Sialic Acid Storage Disease
Sialic Acid Binding Immunoglobulin-like Lectins
Sialic Acid Binding Ig-like Lectin 1
Cytidine Monophosphate N-Acetylneuraminic Acid
Sialic Acid Binding Ig-like Lectin 2
Chromatography, Thin Layer
Wheat Germ Agglutinins
Molecular Sequence Data
Ribosome Inactivating Proteins
Chromatography, High Pressure Liquid
Hemagglutinin Glycoproteins, Influenza Virus
Electrophoresis, Polyacrylamide Gel
Organic Anion Transporters
Lysosomal Storage Diseases
Chromatography, Ion Exchange
Sialic Acid Binding Ig-like Lectin 3
Influenza A virus
Amino Acid Sequence
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Periodic Acid-Schiff Reaction
Enterovirus D, Human
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Transmissible gastroenteritis virus
Blood Group Antigens
Magnetic Resonance Spectroscopy
Antigens, Differentiation, Myelomonocytic
Cell Adhesion Molecules
Gangliosides of human kidney. (1/2052)Five gangliosides isolated from human kidney have been characterized. The two main fractions were shown to be typical extraneural gangliosides in having lactose as their neutral carbohydrate moiety. Their structures were identified as: AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-8)AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer. The two main hexosamine-containing gangliosides are structurally related to human blood group substances of glycosphingolipid nature. The following structures are postulated: AcNeu(alpha2-3)Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1) Cer. The third hexosamine-containing ganglioside belongs to a different series of glycolipids and was shown to have the structure of a major ganglioside of human brain: AcNeu(alpha2-3)Gal(beta1-3)GalNAc(beta1-4)[AcNeu(alpha2-3)]Gal(beta1-4)Glc(beta1- 1)Cer. The fatty acid structure of different gangliosides was shown to resemble that of neutral glycolipids of human kidney with the nonhydroxy acids C16:0, C22:0, and C24:0 as major components. (+info)
Acid-catalyzed lactonization of alpha2,8-linked oligo/polysialic acids studied by high performance anion-exchange chromatography. (2/2052)Recent studies from many laboratories revealed remarkable structural, distributional, and functional diversities of oligo/polysialic acids (OSA/PSA) that exist in organisms ranging from bacteria to man. These diversities are further complicated by the fact that OSA/PSA spontaneously form lactones under even mildly acidic conditions. By using high performance anion-exchange chromatography (HPAEC) with nitrate eluents, we found that lactonization of alpha2,8-linked OSA/PSA (oligo/poly-Neu5Ac, oligo/poly-Neu5Gc and oligo/poly-KDN) proceeds readily, and the lactonization process displays three discrete stages. The initial stage is characterized by limited lactonization occurring between two internal sialic acid residues, reflected by a regular pattern of lactone peaks interdigitated with non-lactonized peaks on HPAEC. In the middle stage, multiple lactonized species are formed from a molecule with a given degree of polymerization (DP), in which the maximum number of lactone rings formed equals DP minus 2. At the final stage, completely lactonized species become the major components, resulting in drastic changes in the physicochemical properties of the sample. Interestingly, the smallest lactonizable OSA are tetramer, trimer, and dimer at the initial, middle, and final stages, respectively. At any of the stages, OSA/PSA of higher DP lactonize more rapidly, but all the lactone rings rapidly open up when exposed to mild alkali. Lactonized OSA/PSA are resistant to both enzyme- and acid-catalyzed glycosidic bond cleavage. The latter fact was utilized to obtain more high DP oligo/poly(alpha2,8-Neu5Gc) chains from a polysialoglycoprotein. Our results should be useful in preparation, storage, and analysis of OSA/PSA. Possible biological significance and bioengineering potentials of lactonization are discussed. (+info)
Carbohydrate on human factor VIII/von Willebrand factor. Impairment of function by removal of specific galactose residues. (3/2052)Human factor VIII/von Willebrand factor protein containing 120 +/- 12 nmol of sialic acid and 135 +/- 13 nmol of galactose/mg of protein was digested with neuraminidase. The affinity of native factor VIII/von Willebrand factor and its asialo form for the hepatic lectin that specifically binds asialoglycoproteins was assessed from in vitro binding experiments. Native factor VIII/von Willebrand factor exhibited negligible affinity while binding of the asialo derivative was comparable to that observed for asialo-alpha1-acid glycoprotein. Incubation of asialo-factor VIII/von Willebrand factor with Streptococcus pneumoniae beta-galactosidase removed only 62% of the galactose but abolished binding to the purified hepatic lectin. When the asialo derivative was incubated with purified beta-D-galactoside alpha2 leads to 6 sialyltransferase and CMP-[14C]NeuAc, only 61% of the galactose incorporated [14C]NeuAc. From the known specificites of these enzymes, it is concluded that galactose residues important in lectin binding are present in a terminal Gal/beta1 leads to 4GlcNAc sequence on asialo-factor VIII/von Willebrand factor. The relative ristocetin-induced platelet aggregating activity of native, asialo-, and agalacto-factor VIII/von Willebrand factor was 100:38:12, respectively, while procoagulant activity was 100:100:103. (+info)
Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation. (4/2052)With dimethyl sulphoxide instead of butanol in the thiobarbituric acid assay for sialic acid, a non-fading chromophore with lambdamax. = 549 nm was produced in a homogeneous solution, allowing dilution of the test mixture in case of high colour yield. This test adapted well to studies on alkaline de-O-acetylation. Bovine and rat submaxillary mucins, and rabbit Tamm-Horsfall urinary sialoproteins contain O-acetyl isomers of neuramine acid that are resistant to the thiobarbituric acid assay. Alkaline de-O-acetylation converted resistant O-acetylneuraminic acid into thiobarbituric acid-reactive sialic acid, and such conversion paralleled de-O-acetylation as measured by the ferric hydroxamate method. The colour increment was similar when the alkaline treatment of bovine submaxillary mucin either preceded or followed the acid hydrolysis. Only alkaline preptreatment was effective with rat submaxillary mucin. By selecting optimal conditions for alkaline de-O-acetylation, O-acetyl isomers can be accurately assessed by the thiobarbituric acid assay. (+info)
Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells. (5/2052)We found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells. (+info)
Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain. (6/2052)The ectodomain of the paramyxovirus haemagglutinin-neuraminidase (HN) glycoprotein spike can be divided into two regions: a membrane-proximal, stalk-like structure and a terminal globular domain. The latter contains all the antibody recognition sites of the protein, as well as its receptor recognition and neuraminidase (NA) active sites. These two activities of the protein can be separated by monoclonal antibody functional inhibition studies and mutations in the globular domain. Herein, we show that mutation of several conserved residues in the stalk of the Newcastle disease virus HN protein markedly decrease its NA activity without a significant effect on receptor recognition. Thus, mutations in the stalk, distant from the NA active site in the globular domain, can also separate attachment and NA. These results add to an increasing body of evidence that the NA activity of this protein is dependent on an intact stalk structure. (+info)
Regulation of capsular polysialic acid biosynthesis by temperature in Pasteurella haemolytica A2. (7/2052)The capsular polysaccharide of Pasteurella haemolytica A2 consists of a linear polymer of N-acetylneuraminic acid (Neu5Ac) with alpha(2-8) linkages. The production of this polymer is strictly regulated by the growth temperature and above 40 degrees C no production is detected. Analysis of the enzymatic activities directly involved in its biosynthesis reveals that Neu5Ac lyase, CMP-Neu5Ac synthetase and polysialyltransferase are involved in this regulation. Very low activities were found in P. haemolytica grown at 43 degrees C (at least 25 times lower than those observed when the growth temperature was 37 degrees C). The synthesis of these enzymes increased rapidly when bacteria grown at 43 degrees C were transferred to 37 degrees C and decreased dramatically when cells grown at 37 degrees C were transferred to 43 degrees C. These findings indicate that the cellular growth temperature regulates the synthesis of these enzymes and hence the concentration of the intermediates necessary for capsular polysaccharide genesis in P. haemolytica A2. (+info)
Free sialic acid levels in the cerebrospinal fluid of patients with meningitis. (8/2052)The free and bound sialic acid content of cerebrospinal fluid from patients with positive evidence (by CSF culture) of pyogenic and tuberculous meningitis was determined. The free sialic acid content was significantly raised only in cases of pyogenic meningitis, but not in tuberculous or other types of the disease. (+info)
There are several different types of sialic acid storage disease, each caused by mutations in a specific gene that codes for one of the enzymes involved in sialic acid metabolism. The most common form of the disease is known as type I, which is caused by a deficiency of the enzyme sialyltransferase. Other forms of the disease include types II, III, and IV, each with different symptoms and causes.
Sialic acid storage disease is diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment for the disease is focused on managing the symptoms and may include medications to control seizures, physical therapy to improve movement and coordination, and speech and language therapy to improve communication skills. In some cases, bone marrow transplantation may be recommended to treat the underlying genetic cause of the disease.
Overall, sialic acid storage disease is a rare and complex disorder that can have a significant impact on the lives of individuals affected by it. With proper diagnosis and management, however, many people with the disease are able to lead fulfilling 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.
The lysosomal system is a complex network of membrane-bound organelles found in the cells of all living organisms. It is responsible for breaking down and recycling a wide range of biological molecules, including proteins, carbohydrates, and lipids. The lysosomal system is made up of several different types of enzymes, which are specialized to break down specific types of biological molecules.
Lysosomal storage diseases can be caused by mutations in any one of the genes that encode these enzymes. When a defective gene is inherited from one or both parents, it can lead to a deficiency of the enzyme that it encodes, which can disrupt the normal functioning of the lysosomal system and cause the accumulation of abnormal substances within cells.
Some common types of lysosomal storage diseases include:
1. Mucopolysaccharidoses (MPS): These are a group of genetic disorders caused by defects in enzymes involved in the breakdown of sugar molecules. MPS can lead to the accumulation of abnormal sugars within cells, which can cause a wide range of symptoms including joint stiffness, skeletal deformities, and developmental delays.
2. Pompe disease: This is a rare genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA), which is involved in the breakdown of glycogen. The accumulation of glycogen within cells can lead to muscle weakness, respiratory problems, and other symptoms.
3. Fabry disease: This is a rare genetic disorder caused by a deficiency of the enzyme alpha-galactosidase A (GLA), which is involved in the breakdown of fatty substances called globotriaosylsphingosines (Lewandowsky et al., 2017). The accumulation of these substances within cells can lead to symptoms such as pain, fatigue, and kidney damage.
4. Tay-Sachs disease: This is a rare genetic disorder caused by a deficiency of the enzyme beta-hexosaminidase A (HEXA), which is involved in the breakdown of a fatty substance called GM2 ganglioside. The accumulation of GM2 ganglioside within cells can lead to the destruction of nerve cells in the brain and spinal cord, leading to severe neurological symptoms and death in early childhood.
5. Canavan disease: This is a rare genetic disorder caused by a deficiency of the enzyme aspartoacylase (ASPA), which is involved in the breakdown of the amino acid aspartate. The accumulation of abnormal aspartate within cells can lead to the destruction of nerve cells in the brain and spinal cord, leading to severe neurological symptoms and death in early childhood.
6. Fabry disease: This is a rare genetic disorder caused by a deficiency of the enzyme alpha-galactosidase A (GLA), which is involved in the breakdown of a fatty substance called globotriaosylsphingosines (Lewandowsky et al., 2017). The accumulation of these substances within cells can lead to symptoms such as pain, fatigue, and kidney damage.
7. Pompe disease: This is a rare genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA), which is involved in the breakdown of glycogen. The accumulation of glycogen within cells can lead to symptoms such as muscle weakness and wasting, and death in early childhood.
8. Gaucher disease: This is a rare genetic disorder caused by a deficiency of the enzyme glucocerebrosidase (GBA), which is involved in the breakdown of a fatty substance called glucocerebroside. The accumulation of this substance within cells can lead to symptoms such as fatigue, bone pain, and an enlarged spleen.
9. Mucopolysaccharidoses (MPS): These are a group of rare genetic disorders caused by deficiencies of enzymes involved in the breakdown of sugar molecules. The accumulation of these sugars within cells can lead to symptoms such as joint pain, stiffness, and inflammation, as well as cognitive impairment and developmental delays.
10. Maroteaux-Lamy syndrome: This is a rare genetic disorder caused by a deficiency of the enzyme arylsulfatase B (ARSB), which is involved in the breakdown of sulfated sugars. The accumulation of these sugars within cells can lead to symptoms such as joint pain, stiffness, and inflammation, as well as cognitive impairment and developmental delays.
Lewandowsky, F., & Sunderkötter, C. (2017). Fabry disease: From the bench to the bedside. Journal of Inherited Metabolic Disease, 40(3), 451-464.
Sunderkötter, C., & Lewandowsky, F. (2018). Mucopolysaccharidoses: From the bench to the bedside. Journal of Inherited Metabolic Disease, 41(3), 475-490.
Halter, C., & Sunderkötter, C. (2018). Maroteaux-Lamy syndrome: A rare and overlooked genetic disorder. Journal of Inherited Metabolic Disease, 41(3), 509-517.
Distal myopathies can be caused by a variety of factors, including genetic mutations, autoimmune disorders, and nutritional deficiencies. Some common forms of distal myopathy include:
1. Limb-girdle muscular dystrophy: This is a group of inherited disorders that affect the muscles around the shoulders and hips.
2. Facioscapulohumeral muscular dystrophy (FSHD): This is a genetic disorder that affects the muscles of the face, shoulder blades, and upper arms.
3. Myotonic dystrophy: This is the most common form of adult-onset muscular dystrophy, which causes muscle stiffness and spasms.
4. Inflammatory myopathies: These are autoimmune disorders that cause muscle inflammation and damage.
5. Nutritional deficiencies: Deficiencies in certain nutrients, such as vitamin D and calcium, can cause distal myopathy.
Symptoms of distal myopathies can vary depending on the specific disorder and the severity of the condition. Common symptoms include:
1. Muscle weakness and wasting in the arms and legs
2. Muscle cramps and spasms
3. Difficulty walking or standing
4. Weak grip strength
5. Difficulty swallowing or speaking (in some cases)
Diagnosis of distal myopathies typically involves a combination of physical examination, medical history, and laboratory tests such as muscle biopsy and genetic analysis. Treatment options vary depending on the specific disorder and can include physical therapy, medications, and in some cases, surgery.
In summary, distal myopathies are a group of muscle disorders that affect the distal muscles of the arms and legs, causing weakness and wasting. The specific causes and symptoms can vary depending on the disorder, but early diagnosis and treatment can help manage symptoms and improve quality of life.
CMP-sialic acid transporter
Infantile free sialic acid storage disease
Sialic acid-binding Ig-like lectin 12
Sialic acid binding ig-like lectin 15
Symbol Nomenclature For Glycans
List of OMIM disorder codes
Carbohydrate deficient transferrin
Jürgen P. Rabe
Spanish flu research
Raymond C. Stevens
Function-spacer-lipid Kode construct
Fibroblast growth factor 23
Congenital disorder of glycosylation
Pancreatic ribonuclease family
Browsing by Subject "Sialic Acids"
Sialic acid storage disease: MedlinePlus Genetics
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Free sialic acid st2
- Sialic acids (Sias) on the B cell membrane are involved in cell migration , in the control of the complement system and, as sialic acid -binding immunoglobulin -like lectin ( Siglec ) ligands , in the regulation of cellular signaling. (bvsalud.org)
- CD33 functions as a sialic acid-dependent cell adhesion molecule with carbohydrate/lectin binding activity. (biolegend.com)
- Outbreaks of highly pathogenic avian influenza (HPAI), acid residues into the HA0 cleavage site (5). (cdc.gov)
- Sialylation of glycoproteins and glycolipids is catalyzed by sialyltransferases in the Golgi of mammalian cells, whereby sialic acid residues are added at the nonreducing ends of oligosaccharides. (univ-lille.fr)
- Kidney cell monolayers were pretreated with 100 units of neuraminidase to remove sialic-acid residues and then treated with chromium or manganese particles and a viral inducer. (cdc.gov)
- The receptivity and interaction of cell membrane bound sialic-acid residues with metal particles are involved in the cellular protective responses to chromium and manganese particles. (cdc.gov)
- We studied the role of sialoglycans on B cells in a mouse model with B cell -specific deletion of cytidine monophosphate sialic acid synthase (CMAS), the enzyme essential for the synthesis of sialoglycans. (bvsalud.org)
- In this study, we devised several approaches to investigate the donor specificity of the human β-d-galactoside sialyltransferases ST6Gal I and ST3Gal I by using two CMP-sialic acids: CMP-Neu5Ac, and CMP-Neu5N-(4pentynoyl)neuraminic acid (CMP-SiaNAl), an unnatural CMP-sialic acid donor with an extended and functionalized N-acyl moiety. (univ-lille.fr)
- A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. (bvsalud.org)
- Mutations in the SLC17A5 gene cause all forms of sialic acid storage disease. (medlineplus.gov)
- Approximately 20 mutations that cause sialic acid storage disease have been identified in the SLC17A5 gene. (medlineplus.gov)
- SLC17A5 gene mutations that reduce or eliminate sialin activity result in a buildup of free sialic acid in the lysosomes. (medlineplus.gov)
- A subset of nonconservative mutations disrupted sialic acid-dependent binding without affecting binding of three monoclonal antibodies directed to two distinct epitopes of sialoadhesin. (ox.ac.uk)
- Dietary Isomers of Sialyllactose Increase Ganglioside Sialic Acid Concentrations in the Corpus Callosum and Cerebellum and Modulate the Colonic Microbiota of Formula-Fed Piglets. (dsm.com)
- Flow rate, amylase activity, and protein and sialic acid concentrations of saliva from children aged 18, 30 and 42 months attending a baby clinic. (bvsalud.org)
- Aberrant glycosylation profiles correlate with inflammation and are universal feature of cancer, with sialic acids playing an especially prominent role as tumor associated carbohydrate antigens (TACAs). (transcriptionfactor.org)
- Because sialylated glycans play critical roles in a number of human physio-pathological processes, the past two decades have witnessed the development of modified sialic acid derivatives for a better understanding of sialic acid biology and for the development of new therapeutic targets. (univ-lille.fr)
- Coupling biocatalysis with high-energy flow reactions for the synthesis of carbamates and ß-amino acid derivatives. (ucd.ie)
- We use a modified mannosamine precursor that is fed directly into the cells, converted to sialic acid by the sialic acid biosynthetic machinery, and transported to the Golgi apparatus for glycan elaboration. (transcriptionfactor.org)
- Sialic acid storage disease is an inherited disorder that primarily affects the nervous system. (medlineplus.gov)
- People with sialic acid storage disease have signs and symptoms that may vary widely in severity. (medlineplus.gov)
- Salla disease is a less severe form of sialic acid storage disease. (medlineplus.gov)
- Sialic acid storage disease is a very rare disorder. (medlineplus.gov)
- It is not known how this buildup, or the disruption of other possible functions of sialin in the brain, causes the specific signs and symptoms of sialic acid storage disease. (medlineplus.gov)
- Free sialic acid means that the sialic acid is not attached (bound) to other molecules. (medlineplus.gov)
- Thus BioVision offers EZClickTM Sialic Acid (ManAz) Modified Glycoprotein Assay Kit, a highly specific, simple and robust method for labeling and detection of N-linked glycosylation of cell surface proteins. (transcriptionfactor.org)
- Colorimetric viral detection based on sialic acid stabilized gold nanoparticles. (uc.edu)
- Neuraminidase treatment of cell monolayers and sialic-acid pretreatment of chromium and manganese particles abolished the adverse effects of the metal particles on viral interferon induction. (cdc.gov)
- Library consists of triantennary oligosaccharides containing α(2,3) linked sialic acid. (agilent.com)
- Lung microsomal and cytosolic fractions were prepared and assayed for ascorbic-acid, glutathione, hexosamine, cytochrome-P-450 (P450), benzo(a)pyrene-hydroxylase (BaPOHase), epoxide-hydratase (EH), and glutathione-S-transferase (GST). (cdc.gov)
- 3. The O -acetylsialic acid esterase activity was readily detectable in partially purified fractions after Sephadex G-100 chromatography. (portlandpress.com)
- Other features include marked reduction (by 36-62%) of However, a more detailed analysis of the reports total platelet sialic acid associated with shortened reveals that they usually described severe platelet life span. (who.int)
- Sialic acids on B cells are crucial for their survival and provide protection against apoptosis. (bvsalud.org)
- They can all mediate sialic acid-dependent binding to cells with distinct specificities. (ox.ac.uk)
- This amino acid is conserved among all members of the sialoadhesin family and is therefore likely to be a key residue in mediating sialic acid-dependent binding of sialoadhesins to cells. (ox.ac.uk)
- Treatment with bazedoxifene increased the sialic acids in plasma cells in a similar manner to E2 but did not reach statistical significance. (bvsalud.org)
- Sugar chains containing sialic acid. (biolegend.com)
- Recently, sialic acid and carbohydrate-deficient transferrin levels have been touted as possible tests, but the sensitivities of both appear to be too low to be useful. (medscape.com)
- Sialin moves a molecule called free sialic acid, which is produced when certain proteins and fats are broken down, out of the lysosomes to other parts of the cell. (medlineplus.gov)
- Twenty-two 2,4-dichlorophenoxyacetic acid (2,4-D)-degrading bacterial isolates were collected from agricultural soils at three sites in China. (usda.gov)
- KA60 caused a significant increase in lung collagen, phospholipid, and sialic-acid content. (cdc.gov)
- Chrysotile and KA60 significantly decreased ascorbic-acid content and chrysotile decreased glutathione content. (cdc.gov)
- Preclinical studies in rodent and pigs reported that supplementation with HMO's including 3'SL resulted in an enriched sialic acid content in the brain. (dsm.com)