition to allergic bronchial asthma in a western Romanian children population: an observational study. (cdc.gov)
SUPPLEMENT1
- E. Coli is responsible for 90% of all UTI's, making D-Mannose an integral supplement for those that suffer from chronic UTI's. (hrsupplements.com)
Receptors2
- This unexpected complementary expression pattern points to specific functions of the two mannose 6-phosphate receptors during mouse embryogenesis. (biologists.com)
- Mannose 6-phosphate receptors (MPRs) mediate the targeting of newly synthesized soluble lysosomal enzymes. (biologists.com)
Protein5
- People with this condition have low levels (deficiency) of an immune system protein called mannose-binding lectin in their blood. (medlineplus.gov)
- This gene provides instructions for making a protein that assembles into a complex called mannose-binding lectin. (medlineplus.gov)
- A decrease in the availability of the normal subunit protein may lead to a reduction of the functional mannose-binding lectin in blood. (medlineplus.gov)
- The antibody pair provided in this kit recognizes mouse MBL-2 /Mannose Binding Protein C. (sigmaaldrich.id)
- BACKGROUND: The role of the innate immune protein mannose-binding lectin (MBL) in host defence against severe respiratory infection remains controversial. (ox.ac.uk)
Sugars1
- Additionally, in contrast to most other ligand-bound β-mannosidases from bacterial and fungal sources where bound sugars were in a boat-like conformation, we find the mannose in the chair conformation. (rcsb.org)
Immune2
- Mannose-binding lectin plays an important role in the body's immune response by attaching to foreign invaders such as bacteria, viruses, or yeast and turning on (activating) the complement system . (medlineplus.gov)
- Mannose-binding lectin can also stimulate special immune cells to engulf and break down the attached pathogen. (medlineplus.gov)
Bladder1
- D-Mannose has clearly proven its worth as a supportive therapy measure and in the prevention of recurrent bladder infections. (vagiflor.com)
Naturally1
- D-Mannose is a type of sugar that occurs naturally in some plants in starch and is mainly found in cranberries. (hrsupplements.com)
Ingredients1
- As a member of the Sprout Supplements family, you can trust that D-Mannose with Cranberry is made with high-quality ingredients. (sproutsupps.com)
Sugar1
- The natural D-Mannose sugar provides effective and lasting relief from acute symptoms such as a burning sensation when passing urine and the more frequent urge to urinate, without attacking the mucosa. (vagiflor.com)
Symptoms1
- however, many affected individuals have no signs or symptoms related to low mannose-binding lectin levels. (medlineplus.gov)
Special1
- Sorry, 'D-Mannose Special' has been discontinued and is no longer available. (baar.com)
Made1
- It galactose, Dcarabinose, Dcxylose and Dc should be made clear to the public that swalc mannose. (who.int)
Clear1
- While there are several treatment options to clear up your kidneys, nothing matches the potency of our organically produced D-Mannose. (viva-nutra.com)
Role2
- β-Mannosidase is a lysosomal enzyme from the glycosyl hydrolase family 2 that cleaves the single β(1-4)-linked mannose at the nonreducing end of N-glycosylated proteins, and plays an important role in the polysaccharide degradation pathway. (rcsb.org)
- The role of mannose-binding lectin in pneumococcal infection. (cdc.gov)
Unique1
- D-Mannose has a unique cell structure that allows it to adhere to undesirable foreign substances, which prevents them from sticking to the bladder's lining. (hrsupplements.com)
Body1
- With decreased levels of mannose-binding lectin, the body does not recognize and fight foreign invaders efficiently. (medlineplus.gov)
Water1
- Dissolve one effervescent tablet containing 2g of D-Mannose in 200 mL of water and drink immediately. (vagiflor.com)
Formation2
- Dolichol-phosphate-mannose synthase catalyzes the formation of Dolichol-phosphate-mannose from Dolichol-phosphate and GDP-mannose. (eurekamag.com)
- One unit is defined as the amount of enzyme that catalyzes the formation of 1 μmol of GDP-Man from Mannose-1-P and GTP per minute at 37°C. (chemilyglycoscience.com)