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Tidsskrift For Den Norske Laegeforening... Apr 1963
Topics: Disaccharides; Metabolic Diseases
PubMed: 13979550
DOI: No ID Found -
Biochemistry Sep 20203--Sulfation on the glucosamine sugar unit in heparan sulfate (HS) is linked to various biological functions, including the anticoagulant activity to treat thrombotic...
3--Sulfation on the glucosamine sugar unit in heparan sulfate (HS) is linked to various biological functions, including the anticoagulant activity to treat thrombotic disorders in hospitals. The 3--sulfated glucosamine is biosynthesized by heparan sulfate glucosamine 3-sulfotransferases. Because of its biological significance, there is a need for 3--sulfated oligosaccharide standards to facilitate the compositional analysis of HS. These oligosaccharides must contain a Δ-unsaturated uronic acid (ΔUA) residue at the nonreducing end, which is due to the depolymerization reaction catalyzed by heparin lyases used during the compositional analysis procedure. Here, we describe a protocol for the preparation of one 3--sulfated disaccharide (compound ) and three 3--sulfated tetrasaccharides (compound -) in a milligram scale. The synthesis of 3--sulfated disaccharide and tetrasaccharide standards was completed by degrading synthetic octasaccharides using heparin lyases. Further analysis revealed that 3--sulfated oligosaccharide standards are labile under basic conditions, confirming the findings from a previous study. The unwanted degradation was reduced by decreasing the pH in the presence of phosphate buffer. The 3--sulfated oligosaccharide standards are reagents to characterize 3--sulfation in HS derived from biological sources.
Topics: Chemistry Techniques, Synthetic; Disaccharides; Heparitin Sulfate; Reference Standards
PubMed: 31608625
DOI: 10.1021/acs.biochem.9b00838 -
Nature Methods Apr 2008
Topics: Carbohydrate Conformation; Disaccharides; Glycosaminoglycans; Oligosaccharides; Terminology as Topic
PubMed: 18376390
DOI: 10.1038/nmeth0408-291 -
Glycoconjugate Journal Apr 2016The heparin disaccharides detected in farmed Atlantic salmon (Salmo salar) gills and intestines have, with one exception, been reported in porcine heparin. The relative...
The heparin disaccharides detected in farmed Atlantic salmon (Salmo salar) gills and intestines have, with one exception, been reported in porcine heparin. The relative amounts of disaccharides appear to be very different in the two species. Two chondroitin disaccharides with a proposed essential role in the zebrafish (Danio rerio) development and differentiation are detected in farmed Atlantic salmon. In addition, most of the chondroitin/dermatan sulfate and heparin disaccharides detected here have been reported in zebrafish, in support of the claims of the heparin presence in fish. The same chondroitin/dermatan disaccharides were detected in the bones of bony fishes. The rare disaccharide UA2S-GalNAc that was found in trace amounts in all 5 bony fishes was found in relative high amounts in gills and in significant amounts in intestines. The rare heparin disaccharide UA2S-GlcN was in relative highest amounts both in gills and intestines. In context with our previous reports, this communication suggests that glycosaminoglycans in farmed Atlantic salmon heparin need further studies in order to clarify structure and function.
Topics: Animals; Chondroitin; Disaccharides; Heparin; Salmo salar; Structure-Activity Relationship; Zebrafish
PubMed: 26993287
DOI: 10.1007/s10719-016-9652-8 -
The American Journal of Clinical... Feb 1969
Review
Topics: Adolescent; Adult; Carbohydrate Metabolism, Inborn Errors; Disaccharides; Galactose; Glucose; Glycoside Hydrolases; Humans; Intestinal Absorption; Lactose Intolerance; Metabolic Diseases; Nutritional Physiological Phenomena; Sucrose
PubMed: 4885929
DOI: 10.1093/ajcn/22.2.181 -
European Journal of Medicinal Chemistry Dec 2021Eight mono- or disaccharide analogues derived from BLM disaccharide, along with the corresponding carbohydate-dye conjugates have been designed and synthesized in this...
Eight mono- or disaccharide analogues derived from BLM disaccharide, along with the corresponding carbohydate-dye conjugates have been designed and synthesized in this study, aiming at exploring the effect of a gulose residue on the cellular binding/uptake of BLM disaccharide and it possible uptake mechanism. Our evidence is presented indicating that, for the cellular binding/uptake of BLM disaccharide, a gulose residue is an essential subunit but unrelated to its chemical nature. Interestingly, d-gulose-dye conjugate is able to selectively target A549 cancer cells, but l-gulose-dye conjugate fails. Further uptake mechanism studies demonstrate d-gulose-dye derivatives similar to BLM disaccharide-dye ones behave in a temperature- and ATP-dependent manner, and are partly directed by the GLUT1 receptor. Moreover, d-gulose modifying gemcitabine 53a exhibits more potent antitumor activity compared to derivatives 53b-c in which gemcitabine is decorated with other monosaccharides. Taken together, the monosacharide d-gulose conjugate offers a new strategy for solving cytotoxic drugs via the increased tumor targeting in the therapy of lung cancer.
Topics: A549 Cells; Antineoplastic Agents; Bleomycin; Cell Proliferation; Disaccharides; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Hexoses; Humans; Molecular Structure; Structure-Activity Relationship; Tumor Cells, Cultured
PubMed: 34619466
DOI: 10.1016/j.ejmech.2021.113866 -
Analytical Biochemistry Dec 1991Capillary zone electrophoresis (CZE) was used to separate eight commercial disaccharide standards of the structure delta UA2X(1----4)-D-GlcNY6X (where delta UA is... (Comparative Study)
Comparative Study
Capillary zone electrophoresis (CZE) was used to separate eight commercial disaccharide standards of the structure delta UA2X(1----4)-D-GlcNY6X (where delta UA is 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid, GlcN is 2-deoxy-2-aminoglucopyranose, S is sulfate, Ac is acetate, X may be S, and Y is S or Ac). These eight disaccharides had been prepared from heparin, heparan sulfate, and derivatized heparins. A similar CZE method was recently reported for the analysis of eight chondroitin and dermatan sulfate disaccharides (A. Al-Hakim and R.J. Linhardt, Anal. Biochem. 195, 68-73, 1991). Two of the standard heparin/heparan sulfate disaccharides, having an identical charge of -2, delta UA2S(1----4)-D-GlcNAc and delta UA(1----4)-D-GlcNS, were not fully resolved using standard sodium borate/boric acid buffer. This buffer had proven effective in separating chondroitin/dermatan sulfate disaccharides of identical charge. Resolution of these two heparin/heparan sulfate disaccharides could be improved by extending the capillary length, preparing the buffer in 2H2O, or eliminating boric acid. Baseline resolution was achieved in sodium dodecyl sulfate in the absence of buffer. The structure and purity of each of the eight new commercial heparin/heparan sulfate disaccharide standards were confirmed using fast-atom-bombardment mass spectrometry and high-field 1H-NMR spectroscopy. Heparin and heparan sulfate were then depolymerized using heparinase (EC 4.2.2.7), heparin lyase II (EC 4.2.2.-), heparinitase (EC 4.2.2.8), and a combination of all three enzymes. CZE analysis of the products formed provided a disaccharide composition of each glycosaminoglycan. As little as 50 fmol of disaccharide could be detected by ultraviolet absorbance.
Topics: Carbohydrate Sequence; Disaccharides; Electrophoresis; Heparin; Heparin Lyase; Heparitin Sulfate; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Polysaccharide-Lyases; Sensitivity and Specificity; Spectrometry, Mass, Fast Atom Bombardment
PubMed: 1812791
DOI: 10.1016/0003-2697(91)90098-e -
Angewandte Chemie (International Ed. in... Feb 2024Disaccharides are composed of two monosaccharide subunits joined by a glycosidic linkage in an α or β configuration. Different combinations of isomeric monosaccharide...
Disaccharides are composed of two monosaccharide subunits joined by a glycosidic linkage in an α or β configuration. Different combinations of isomeric monosaccharide subunits and different glycosidic linkages result in different isomeric disaccharide products. Thus, direct discrimination of these disaccharide isomers from a mixture is extremely difficult. In this paper, a hetero-octameric Mycobacterium smegmatis porin A (MspA) nanopore conjugated with a phenylboronic acid (PBA) adapter was applied for disaccharide sensing, with which three most widely known disaccharides in nature, including sucrose, lactose and maltose, were clearly discriminated. Besides, all six isomeric α-D-glucopyranosyl-D-fructoses, differing only in their glycosidic linkages, were also well resolved. Assisted by a custom machine learning algorithm, a 0.99 discrimination accuracy is achieved. Nanopore discrimination of disaccharide isomers with different glycosidic linkages, which has never been previously demonstrated, is inspiring for nanopore saccharide sequencing. This sensing capacity was also applied in direct identification of isomaltulose additives in a commercial sucrose-free yogurt, from which isomaltulose, lactose and L-lactic acid were simultaneously detected.
Topics: Disaccharides; Glycosides; Mycobacterium smegmatis; Lactose; Nanopores; Porins; Monosaccharides
PubMed: 38116834
DOI: 10.1002/anie.202316766 -
Methods in Molecular Biology (Clifton,... 2001
Topics: Animals; Carbohydrate Sequence; Cattle; Chondroitin ABC Lyase; Chondroitin Sulfates; Dermatan Sulfate; Disaccharides; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Humans; Hyaluronic Acid
PubMed: 11450222
DOI: 10.1385/1-59259-209-0:117 -
The FEBS Journal May 2023O-sulfated N-acetyl-d-galactosamine (GalNAc) residues in chondroitin sulfate (CS) play a crucial role in chondroitinase ABC I (cABC-I) activity. CSA containing mainly...
O-sulfated N-acetyl-d-galactosamine (GalNAc) residues in chondroitin sulfate (CS) play a crucial role in chondroitinase ABC I (cABC-I) activity. CSA containing mainly 4-O-monosulfated GalNAc was a good substrate for the enzyme, but not CSE containing mainly 4,6-O-disulfated GalNAc [GalNAc(4S,6S)]. Each CS isomer exhibits structural heterogeneity; CSE has di-sulfated disaccharide units and mono-sulfated disaccharide units. Disaccharide composition analysis of digested products revealed that mono-sulfated disaccharide units in CSE contributed to the enzyme reactivity. Although enough substrate (CSA) was present in mixtures of CSA and CSE for reaction, the reactivity was reduced depending on the amount of CSE in the mixture. These results suggested that CSE is not only resistant to enzyme digestion but also attenuates enzyme activity. To understand the mechanism of action, crystallography of cABC-I in complex with unsaturated CSE-disaccharide, ΔDi-(4,6)S, was performed. Both 4-O- and 6-O-sulfate groups in ΔDi-(4,6)S interact with Arg500, suggesting that there was a greater interaction between ΔDi-(4,6)S and Arg500 than between mono-sulfated disaccharides and Arg500. Besides, this interaction attenuated enzyme activity by interfering with a function of Arg500, which is the charge neutralization of the carboxy group of D-glucuronic acid (GlcA) residues in CS. When interacting with the CSE-disaccharide unit [GlcAβ1-3GalNAc(4S,6S)] in CS, cABC-I cannot interact with other CS-disaccharide units until it has digested the CSE-disaccharide unit. The low reactivity of cABC-I with CSE is attributable to two suggested factors: (a) resistance of E-units in CSE molecules to digestion by cABC-I, and (b) tendency of E-units in CSE molecules to attenuate cABC-I activity.
Topics: Disaccharides; Chondroitin Sulfates; Chondroitin ABC Lyase; Crystallography; Sulfates; Antibodies; Galactosamine
PubMed: 36478634
DOI: 10.1111/febs.16685