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Vicente, C. P., P. Zancan, L. L. Peixoto, R. Alves-Sá, F. S. Araújo, P. A. S. Mourão, and M. S. G. Pavão. "Unbalanced Effects of Dermatan Sulfates with Different Sulfation Patterns on Coagulation, Thrombosis and Bleeding." Thrombosis and Haemostasis 86, no. 11 (2001): 1215–20. http://dx.doi.org/10.1055/s-0037-1616054.
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SummaryWe compared the anticoagulant, antithrombotic and bleeding effects of highly sulfated dermatan sulfates from invertebrates and their mammalian counterpart. An invertebrate dermatan sulfate containing 2-O-sulfated α-L-iduronic acid and 4-O-sulfated N-acetyl-β-D-galactosamine residues is a potent anticoagulant due to a high heparin cofactor II activity. It inhibits thrombin due to the formation of a covalent complex with heparin cofactor II, as in the case of mammalian dermatan sulfate, but the effect occurs at lower concentrations for the invertebrate polysaccharide. Surprisingly, the invertebrate dermatan sulfate has a lower potency to prevent thrombus formation on an experimental model and a lower bleeding effect in rats than the mammalian dermatan sulfate. In contrast, another invertebrate dermatan sulfate, also enriched in 2-O-sulfated α-L-iduronic acid, but in this case sulfated at O-6 position of the N-acetyl-β-D-galactosamine units, has no in vitro or in vivo anticoagulant activity, does not prevent thrombus formation but shows a bleeding effect similar to the mammalian glycosaminoglycan. Overall, these results demonstrate unbalanced effects of dermatan sulfates with different sulfation patterns on coagulation, thrombosis and bleeding, and raise interesting questions concerning the relationship among these three biological actions of sulfated polysaccharides.
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PAVÃO, MAURO S. G. "Structure and anticoagulant properties of sulfated glycosaminoglycans from primitive Chordates." Anais da Academia Brasileira de Ciências 74, no. 1 (March 2002): 105–12. http://dx.doi.org/10.1590/s0001-37652002000100007.
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Dermatan sulfates and heparin, similar to the mammalian glycosaminoglycans, but with differences in the degree and position of sulfation were previously isolated from the body of the ascidian Styela plicata and Ascidia nigra. These differences produce profound effects on their anticoagulant properties. S. plicata dermatan sulfate composed by 2-O-sulfatedalpha-L-iduronic acid and 4-O-sulfated N-acetyl-beta-D-galactosamine residues is a potent anticoagulant due to a high heparin cofactor II activity. Surprisingly, it has a lower potency to prevent thrombus formation on an experimental model and a lower bleeding effect in rats than the mammalian dermatan sulfate. In contrast, A. nigra dermatan sulfate, also enriched in 2-O-sulfated alpha-L-iduronic acid, but in this case sulfated at O-6 of the N-acetyl-beta-D-galactosamine units, has no in vitro or in vivo anticoagulant activity, does not prevent thrombus formation but shows a bleeding effect similar to the mammalian glycosaminoglycan. Ascidian heparin, composed by 2-O-sulfated alpha-L-iduronic acid, N- and 6-O-sulfated glucosamine (75%) and alpha-L-iduronic acid, N- and 6-O-sulfated glucosamine (25%) disaccharide units has an anticoagulant activity 10 times lower than the mammalian heparin, is about 20 times less potent in the inhibition of thrombin by antithrombin, but has the same heparin cofactor II activity as mammalian heparin.
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Valentová, Kateřina, Kateřina Purchartová, Lenka Rydlová, Lenka Roubalová, David Biedermann, Lucie Petrásková, Alena Křenková, et al. "Sulfated Metabolites of Flavonolignans and 2,3-Dehydroflavonolignans: Preparation and Properties." International Journal of Molecular Sciences 19, no. 8 (August 9, 2018): 2349. http://dx.doi.org/10.3390/ijms19082349.
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Silymarin, an extract from milk thistle (Silybum marianum) fruits, is consumed in various food supplements. The metabolism of silymarin flavonolignans in mammals is complex, the exact structure of their metabolites still remains partly unclear and standards are not commercially available. This work is focused on the preparation of sulfated metabolites of silymarin flavonolignans. Sulfated flavonolignans were prepared using aryl sulfotransferase from Desulfitobacterium hafniense and p-nitrophenyl sulfate as a sulfate donor and characterized by high-resolution mass spectrometry (HRMS) and nuclear magnetic resonance (NMR). Their 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and N,N-dimethyl-p-phenylenediamine (DMPD) radical scavenging; ferric (FRAP) and Folin–Ciocalteu reagent (FCR) reducing activity; anti-lipoperoxidant potential; and effect on the nuclear erythroid 2-related factor 2 (Nrf2) signaling pathway were examined. Pure silybin A 20-O-sulfate, silybin B 20-O-sulfate, 2,3-dehydrosilybin-20-O-sulfate, 2,3-dehydrosilybin-7,20-di-O-sulfate, silychristin-19-O-sulfate, 2,3-dehydrosilychristin-19-O-sulfate, and silydianin-19-O-sulfate were prepared and fully characterized. Sulfated 2,3-dehydroderivatives were more active in FCR and FRAP assays than the parent compounds, and remaining sulfates were less active chemoprotectants. The sulfated flavonolignans obtained can be now used as authentic standards for in vivo metabolic experiments and for further research on their biological activity.
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Pancake, SJ, GD Holt, S. Mellouk, and SL Hoffman. "Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates." Journal of Cell Biology 117, no. 6 (June 15, 1992): 1351–57. http://dx.doi.org/10.1083/jcb.117.6.1351.
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Circumsporozoite (CS) proteins, which densely coat malaria (Plasmodia) sporozoites, contain an amino acid sequence that is homologous to segments in other proteins which bind specifically to sulfated glycoconjugates. The presence of this homology suggests that sporozoites and CS proteins may also bind sulfated glycoconjugates. To test this hypothesis, recombinant P. yoelii CS protein was examined for binding to sulfated glycoconjugate-Sepharoses. CS protein bound avidly to heparin-, fucoidan-, and dextran sulfate-Sepharose, but bound comparatively poorly to chondroitin sulfate A- or C-Sepharose. CS protein also bound with significantly lower affinity to a heparan sulfate biosynthesis-deficient mutant cell line compared with the wild-type line, consistent with the possibility that the protein also binds to sulfated glycoconjugates on the surfaces of cells. This possibility is consistent with the observation that CS protein binding to hepatocytes, cells invaded by sporozoites during the primary stage of malaria infection, was inhibited by fucoidan, pentosan polysulfate, and heparin. The effects of sulfated glycoconjugates on sporozoite infectivity were also determined. P. berghei sporozoites bound specifically to sulfatide (galactosyl[3-sulfate]beta 1-1ceramide), but not to comparable levels of cholesterol-3-sulfate, or several examples of neutral glycosphingolipids, gangliosides, or phospholipids. Sporozoite invasion into hepatocytes was inhibited by fucoidan, heparin, and dextran sulfate, paralleling the observed binding of CS protein to the corresponding Sepharose derivatives. These sulfated glycoconjugates blocked invasion by inhibiting an event occurring within 3 h of combining sporozoites and hepatocytes. Sporozoite infectivity in mice was significantly inhibited by dextran sulfate 500,000 and fucoidan. Taken together, these data indicate that CS proteins bind selectively to certain sulfated glycoconjugates, that sporozoite infectivity can be inhibited by such compounds, and that invasion of host hepatocytes by sporozoites may involve interactions with these types of compounds.
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Barron, Denis, and Ragai K. Ibrahim. "Synthesis of Flavonoid Sulfates. II. The Use of Aryl Sulfatase in the Synthesis of Flavonol-3-sulfates." Zeitschrift für Naturforschung C 43, no. 9-10 (October 1, 1988): 625–30. http://dx.doi.org/10.1515/znc-1988-9-1001.
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Abstract The rates of aryl sulfatase hydrolysis of several 7-, 4′- and 3-sulfated flavonoids were compared and found to follow the order 7 or 4′ >>> 3. The complete resistance of the 3-sulfate ester to enzyme hydrolysis provided a unique and convenient method for the synthesis of a number of naturally occurring flavonol-3-sulfates from the corresponding higher sulfated analogs in quantitative yield.
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Løvtrup-Rein, Huguette. "Biosynthesis of sulfated proteoglycans in amphibian embryonal cells." Bioscience Reports 9, no. 2 (April 1, 1989): 213–22. http://dx.doi.org/10.1007/bf01115998.
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The synthesis of sulfated proteoglycans in small explants from various parts of late blastulae from Ambystoma mexicanum or Xenopus laevis was investigated by incorporation of radioactive sulfate or glucosamine and galactosamine in media of low, normal or high tonicity. The explants differentiated into ciliated aggregates or fibroblast-like cells, or remained undifferentiated depending upon their origin in the embryo. High tonicity induces the explants to dissociated and prevents morphological differentiation, while low tonicity hardly affects this process. Yet, both types of media decrease the incorporation into glycosaminoglycans to various degrees, ranging from 40 to 80%, depending upon the species. In Xenopus, the uptake of sulfate is inhibited by as much as 90% in high tonicity media. The rate of incorporation of label is approximately twice as much in mesodermal as in animal or vegetal aggregates, which do not differ significantly. Animal aggregates from Ambystoma, however, revealed an exceptionally high uptake of sulfate. The relative distribution of chondroitin sulfates and heparan sulfates is not affected by changes in tonicity, except in Xenopus where high tonicity severely suppresses the synthesis of heparan sulfates, and is independent of the type of aggregate. The relationship between the synthesis of sulfated proteoglycans and processes involved in cell differentiation, especially cell adhesion, is discussed.
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Peres-Sampaio, Carlos Eduardo, Simone Thorp Palumbo, and José Roberto Meyer-Fernandes. "An Ecto-ATPase Activity Present in Leishmania tropica Stimulated by Dextran Sulfate." Zeitschrift für Naturforschung C 56, no. 9-10 (October 1, 2001): 820–25. http://dx.doi.org/10.1515/znc-2001-9-1023.
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AbstractIn this study we report the effects of sulfated polysaccharides on the ecto-ATPase activity of intact cells of Leishmania tropica. Increasing concentrations of dextran sulfate stimulated progressively the ecto-ATPase activity, but did not modify other ecto-enzymes present on the surface of this parasite, such as 5′ nucleotidase, 3′nucleotidase and a membrane-bound acid phosphatase activity. This stimulation was not observed when other sulfated polysaccharides such as chondroitin sulfates and heparin were tested. It depends on size and charge of the dextran sulfated molecule. When the cells were incubated in the presence of dextran sulfate Mr 8,000; 40,000 and 500,000 the stimulation of the ecto-ATPase activity was 11%; 23%; and 63%, respectively, and the stimulation was not observed when desulfated dextran (Mr 40,000) was used. The effects of dextran sulfate also depend on pH of the medium. At pH 7.5, the stimulation was over 60%, whereas at pH 8.5 only 25%. The effects of dextran sulfate 500,000 on the ecto-ATPase activity was totally abolished by spermidine and partially by putrescine, two polyamines synthesized and released by Leishmania.
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Reinehr, Thomas, Alberto Sánchez-Guijo, Nina Lass, and Stefan A. Wudy. "Higher steroid sulfation is linked to successful weight loss in obese children." Endocrine Connections 7, no. 10 (October 2018): 1020–30. http://dx.doi.org/10.1530/ec-18-0233.
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Objective Little information is available on the steroid sulfates profile in obese children. Therefore, we examined whether sulfated steroids are linked with weight status and associated comorbidities in obese children. Methods We analyzed 66 obese children (mean age 10.5 ± 2.5 years, 57.6% female, 53.9% prepubertal, mean BMI 27.0 ± 4.6 kg/m2, 50% with BMI-SDS reduction >0.5, 50% without BMI-SDS reduction) who participated in an outpatient 1-year intervention program based on exercise, behavior and nutrition therapy. We measured intact sulfated steroids (cholesterol sulfate (CS), pregnenolone sulfate (PregS), 17αOH pregnenolone sulfate (17OH-PregS), 16αOH dehydroepiandrosterone sulfate (16OH-DHEAS), DHEAS, androstenediol-3-sulfate, androsterone sulfate and epiandrosterone sulfate) by LC–MS/MS, and insulin resistance index HOMA, lipids, blood pressure at baseline and 1 year later. Results All sulfated steroids except 17OH-PregS, 16OH-DHEAS, androsterone sulfate and epiandrosterone sulfate were higher in boys compared to girls. Concentrations of CS before intervention were higher in children who lost weight. After 1 year of treatment, both groups showed increased levels of DHEAS, 16OH-DHEAS and androstenediol-3-sulfate, but PregS was only increased in children with weight loss. None of the steroid sulfates was significantly related to cardiovascular risk factors or HOMA except 17OH-PregS, which was associated with systolic blood pressure both in cross-sectional (β-coefficient: 0.09 ± 0.07, P = 0.020) and longitudinal analyses (β-coefficient: 0.06 ± 0.04, P = 0.013) in multiple linear regression analyses. Conclusions Since higher steroid sulfation capacity was associated with successful weight intervention in children disruption of sulfation may be associated with difficulties to lose weight. Future studies are necessary to prove this hypothesis.
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Kazachenko, Aleksandr Sergeyevich, Vladimir Aleksandrovich Levdansky, Aleksandr Vladimirovich Levdansky, and Boris Nikolayevich Kuznetsov. "MATHEMATICAL OPTIMIZATION OF THE PROCESS OF BIRCH WOOD XYLAN SULFATION BY SULFAMIC ACID IN N, N-DIMETHYLFORMAMIDE MEDIUM." chemistry of plant raw material, no. 2 (June 10, 2021): 87–94. http://dx.doi.org/10.14258/jcprm.2021027558.
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The effect of temperature and duration of sulfation of birch wood xylan by sulfamic acid in N, N-dimethylformamide (DMF) medium in the presence of urea on the yield of sulfated xylan and on the sulphur content was studied. By mathematical optimization, the sulfation conditions have been established allowing to achieve a high yield of the obtained xylan sulfates with a high sulphur content. Under optimal sulfation conditions: temperature 100±3 °C, duration 1.5 hours, the yield of sulfated xylan reaches to 63% mas. and the content of sulfur – 17.6% mas. The presence of sulfate groups in sulfated xylan samples obtained under optimal conditions was confirmed by elemental analysis and FTIR and 13C NMR spectroscopy.
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Chambers, W. H., and T. N. Oeltmann. "The effects of hexose 6-O-sulfate esters on human natural killer cell lytic function." Journal of Immunology 137, no. 5 (September 1, 1986): 1469–74. http://dx.doi.org/10.4049/jimmunol.137.5.1469.
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Abstract Natural cell-mediated cytotoxicity (NCMC) is inhibited by some neutral hexoses and hexose phosphates at 25 to 100 mM concentrations. In this study we describe the effects of hexose 6-O-sulfate esters on NCMC against K-562 target cells. Mannose 6-sulfate, galactose 6-sulfate, N-acetylglucosamine 6-sulfate, and N-acetylgalactosamine 6-sulfate inhibit NCMC in a dose-dependent manner at concentrations of 10 mM and below. Inhibitory effects of mannose 6-sulfate and galactose 6-sulfate were evident at concentrations as low as 1.25 mM. The neutral forms of these sugars, glucose and glucose 6-sulfate, did not inhibit NCMC over this range of concentrations. Comparison of the inhibitory effects of sulfated and phosphorylated forms of mannose and galactose indicated that the sulfated forms are much more potent inhibitors. Formation of effector cell:target cell conjugates was unaffected by the presence of sugar sulfates. Calcium pulse experiments demonstrated that inhibitory effects of sugar sulfates were exerted after the Ca++-dependent triggering step in the NK lytic process. Kinetic studies showed that addition of sugars as long as 60 min after initiation of cultures yielded potent inhibitory effects. Sugar sulfates were not toxic for effector cell populations and effectors were not refractory for lytic function after removal of sugars. Sugar sulfates were inhibitory against multiple tumor types in both human and murine NK lytic assays. These results suggest that the sugar sulfates inhibit NK cells at a postconjugation, posttriggering step involving lectin-like receptors or lectin-like molecules.
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Brandan, E., M. Maldonado, J. Garrido, and N. C. Inestrosa. "Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans." Journal of Cell Biology 101, no. 3 (September 1, 1985): 985–92. http://dx.doi.org/10.1083/jcb.101.3.985.
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Heparan sulfate and heparin, two sulfated glycosaminoglycans (GAGs), extracted collagen-tailed acetylcholinesterase (AChE) from the extracellular matrix (ECM) of the electric organ of Discopyge tschudii. The effect of heparan sulfate and heparin was abolished by protamine; other GAGs could not extract the esterase. The solubilization of the asymmetric AChE apparently occurs through the formation of a soluble AChE-GAG complex of 30S. Heparitinase treatment but not chondroitinase ABC treatment of the ECM released asymmetric AChE forms. This provides direct evidence for the vivo interaction between asymmetric AChE and heparan sulfate residues of the ECM. Biochemical analysis of the electric organ ECM showed that sulfated GAGs bound to proteoglycans account for 5% of the total basal lamina. Approximately 20% of the total GAGs were susceptible to heparitinase or nitrous acid oxidation which degrades specifically heparan sulfates, and approximately 80% were susceptible to digestion with chondroitinase ABC, which degrades chondroitin-4 and -6 sulfates and dermatan sulfate. Our experiments provide evidence that asymmetric AChE and carbohydrate components of proteoglycans are associated in the ECM; they also indicate that a heparan sulfate proteoglycan is involved in the anchorage of the collagen-tailed AChE to the synaptic basal lamina.
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Ray, Bimalendu, Martin Schütz, Shuvam Mukherjee, Subrata Jana, Sayani Ray, and Manfred Marschall. "Exploiting the Amazing Diversity of Natural Source-Derived Polysaccharides: Modern Procedures of Isolation, Engineering, and Optimization of Antiviral Activities." Polymers 13, no. 1 (December 30, 2020): 136. http://dx.doi.org/10.3390/polym13010136.
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Naturally occurring polysaccharide sulfates are highly diverse, owning variations in the backbone structure, linkage pattern and stereochemistry, branching diversity, sulfate content and positions of sulfate group(s). These structural characteristics bring about diverse sulfated polymers with dissimilar negative charge densities and structure–activity relationships. Herein, we start with a short discussion of techniques needed for extraction, purification, chemical sulfation, and structural characterization of polysaccharides. Processes of isolation and sulfation of plant-derived polysaccharides are challenging and usually involve two steps. In this context, we describe an integrated extraction-sulfation procedure that produces polysaccharide sulfates from natural products in one step, thereby generating additional pharmacological activities. Finally, we provide examples of the spectrum of natural source-derived polysaccharides possessing specific features of bioactivity, in particular focusing on current aspects of antiviral drug development and drug–target interaction. Thus, the review presents a detailed view on chemically engineered polysaccharides, especially sulfated derivatives, and underlines their promising biomedical perspectives.
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Fonseca, Roberto, Gustavo Santos, and Paulo Mourão. "Effects of polysaccharides enriched in 2,4-disulfated fucose units on coagulation, thrombosis and bleeding." Thrombosis and Haemostasis 102, no. 11 (2009): 829–36. http://dx.doi.org/10.1160/th08-11-0773.
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SummarySulfated polysaccharides from marine invertebrates have welldefined structures and constitute a reliable class of molecules for structure-activity relationship studies.We tested the effects of two of these polysaccharides,namely a sulfated fucan and a fucosylated chondroitin sulfate, on coagulation, thrombosis and bleeding. The compounds share similar 2,4-disulfated fucose units, which are required for high anticoagulant activity in this class of polymer.These residues occur either as branches in fucosylated chondroitin sulfate or as components of the linear chain in the sulfated fucan.These polysaccharides possess anticoagulant activity but differ significantly in their mechanisms of action.The fucosylated chondroitin sulfate inhibits thrombin by heparin cofactor II, whereas sulfated fucan inhibits thrombin by both antithrombin and heparin cofactor II. In addition, these polysaccharides also have serpin-independent anticoagulant activities. Fucosylated chondroitin sulfate, but not sulfated fucan, activates factor XII. As a result of the complex anticoagulant mechanism, the invertebrate polysaccharides differ in their effects on experimental thrombosis. For instance, the sulfated fucan inhibits venous thrombosis at lower doses than fucosylated chondroitin sulfate. In contrast, fucosylated chondroitin sulfate is significantly more potent than sulfated fucan in arterial thrombosis. Finally, fucosylated chondroitin sulfate increases bleeding, while sulfated fucan has only a discrete effect. In conclusion, the location of 2,4-disulfated fucose units in the polysaccharide chains dictates the effects on coagulation, thrombosis and bleeding.
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Fonseca, Roberto, Stephan-Nicollas Oliveira, Vitor Pomin, André Mecawi, Iracema Araujo, and Paulo Mourão. "Effects of oversulfated and fucosylated chondroitin sulfates on coagulation." Thrombosis and Haemostasis 103, no. 05 (2010): 994–1004. http://dx.doi.org/10.1160/th09-10-0734.
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SummaryWe report the effects of a chemically oversulfated chondroitin sulfate and a naturally fucosylated chondroitin sulfate on the coagulation system. The former has been recently identified as a contaminant of heparin preparations and the latter has been proposed as an alternative anticoagulant. The mechanism of action of these polymers on coagulation is complex and target different components of the coagulation system. They have serpin-independent anticoagulant activity, which preponderates in plasma. They also have serpin-dependent anticoagulant activity but differ significantly in the target coagulation protease and preferential serpin. Their anticoagulant effects differ even more markedly when tested as inhibitors of coagulation proteases using plasma as a source of serpins. It is possible that the difference is due to the high availability of fucosylated chondroitin sulfate whereas over-sulfated chondroitin sulfate has strong unspecific binding to plasma protein and low availability for the binding to serpins. When tested using a venous thrombosis experimental model, oversulfated chondroitin sulfate is less potent as an antithrombotic agent than fucosylated chondroitin sulfate. These highly sulfated chondroitin sulfates activate factor XII in in vitro assays, based on kallikrein release. However, only fucosylated chondroitin sulfate induces hypotension when intravenously injected into rats. In conclusion, the complexity of the regulatory mechanisms involved in the action of highly sulfated polysaccharides in coagulation requires their analysis by a combination of in vitro and in vivo assays. Our results are relevant due to the urgent need for new anticoagulant drugs or alternative sources of heparin.
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Ley, K., M. Cerrito, and K. E. Arfors. "Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 5 (May 1, 1991): H1667—H1673. http://dx.doi.org/10.1152/ajpheart.1991.260.5.h1667.
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Before firm adhesion, leukocytes roll slowly along the walls of small venules at velocities ranging from 0.7 to 36% of mean blood flow velocity. To investigate the nature of the adhesive process underlying leukocyte rolling, synthetic (dextran sulfate) and naturally occurring sulfated polysaccharides (heparin, chondroitin sulfates, keratan sulfate, and heparan sulfate) were infused via glass micropipettes into the lumen of small venules (20–60 microns diam) of the rabbit mesentery. Leukocyte rolling was observed and quantified using both transmitted light and incident fluorescence intravital microscopy. Rolling leukocytes accounted for 27–80% of total leukocyte flux, exhibiting a wide range of individual velocities (0.01–0.84 mm/s) with a mean value of 4% of centerline velocity. Dextran sulfate (Mr 500,000) inhibited leukocyte rolling very effectively [half-effective concentration (ED50) approximately 10 micrograms/ml] and was able to almost completely abolish rolling at 500 micrograms/ml. Heparin (ED50 approximately 50 micrograms/ml), chondroitin 6-sulfate C (ED50 approximately 500 micrograms/ml), and heparan sulfate (ED50 approximately 5 mg/ml) also reduced leukocyte rolling. At 5 mg/ml, chondroitin 4-sulfate B (dermatan sulfate) was marginally effective, but chondroitin 4-sulfate A and keratan sulfate were ineffective. The present data suggest that an adhesion receptor-ligand system distinct from the leukocyte integrins may be underlying transient leukocyte adhesion (rolling). Endothelial glycoproteins or proteoglycans containing sulfated side chains may be involved in mediating this adhesive process.
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Maccari, Francesca, Dealba Gheduzzi, and Nicola Volpi. "Anomalous Structure of Urinary Glycosaminoglycans in Patients with Pseudoxanthoma Elasticum." Clinical Chemistry 49, no. 3 (March 1, 2003): 380–88. http://dx.doi.org/10.1373/49.3.380.
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Abstract Background: Pseudoxanthoma elasticum (PXE) is a hereditary connective tissue disease in which proteoglycans have altered properties. We investigated whether altered proteoglycan metabolism occurs in vivo and may be reflected in the urine of PXE individuals by analyzing the excreted polysaccharides. Methods: We measured sulfated glycosaminoglycans in the urine of 10 PXE-affected patients, 12 healthy carriers, and 20 healthy controls by agarose gel electrophoresis. Chondroitin sulfate and heparan sulfate disaccharides were also quantified by treatment with specific lyases and separation of products by chromatography. Results: Total polysaccharides were 34% lower in the urine of PXE-affected patients and 17% lower in healthy carriers than in the control group. Chondroitin sulfate was significantly (P <0.01) decreased, and heparan sulfate was significantly increased. The ratio of chondroitin sulfate to heparan sulfate was 2.7 for PXE-affected patients, 2.3 for healthy carriers, and 10.7 for controls. In PXE-affected individuals and carriers, chondroitin sulfate contained more 4-sulfated disaccharide, less 6-sulfated disaccharide, and decreased nonsulfated disaccharide. Heparan sulfate from PXE-affected individuals and healthy carriers produced significantly less N-sulfated disaccharide and more disaccharide sulfated at the C-6 position with no significant abnormality of the nonsulfated disaccharide percentage and sulfates:disaccharide ratio. Conclusions: The urinary data support the concept that the inherited defect of the ABCC6/MRP6 transporter in PXE alters metabolism of key polysaccharides. Structural analysis of urinary sulfated polyanions may be useful in the diagnosis of PXE.
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Sheng, Juzheng, Renpeng Liu, Yongmei Xu, and Jian Liu. "The Dominating Role of N-Deacetylase/N-Sulfotransferase 1 in Forming Domain Structures in Heparan Sulfate." Journal of Biological Chemistry 286, no. 22 (March 28, 2011): 19768–76. http://dx.doi.org/10.1074/jbc.m111.224311.
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Heparan sulfate (HS) is a highly sulfated polysaccharide participated in essential physiological functions from regulating cell growth to blood coagulation. HS contains sulfated domains known as N-S domains and low sulfate domains known as N-Ac domains. The distribution of the domain structures is likely governed by the action of glucosaminyl N-deacetylase/N-sulfotransferase (NDST). Here, we sought to determine the substrate specificity of NDST using model substrates and recombinant NDST protein. We discovered that NDST-1 carries out the modification in a highly ordered fashion. The enzyme sulfates the substrate from the nonreducing end toward the reducing end consecutively, leading to the product with a cluster of N-sulfo glucosamine residues. Furthermore, a preexisting N-sulfo glucosamine residue prevents the action of NDST-1 at the residues immediately located at the nonreducing end, allowing the formation of an N-Ac domain. Our results provide the long sought evidence for understanding the formation of sulfated versus nonsulfated domains in the HS isolated from cells and tissues. The study demonstrates the regulating role of NDST-1 in mapping the sulfation patterns of HS.
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Shi, Jia, Riku Kanoya, Yurina Tani, Sodai Ishikawa, Rino Maeda, Sana Suzuki, Fumiya Kawanami, et al. "Sulfated Hyaluronan Binds to Heparanase and Blocks Its Enzymatic and Cellular Actions in Carcinoma Cells." International Journal of Molecular Sciences 23, no. 9 (May 2, 2022): 5055. http://dx.doi.org/10.3390/ijms23095055.
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We examined whether sulfated hyaluronan exerts inhibitory effects on enzymatic and biological actions of heparanase, a sole endo-beta-glucuronidase implicated in cancer malignancy and inflammation. Degradation of heparan sulfate by human and mouse heparanase was inhibited by sulfated hyaluronan. In particular, high-sulfated hyaluronan modified with approximately 2.5 sulfate groups per disaccharide unit effectively inhibited the enzymatic activity at a lower concentration than heparin. Human and mouse heparanase bound to immobilized sulfated hyaluronan. Invasion of heparanase-positive colon-26 cells and 4T1 cells under 3D culture conditions was significantly suppressed in the presence of high-sulfated hyaluronan. Heparanase-induced release of CCL2 from colon-26 cells was suppressed in the presence of sulfated hyaluronan via blocking of cell surface binding and subsequent intracellular NF-κB-dependent signaling. The inhibitory effect of sulfated hyaluronan is likely due to competitive binding to the heparanase molecule, which antagonizes the heparanase-substrate interaction. Fragment molecular orbital calculation revealed a strong binding of sulfated hyaluronan tetrasaccharide to the heparanase molecule based on electrostatic interactions, particularly characterized by interactions of (−1)- and (−2)-positioned sulfated sugar residues with basic amino acid residues composing the heparin-binding domain-1 of heparanase. These results propose a relevance for sulfated hyaluronan in the blocking of heparanase-mediated enzymatic and cellular actions.
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Zhao, Tingting, Xiaoguang Lu, Neal M. Davies, Yuewen Gong, Jingzhen Guo, Haojun Zhang, Zhiguo Li, Jing Hong, Guixiang Fu, and Ping Li. "Diabetes Results in Structural Alteration of Chondroitin Sulfate in the Urine." Journal of Pharmacy & Pharmaceutical Sciences 16, no. 3 (July 30, 2013): 486. http://dx.doi.org/10.18433/j3gs3c.
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Purpose. The assessment of the clinical significance of chondroitin sulfate in patients with type 2 diabetes mellitus (T2DM) and diabetic nephropathy (DN) for the detection of the relationship between chondroitin sulfate (CS) structure and disease. Methods. Healthy control (n=15), type 2 diabetic patients with normalbuminuria (n=12), and patients with microalbuminuria (n=13) were enrolled in the study. Total sulfated glycosaminoglycans (GAGs) concentration in the first morning urine was evaluated by 1,9-dimethylmethylene blue method and the composition was determined by agarose gel electrophoresis. Urinary chondroitin sulfate was quantified by a combination of treatment with specific lyase digestions and separation of products by SAX-HPLC. Results: GAGs concentration significantly increased in diabetic patients with microalbuminuria compared to diabetic patients with normalbuminuria. Qualitative analysis of urinary GAGs revealed the presence of chondroitin sulfate, heparan sulfate, and low-sulphated chondroitin sulphate-protein complex (LSC-PG). There was a decrease in CS and an increase in LSC-PG in the urine of patients with diabetes compared to healthy controls. Moreover, in diabetic patients, chondroitin sulfate contains more 6-sulfated disaccharide and less 4-sulfated disaccharide. There was a statistically significant difference in ratio of 6-sulfated disaccharide to 4-sulfated disaccharide among the three groups. Conclusions: GAGs were significantly increased in diabetic patients with microalbuminuria. The levels of urinary GAGs, ratio of LSC-PG/CS, as well as ratio of 6-sulfated to 4-sulfated disaccharides could be useful markers for diagnosis of patients with diabetic nephropathy. This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page.
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Alban, Susanne, and Robert Gastpar. "Development of SPC-ELISA: A New Assay Principle for the Study of Sulfated Polysaccharide-Protein Interactions." Journal of Biomolecular Screening 6, no. 6 (December 2001): 393–400. http://dx.doi.org/10.1177/108705710100600605.
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A sulfated polysaccharide-coating enzyme-linked immunosorbent assay (SPC-ELISA), a new screening assay for the study of interactions between sulfated polysaccharides and proteins, has been developed. Fibrinogen was used as representative for the protein. A microplate is coated with the sulfated polysaccharide to be tested and then incubated with various concentrations of fibrinogen. The bound fibrinogen is quantified by ELISA technique. The assay has been optimized with respect to coating procedure, incubation times, antibody concentrations, and detection conditions. Its capacity was demonstrated using three different sulfated polysaccharides: heparin, a sulfated glucuronogalactan extracted from a red algae, and a semisynthetic xanthan sulfate. Furthermore, the fibrinogen binding of semisynthetic laminarin sulfates with different degrees of sulfation showed good correlation with their anticoagulant effect as measured by fibrinogen clotting time. The intraassay as well as the interassay variations were lower than 8%. The binding properties observed in the SPC-ELISA correlated well with those found utilizing conventional gel permeation chromatography and fibrinogen affinity gel electrophoresis. Compared to these methods, the SPC-ELISA has several advantages: It is more rapid and far easier to perform, allows high throughput screening, and is suitable for automation. Furthermore, it is inexpensive, highly sensitive, and reproducible and has no special equipment requirements. Finally, the method represents the basis for multiple variations with regard to the target proteins as well as the detection methods.
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Zhuang, Quan, and Jack M. Miller. "One-pot sol-gel synthesis of sulfated ZrO2-SiO2 catalysts for alcohol dehydration." Canadian Journal of Chemistry 79, no. 8 (August 1, 2001): 1220–23. http://dx.doi.org/10.1139/v01-109.
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Sulfated ZrO2SiO2 catalysts were synthesized by one-pot sol-gel method using ammonium sulfate, zirconium propoxide, and tetraethyl orthosilicate as precursors. The catalysts were characterized by N2 adsorption and DRIFTS. On calcining the gel at elevated temperature, the ammonium sulfate decomposed, giving a sulfated zirconiasilica catalyst. By adding ammonium sulfate to the sol-gel synthesis system, the surface area, pore size, and pore volume of the resultant catalyst were increased. The one-pot sol-gel synthesized catalyst with an optimum loading of SO42 14 mol% showed significantly higher catalytic activity, with a selectivity of 100%, for isopropanol dehydration when compared to the impregnated catalyst. The one-pot sol-gel synthesis method is an effective way to prepare sulfated zirconia catalyst.Key words: sulfated zirconia, sol-gel synthesis, acid catalyst, alcohol dehydration, N2 adsorption, DRIFT.
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Sant, A. J., M. Zacheis, T. Rumbarger, K. S. Giacoletto, and B. D. Schwartz. "Human Ia alpha- and beta-chains are sulfated." Journal of Immunology 140, no. 1 (January 1, 1988): 155–60. http://dx.doi.org/10.4049/jimmunol.140.1.155.
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Abstract The human Ia antigens (DR, DQ, and DP), determined by genes with the HLA complex, are heterodimers consisting of a 34,000-Da alpha-chain glycoprotein and a 29,000-Da beta-chain glycoprotein. During the course of studies characterizing a recently described sulfated proteoglycan that is specifically associated with Ia, we discovered that there were also nonproteoglycan sulfated components present in the Ia immunoprecipitates. One-dimensional sodium dodecyl sulfate-gel analysis of these latter sulfated components derived from both DR and DQ immunoprecipitates indicated that these components have mobilities indistinguishable from conventional Ia alpha and beta glycoproteins. Two-dimensional gel analysis confirmed these findings and revealed that Ia-associated invariant proteins are sulfated as well. The sulfate moiety was not removed by endoglycosidase F treatment, suggesting that the protein portion of the molecule was sulfated. These results indicate that Ia alpha-, beta-, and invariant chains can be sulfated and raise the possibility that sulfation may play a role in the physiology of Ia molecules.
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Kowalewski, Björn, Heike Lange, Sabrina Galle, Thomas Dierks, Torben Lübke, and Markus Damme. "Decoding the consecutive lysosomal degradation of 3-O-sulfate containing heparan sulfate by Arylsulfatase G (ARSG)." Biochemical Journal 478, no. 17 (September 7, 2021): 3221–37. http://dx.doi.org/10.1042/bcj20210415.
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The lysosomal degradation of heparan sulfate is mediated by the concerted action of nine different enzymes. Within this degradation pathway, Arylsulfatase G (ARSG) is critical for removing 3-O-sulfate from glucosamine, and mutations in ARSG are causative for Usher syndrome type IV. We developed a specific ARSG enzyme assay using sulfated monosaccharide substrates, which reflect derivatives of its natural substrates. These sulfated compounds were incubated with ARSG, and resulting products were analyzed by reversed-phase HPLC after chemical addition of the fluorescent dyes 2-aminoacridone or 2-aminobenzoic acid, respectively. We applied the assay to further characterize ARSG regarding its hydrolytic specificity against 3-O-sulfated monosaccharides containing additional sulfate-groups and N-acetylation. The application of recombinant ARSG and cells overexpressing ARSG as well as isolated lysosomes from wild-type and Arsg knockout mice validated the utility of our assay. We further exploited the assay to determine the sequential action of the different sulfatases involved in the lysosomal catabolism of 3-O-sulfated glucosamine residues of heparan sulfate. Our results confirm and extend the characterization of the substrate specificity of ARSG and help to determine the sequential order of the lysosomal catabolic breakdown of (3-O-)sulfated heparan sulfate.
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Erickson, Deborah R., Sarah Ordille, Angela Martin, and V. P. Bhavanandan. "Urinary Chondroitin Sulfates, Heparan Sulfate and Total Sulfated Glycosaminoglycans in Interstitial Cystitis." Journal of Urology 157, no. 1 (January 1997): 61–64. http://dx.doi.org/10.1016/s0022-5347(01)65280-7.
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Pavão, Mauro S. G., Karin R. M. Aiello, Claudio C. Werneck, Luiz Claudio F. Silva, Ana-Paula Valente, Barbara Mulloy, Niall S. Colwell, Douglas M. Tollefsen, and Paulo A. S. Mourão. "Highly Sulfated Dermatan Sulfates from Ascidians." Journal of Biological Chemistry 273, no. 43 (October 23, 1998): 27848–57. http://dx.doi.org/10.1074/jbc.273.43.27848.
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Zarubica, Aleksandra, Branislav Jovic, Aleksandar Nikolic, Paula Putanov, and Goran Boskovic. "Temperature imposed textural and surface synergism affecting the isomerization activity of sulfated zirconia catalysts." Journal of the Serbian Chemical Society 74, no. 12 (2009): 1429–42. http://dx.doi.org/10.2298/jsc0912429z.
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Using sulfuric acid as the sulfating agent, two catalyst series were obtained from hydroxide and nitrate precursor with a sulfate loading identical to commercial sulfated hydroxide, i.e., 4.2 mass%. After calcination at 500, 600 and 700?C, all nine samples had various contents of residual sulfates depending on the origin of the catalyst. Accordingly, their surface properties were different, which, together with various textural properties, govern the formation of the active phase and their catalytic activity in the n-hexane isomerization reaction. The dominant activity and yield of mainly mono-branched isomers were attained in reaction at 200?C with a commercially sulfated zirconia catalyst calcined at 500?C. Among the SZ catalyst series synthesized from hydroxide and nitrate, the second according to its activity profile was similar to that of the commercially sulfated one, while samples originating from hydroxide showed some activity only after calcination at 600?C. This is due to the poorer textural properties of the hydroxide series, necessitating a higher calcination temperature in order to promote the simultaneous decomposition of S-containing species and their re-adsorption into the zirconia matrix following interaction and active phase formation. It seems that the tetragonal zirconia phase was not responsible for the catalytic activity but a synergistic effect of the textural properties of the samples and the sulfate loadings, which determine different acid strengths on the catalyst surface.
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Hueber, A. O., M. Pierres, and H. T. He. "Sulfated glycans directly interact with mouse Thy-1 and negatively regulate Thy-1-mediated adhesion of thymocytes to thymic epithelial cells." Journal of Immunology 148, no. 12 (June 15, 1992): 3692–99. http://dx.doi.org/10.4049/jimmunol.148.12.3692.
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Abstract Thy-1 is a major brain cell surface glycoprotein of adult mammal species also expressed in rodent thymus. Despite extensive studies, the function(s) of this molecule has remained so far ill defined. We have recently shown that Thy-1 was involved in the adhesion of mouse thymocytes to thymic epithelium through a specific interaction with a heterophilic ligand(s) expressed on the epithelial cell surface. In the present study, we aimed at evaluating the interaction of sulfated glycans with mouse Thy-1, as well as its consequence on Thy-1-mediated thymic lympho-epithelial cell interaction. It was shown that 125I-labeled Thy-1 directly bound to immobilized heparin. Sulfated glycans such as pentosan sulfate, dextran sulfate, and fucoidan were found to strongly inhibit the binding of Thy-1 to heparin. In contrast, chondroitin sulfate, keratan sulfate, and heparan sulfate were not inhibitory. Sulfated glycans (e.g., pentosan sulfate, assayed at a concentration of 50 micrograms/ml) completely blocked the Thy-1-dependent adhesion of T cells to a mouse thymic epithelial cell monolayer. To explore the mechanism of this inhibition, we compared the ability of T cell to adhere to mouse thymic epithelial cell monolayer or to sulfated glycans. Our results suggest that sulfated glycans bind to a Thy-1 site distinct from that with which this molecule interacts with its heterophilic ligand. Moreover, sulfate glycans could modulate the binding of rat mAb directed at spatially distinct Thy-1 epitopes. The present results identified a potential mechanism regulating Thy-1-mediated lympho-epithelial cell adhesion.
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Benito-Arenas, Raúl, Sandra Zárate, Julia Revuelta, and Agatha Bastida. "Chondroitin Sulfate-Degrading Enzymes as Tools for the Development of New Pharmaceuticals." Catalysts 9, no. 4 (April 1, 2019): 322. http://dx.doi.org/10.3390/catal9040322.
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Chondroitin sulfates are linear anionic sulfated polysaccharides found in biological tissues, mainly within the extracellular matrix, which are degraded and altered by specific lyases depending on specific time points. These polysaccharides have recently acquired relevance in the pharmaceutical industry due to their interesting therapeutic applications. As a consequence, chondroitin sulfate (CS) lyases have been widely investigated as tools for the development of new pharmaceuticals based on these polysaccharides. This review focuses on the major breakthrough represented by chondroitin sulfate-degrading enzymes and their structures and mechanisms of function in addition to their major applications.
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Arnoštová, Libuše, Ivan Černý, Vladimír Pouzar, and Pavel Drašar. "Synthesis of 5α-Cholestane Type Glycoside Sulfates." Collection of Czechoslovak Chemical Communications 58, no. 5 (1993): 1180–90. http://dx.doi.org/10.1135/cccc19931180.
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Synthesis of steroid glycoside sulfates sulfated both on the steroid skeleton and in sugar part are presented. Sodium salts of 5α-cholestane-3β,6α-diol 6-β-D-glucoside 3-sulfate V and 3-β-D-glucoside 6-sulfate XI were prepared from 3β-(2-tetrahydropyranyloxy)-5α-cholestan-6α-ol (I) using acetyl and methoxymethyl groups for temporary protection. Sulfation in the sugar part was at first checked in pregnane series and triethylammonium salts of 3β-(β-D-glucopyranosyloxy)pregn-5-en-20-one 6'-sulfate (XXVI) and 4'-sulfate 2',3'-diacetate XXVII were prepared. Application of the method on cholestane derivatives gave triethylammonium salt of 5α-cholestan-3β-yl β-D-glucopyranoside-6-sulfate (XXXI).
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Kazachenko, Aleksandr S., Natalya Yu Vasilieva, Valentina S. Borovkova, Olga Yu Fetisova, Noureddine Issaoui, Yuriy N. Malyar, Evgeniy V. Elsuf’ev, et al. "Food Xanthan Polysaccharide Sulfation Process with Sulfamic Acid." Foods 10, no. 11 (October 25, 2021): 2571. http://dx.doi.org/10.3390/foods10112571.
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Xanthan is an important polysaccharide with many beneficial properties. Sulfated xanthan derivatives have anticoagulant and antithrombotic activity. This work proposes a new method for the synthesis of xanthan sulfates using sulfamic acid. Various N-substituted ureas have been investigated as process activators. It was found that urea has the greatest activating ability. BBD of xanthan sulfation process with sulfamic acid in 1,4-dioxane has been carried out. It was shown that the optimal conditions for the sulfation of xanthan (13.1 wt% sulfur content) are: the amount of sulfating complex per 1 g of xanthan is 3.5 mmol, temperature 90 °C, duration 2.3 h. Sulfated xanthan with the maximum sulfur content was analyzed by physicochemical methods. Thus, in the FTIR spectrum of xanthan sulfate, in comparison with the initial xanthanum, absorption bands appear at 1247 cm−1, which corresponds to the vibrations of the sulfate group. It was shown by GPC chromatography that the starting xanthan gum has a bimodal molecular weight distribution of particles, including a high molecular weight fraction with Mw > 1000 kDa and an LMW fraction with Mw < 600 kDa. It was found that the Mw of sulfated xanthan gum has a lower value (~612 kDa) in comparison with the original xanthan gum, and a narrower molecular weight distribution and is characterized by lower PD values. It was shown by thermal analysis that the main decomposition of xanthan sulfate, in contrast to the initial xanthan, occurs in two stages. The DTG curve has two pronounced peaks, with maxima at 226 and 286 °C.
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McCormick, Christopher John, Christopher I. Newbold, and Anthony R. Berendt. "Sulfated glycoconjugates enhance CD36-dependent adhesion ofPlasmodium falciparum–infected erythrocytes to human microvascular endothelial cells." Blood 96, no. 1 (July 1, 2000): 327–33. http://dx.doi.org/10.1182/blood.v96.1.327.
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Abstract A novel adhesive pathway that enhances the adhesion ofPlasmodium falciparum-infected erythrocytes (IEs) to endothelial cells has been identified. The sulfated glycoconjugates heparin, fucoidan, dextran sulfate 5000, and dextran sulfate 500 000 caused a dramatic increase in adhesion of IEs to human dermal microvascular endothelial cells. The same sulfated glycoconjugates had little effect on IE adhesion to human umbilical vein endothelial cells, a CD36-negative cell line. The effect was abolished by a monoclonal antibody directed against CD36, suggesting that enhanced adhesion to endothelium is dependent on CD36. No effect was observed on adhesion to purified platelet CD36 cells immobilized on plastic. The same sulfated glycoconjugates enhanced adhesion of infected erythrocytes to COS cells transfected with CD36, and this was inhibited by the CD36 monoclonal antibody. These findings demonstrate a role for sulfated glycoconjugates in endothelial adherence that may be important in determining the location and magnitude of sequestration through endogenous carbohydrates. In addition, they highlight possible difficulties that may be encountered from the proposed use of sulfated glycoconjugates as antiadhesive agents in patients with severe malaria.
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McCormick, Christopher John, Christopher I. Newbold, and Anthony R. Berendt. "Sulfated glycoconjugates enhance CD36-dependent adhesion ofPlasmodium falciparum–infected erythrocytes to human microvascular endothelial cells." Blood 96, no. 1 (July 1, 2000): 327–33. http://dx.doi.org/10.1182/blood.v96.1.327.013k29_327_333.
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A novel adhesive pathway that enhances the adhesion ofPlasmodium falciparum-infected erythrocytes (IEs) to endothelial cells has been identified. The sulfated glycoconjugates heparin, fucoidan, dextran sulfate 5000, and dextran sulfate 500 000 caused a dramatic increase in adhesion of IEs to human dermal microvascular endothelial cells. The same sulfated glycoconjugates had little effect on IE adhesion to human umbilical vein endothelial cells, a CD36-negative cell line. The effect was abolished by a monoclonal antibody directed against CD36, suggesting that enhanced adhesion to endothelium is dependent on CD36. No effect was observed on adhesion to purified platelet CD36 cells immobilized on plastic. The same sulfated glycoconjugates enhanced adhesion of infected erythrocytes to COS cells transfected with CD36, and this was inhibited by the CD36 monoclonal antibody. These findings demonstrate a role for sulfated glycoconjugates in endothelial adherence that may be important in determining the location and magnitude of sequestration through endogenous carbohydrates. In addition, they highlight possible difficulties that may be encountered from the proposed use of sulfated glycoconjugates as antiadhesive agents in patients with severe malaria.
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Bone, Christine, Heidi Laderoute, Dyanne Brewer, Jocelyn Cameron, and E. James Squires. "91 The production of sulfated 16-androstene steroids by porcine Leydig cells and their potential role in the development of boar taint." Journal of Animal Science 97, Supplement_3 (December 2019): 77. http://dx.doi.org/10.1093/jas/skz258.159.
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Abstract Boar taint is a meat quality issue characterized by an off-odour or off-flavour in pork caused primarily by the accumulation of androstenone in the fat, but sensory estimates of boar taint do not always correlate with fat androstenone concentrations. However, these evaluations examine the sensory qualities of both the fat and lean tissue of heated pork products. Sulfated metabolites of androstenone are polar compounds that are abundantly produced by the Leydig cells of the testes, which may accumulate in more hydrophilic lean tissue. Therefore, the purpose of this study was to investigate the testicular metabolism of androstenone, which is responsible for the high production of sulfated androstenone metabolites. Leydig cells were isolated from 7-month-old Yorkshire, Duroc and terminal cross [Duroc x (Landrace x Yorkshire)] (n = 3) boars and incubated with radiolabeled androstenone for 8 hours. The proportion of sulfated metabolites produced was quantified using reverse phase high performance liquid chromatography (HPLC) and radioisotope detection. The sulfated metabolites were subsequently identified using liquid chromatography-mass spectrometry (LC-MS/MS). Statistical analysis was conducted using a one-way ANOVA in SAS. Following isolation and analysis with LC-MS/MS, the sulfated metabolites were identified as androstenol-3-sulfate and two major sulfated forms of androstenone. Additionally, removal of the sulfate group from these two sulfated forms of androstenone returned the parent compound androstenone, and not a hydroxylated metabolite. The average production of sulfated androstenol produced across all boars was 52.1±8.6%, which was not significantly different (P = 0.7) from the average production of sulfated androstenone (47.9±8.6%). The results of this study indicate that androstenone is directly sulfated, which allows these sulfated metabolites to function as steroid reservoirs that can enzymatically regenerate free androstenone within hydrophilic lean tissue. Alternatively, these metabolites may accumulate in the lean tissue, which we are proposing as a novel mechanism that contributes to the development of boar taint.
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Lederman, S., R. Gulick, and L. Chess. "Dextran sulfate and heparin interact with CD4 molecules to inhibit the binding of coat protein (gp120) of HIV." Journal of Immunology 143, no. 4 (August 15, 1989): 1149–54. http://dx.doi.org/10.4049/jimmunol.143.4.1149.
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Abstract Dextran sulfate, heparin, and certain other sulfated polysaccharides potently inhibit the adsorption of HIV to CD4+ cells. The mechanism of this inhibition is unclear and, specifically, it is unknown if these agents act at the level of CD4-gp120 binding. For example, previous reports have demonstrated that dextran sulfate does not inhibit the cell surface binding of anti-CD4 mAb known to be directed at the gp120 binding site. In order to confirm and extend these observations, in the present study, it was shown that dextran sulfate does not inhibit the binding of OKT4A, OKT4C, Leu3a, or B66.6 to CD4+ cells as measured by cytofluorography. Next, recombinant forms of CD4 (rT4) and gp120 (rgp120) were utilized to directly study their molecular interaction in the absence of other viral or cellular structures. Reciprocal solid phase ELISA assays were developed to study directly the effects of sulfated polysaccharides on the binding of rT4 to immobilized rgp120 and vice versa. Dextran sulfate, heparin, and fucoidan, but not chondroitin sulfate, inhibited the binding of rgp120 to rT4. Importantly, dextran sulfate and heparin pre-treatment of immobilized rT4, but not immobilized rgp120, inhibited rT4-rgp120 binding. Taken together, these data suggest that while both sulfated polysaccharides and anti-CD4 mAb inhibit gp120 binding, the sulfated polysaccharides interact with sites on CD4 that are distinct from those with which the antibodies bind.
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Groggel, G. C., G. N. Marinides, P. Hovingh, E. Hammond, and A. Linker. "Inhibition of rat mesangial cell growth by heparan sulfate." American Journal of Physiology-Renal Physiology 258, no. 2 (February 1, 1990): F259—F265. http://dx.doi.org/10.1152/ajprenal.1990.258.2.f259.
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The ability of heparan sulfate, an endogenous component of the glomerulus, to regulate the growth of cultured rat mesangial cells was investigated. Heparan sulfate caused a dose-dependent inhibition of rat mesangial cell growth, 85% inhibition compared with controls at the highest dose (1,000 micrograms/ml). Chondroitin sulfate produced no inhibition. The low-sulfated fraction of heparan sulfate (9%) produced more inhibition than the high-sulfated fraction (13%), 90 +/- 1 vs. 71 +/- 2% (P = 0.002). The effects of the heparan sulfate were completely reversible. Treatment of heparan sulfate with heparitinase increased the degree of inhibition, 71 +/- 1 vs. 84 +/- 1% (P less than 0.001). Four different oligosaccharides derived from heparan sulfate and heparin were tested for their ability to inhibit growth. One of the oligosaccharides, low-sulfated (10%), caused significant inhibition, 76 +/- 2%. Heparan sulfate was also able to inhibit the growth of Swiss 3T3 fibroblasts (63 +/- 5%). This inhibition was less marked than that seen with mesangial cells. Thus heparan sulfate was able to significantly inhibit rat mesangial cell growth in culture. Alterations in glomerular heparan sulfate may play an important role in alterations in mesangial cell growth.
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Wang, Yaping, Xiaobo Li, and Shunlin Ren. "Cholesterol Metabolites 25-Hydroxycholesterol and 25-Hydroxycholesterol 3-Sulfate Are Potent Paired Regulators: From Discovery to Clinical Usage." Metabolites 11, no. 1 (December 25, 2020): 9. http://dx.doi.org/10.3390/metabo11010009.
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Oxysterols have long been believed to be ligands of nuclear receptors such as liver × receptor (LXR), and they play an important role in lipid homeostasis and in the immune system, where they are involved in both transcriptional and posttranscriptional mechanisms. However, they are increasingly associated with a wide variety of other, sometimes surprising, cell functions. Oxysterols have also been implicated in several diseases such as metabolic syndrome. Oxysterols can be sulfated, and the sulfated oxysterols act in different directions: they decrease lipid biosynthesis, suppress inflammatory responses, and promote cell survival. Our recent reports have shown that oxysterol and oxysterol sulfates are paired epigenetic regulators, agonists, and antagonists of DNA methyltransferases, indicating that their function of global regulation is through epigenetic modification. In this review, we explore our latest research of 25-hydroxycholesterol and 25-hydroxycholesterol 3-sulfate in a novel regulatory mechanism and evaluate the current evidence for these roles.
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Carruthers, Vern B., Sebastian Håkansson, Olivia K. Giddings, and L. David Sibley. "Toxoplasma gondii Uses Sulfated Proteoglycans for Substrate and Host Cell Attachment." Infection and Immunity 68, no. 7 (July 1, 2000): 4005–11. http://dx.doi.org/10.1128/iai.68.7.4005-4011.2000.
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ABSTRACT Toxoplasma gondii is an obligate intracellular parasite that actively invades a wide variety of vertebrate cells, although the basis of this pervasive cell recognition is not understood. We demonstrate here that binding to the substratum and to host cells is partially mediated by interaction with sulfated glycosaminoglycans (GAGs). Addition of excess soluble GAGs blocked parasite attachment to serum-coated glass, thereby preventing gliding motility of extracellular parasites. Similarly, excess soluble GAGs decreased the attachment of parasites to human host cells from a variety of lineages, including monocytic, fibroblast, endothelial, epithelial, and macrophage cells. The inhibition of parasite attachment by GAGs was observed with heparin and heparan sulfate and also with chondroitin sulfates, indicating that the ligands for attachment are capable of recognizing a broad range of GAGs. The importance of sulfated proteoglycan recognition was further supported by the demonstration that GAG-deficient mutant host cells, and wild-type cells treated enzymatically to remove GAGs, were partially resistant to parasite invasion. Collectively, these studies reveal that sulfated proteoglycans are one determinant used for substrate and cell recognition by Toxoplasma. The widespread distribution of these receptors may contribute to the broad host and tissue ranges of this highly successful intracellular parasite.
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Shubina, Larisa K., Anatoly I. Kalinovsky, Tatyana N. Makarieva, Sergey N. Fedorov, Sergey A. Dyshlovoy, Pavel S. Dmitrenok, Irina I. Kapustina, et al. "New Meroterpenoids from the Marine Sponge Aka coralliphaga." Natural Product Communications 7, no. 4 (April 2012): 1934578X1200700. http://dx.doi.org/10.1177/1934578x1200700418.
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Three new sulfated meroterpenoids containing sesquiterpene and hydroquinone moieties, namely siphonodictyal A sulfate (1), akadisulfate A (2) and akadisulfate B (3), along with the known siphonodictyal B3 and bis(sulfato)-cyclosiphonodictyol A were isolated from the sponge Aka coralliphaga. Their structures were elucidated on the basis of spectroscopic data. Akadisulfate B and siphonodictyal B3 showed a radical-scavenging activity comparable with that of the known lipophylic antioxidant BHT.
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Kaufmann, Christine, and Margret Sauter. "Sulfated plant peptide hormones." Journal of Experimental Botany 70, no. 16 (June 20, 2019): 4267–77. http://dx.doi.org/10.1093/jxb/erz292.
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Abstract Sulfated peptides are plant hormones that are active at nanomolar concentrations. The sulfation at one or more tyrosine residues is catalysed by tyrosylprotein sulfotransferase (TPST), which is encoded by a single-copy gene. The sulfate group is provided by the co-substrate 3´-phosphoadenosine 5´-phosphosulfate (PAPS), which links synthesis of sulfated signaling peptides to sulfur metabolism. The precursor proteins share a conserved DY-motif that is implicated in specifying tyrosine sulfation. Several sulfated peptides undergo additional modification such as hydroxylation of proline and glycosylation of hydroxyproline. The modifications render the secreted signaling molecules active and stable. Several sulfated signaling peptides have been shown to be perceived by leucine-rich repeat receptor-like kinases (LRR-RLKs) but have signaling pathways that, for the most part, are yet to be elucidated. Sulfated peptide hormones regulate growth and a wide variety of developmental processes, and intricately modulate immunity to pathogens. While basic research on sulfated peptides has made steady progress, their potential in agricultural and pharmaceutical applications has yet to be explored.
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Schlachter, Caleb R., Andrea O’Malley, Linda L. Grimes, John J. Tomashek, Maksymilian Chruszcz, and L. Andrew Lee. "Purification, Characterization, and Structural Studies of a Sulfatase from Pedobacter yulinensis." Molecules 27, no. 1 (December 24, 2021): 87. http://dx.doi.org/10.3390/molecules27010087.
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Sulfatases are ubiquitous enzymes that hydrolyze sulfate from sulfated organic substrates such as carbohydrates, steroids, and flavones. These enzymes can be exploited in the field of biotechnology to analyze sulfated metabolites in humans, such as steroids and drugs of abuse. Because genomic data far outstrip biochemical characterization, the analysis of sulfatases from published sequences can lead to the discovery of new and unique activities advantageous for biotechnological applications. We expressed and characterized a putative sulfatase (PyuS) from the bacterium Pedobacter yulinensis. PyuS contains the (C/S)XPXR sulfatase motif, where the Cys or Ser is post-translationally converted into a formylglycine residue (FGly). His-tagged PyuS was co-expressed in Escherichia coli with a formylglycine-generating enzyme (FGE) from Mycobacterium tuberculosis and purified. We obtained several crystal structures of PyuS, and the FGly modification was detected at the active site. The enzyme has sulfatase activity on aromatic sulfated substrates as well as phosphatase activity on some aromatic phosphates; however, PyuS did not have detectable activity on 17α-estradiol sulfate, cortisol 21-sulfate, or boldenone sulfate.
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Thornton, Mark, Laura Barkley, Justin C. Mason, and Sunil Shaunak. "Anti-Kaposi’s Sarcoma and Antiangiogenic Activities of Sulfated Dextrins." Antimicrobial Agents and Chemotherapy 43, no. 10 (October 1, 1999): 2528–33. http://dx.doi.org/10.1128/aac.43.10.2528.
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ABSTRACT Delivery of the sulfated polysaccharide dextrin 2-sulfate by the intraperitoneal route to the lymphatic circulation resulted in a clinically significant improvement in Kaposi’s sarcoma in three patients. Our in vitro studies show that although sulfated dextrins do not interfere with the growth of isolated human umbilical vein endothelial cells, they do inhibit the morphological differentiation of endothelial cells into tubes as well as reduce new vessel formation in a placental angiogenesis assay. The antiangiogenic effect of dextrin 6-sulfate is greater than that of dextrin 2-sulfate and is independent of their anti-human immunodeficiency virus type 1 activities.
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Tykesson, Emil, Marco Maccarana, Hanna Thorsson, Jian Liu, Anders Malmström, Ulf Ellervik, and Gunilla Westergren-Thorsson. "Recombinant dermatan sulfate is a potent activator of heparin cofactor II-dependent inhibition of thrombin." Glycobiology 29, no. 6 (April 23, 2019): 446–51. http://dx.doi.org/10.1093/glycob/cwz019.
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Abstract The glycosaminoglycan dermatan sulfate (DS) is a well-known activator of heparin cofactor II-dependent inactivation of thrombin. In contrast to heparin, dermatan sulfate has never been prepared recombinantly from material of non-animal origin. Here we report on the enzymatic synthesis of structurally well-defined DS with high anticoagulant activity. Using a microbial K4 polysaccharide and the recombinant enzymes DS-epimerase 1, dermatan 4-O-sulfotransferase 1, uronyl 2-O-sulfotransferase and N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase, several new glycostructures have been prepared, such as a homogenously sulfated IdoA-GalNAc-4S polymer and its 2-O-, 6-O- and 2,6-O-sulfated derivatives. Importantly, the recombinant highly 2,4-O-sulfated DS inhibits thrombin via heparin cofactor II, approximately 20 times better than heparin, enabling manipulation of vascular and extravascular coagulation. The potential of this method can be extended to preparation of specific structures that are of importance for binding and activation of cytokines, and control of inflammation and metastasis, involving extravasation and migration.
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Liu, Yixiang, Wenqiang Liu, Yanbo Wang, Yu Ma, Ling Huang, Chao Zou, Donghui Li, Min-Jie Cao, and Guang-Ming Liu. "Inhibitory Effect of Depolymerized Sulfated Galactans from Marine Red Algae on the Growth and Adhesion of Diarrheagenic Escherichia coli." Marine Drugs 17, no. 12 (December 10, 2019): 694. http://dx.doi.org/10.3390/md17120694.
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Active polysaccharides as safe and natural polymers against bacterial diarrhea have been reconsidered as an alternative to antibiotics. This work investigated the inhibiting effect of depolymerized sulfated galactans from Eucheuma serra and Gracilaria verrucosa on the growth and adhesion of diarrheagenic enterotoxigenic Escherichia coli (ETEC) K88. Results showed that the sulfated polysaccharides with molecular weight distribution ≤20.0 kDa exhibited antibacterial activity against ETEC K88. A structure–activity study revealed that the anti-ETEC K88 activity of sulfated polysaccharides is strictly determined by their molecular weight distribution, sulfate group content, and monosaccharide composition. In addition, the promoted nucleic acid release and the fluorescence quenching of membrane proteins were observed after the treatment with selected polysaccharides. Scanning electron microscopy further confirmed that the depolymerized sulfated galactans can effectively inhibit ETEC K88 adhesion. In conclusion, depolymerized sulfated galactans exhibited an inhibitory effect on the growth and adhesion of ETEC K88.
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Levdansky, Alexander V., Natalya Yu Vasilyeva, Yuriy N. Malyar, Alexander A. Kondrasenko, Olga Yu Fetisova, Aleksandr S. Kazachenko, Vladimir A. Levdansky, and Boris N. Kuznetsov. "An Efficient Method of Birch Ethanol Lignin Sulfation with a Sulfaic Acid-Urea Mixture." Molecules 27, no. 19 (September 26, 2022): 6356. http://dx.doi.org/10.3390/molecules27196356.
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For the first time, the process of birch ethanol lignin sulfation with a sulfamic acid-urea mixture in a 1,4-dioxane medium was optimized experimentally and numerically. The high yield of the sulfated ethanol lignin (more than 96%) and containing 7.1 and 7.9 wt % of sulfur was produced at process temperatures of 80 and 90 °C for 3 h. The sample with the highest sulfur content (8.1 wt %) was obtained at a temperature of 100 °C for 2 h. The structure and molecular weight distribution of the sulfated birch ethanol lignin was established by FTIR, 2D 1H and 13C NMR spectroscopy, and gel permeation chromatography. The introduction of sulfate groups into the lignin structure was confirmed by FTIR by the appearance of absorption bands characteristic of the vibrations of sulfate group bonds. According to 2D NMR spectroscopy data, both the alcohol and phenolic hydroxyl groups of the ethanol lignin were subjected to sulfation. The sulfated birch ethanol lignin with a weight average molecular weight of 7.6 kDa and a polydispersity index of 1.81 was obtained under the optimum process conditions. Differences in the structure of the phenylpropane units of birch ethanol lignin (syringyl-type predominates) and abies ethanol lignin (guaiacyl-type predominates) was manifested in the fact that the sulfation of the former proceeds more completely at moderate temperatures than the latter. In contrast to sulfated abies ethanol lignin, the sulfated birch ethanol lignin had a bimodal and wider molecular weight distribution, as well as less thermal stability. The introduction of sulfate groups into ethanol lignin reduced its thermal stability.
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Ustyuzhanina, Nadezhda E., Maria I. Bilan, Andrey S. Dmitrenok, Eugenia A. Tsvetkova, Sofya P. Nikogosova, Cao Thi Thuy Hang, Pham Duc Thinh, et al. "Fucose-Rich Sulfated Polysaccharides from Two Vietnamese Sea Cucumbers Bohadschia argus and Holothuria (Theelothuria) spinifera: Structures and Anticoagulant Activity." Marine Drugs 20, no. 6 (June 6, 2022): 380. http://dx.doi.org/10.3390/md20060380.
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Fucosylated chondroitin sulfates (FCSs) FCS-BA and FCS-HS, as well as fucan sulfates (FSs) FS-BA-AT and FS-HS-AT were isolated from the sea cucumbers Bohadschia argus and Holothuria (Theelothuria) spinifera, respectively. Purification of the polysaccharides was carried out by anion-exchange chromatography on DEAE-Sephacel column. Structural characterization of polysaccharides was performed in terms of monosaccharide and sulfate content, as well as using a series of non-destructive NMR spectroscopic methods. Both FCSs were shown to contain a chondroitin core [→3)-β-d-GalNAc-(1→4)-β-d-GlcA-(1→]n bearing sulfated fucosyl branches at O-3 of every GlcA residue in the chain. These fucosyl residues were different in pattern of sulfation: FCS-BA contained Fuc2S4S, Fuc3S4S and Fuc4S at a ratio of 1:8:2, while FCS-HS contained these residues at a ratio of 2:2:1. Polysaccharides differed also in content of GalNAc4S6S and GalNAc4S units, the ratios being 14:1 for FCS-BA and 4:1 for FCS-HS. Both FCSs demonstrated significant anticoagulant activity in clotting time assay and potentiated inhibition of thrombin, but not of factor Xa. FS-BA-AT was shown to be a regular linear polymer of 4-linked α-L-fucopyranose 3-sulfate, the structure being confirmed by NMR spectra of desulfated polysaccharide. In spite of considerable sulfate content, FS-BA-AT was practically devoid of anticoagulant activity. FS-HS-AT cannot be purified completely from contamination of some FCS. Its structure was tentatively represented as a mixture of chains identical with FS-BA-AT and other chains built up of randomly sulfated alternating 4- and 3-linked α-L-fucopyranose residues.
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Vrba, Jiří, Barbora Papoušková, Pavel Kosina, Kateřina Lněničková, Kateřina Valentová, and Jitka Ulrichová. "Identification of Human Sulfotransferases Active towards Silymarin Flavonolignans and Taxifolin." Metabolites 10, no. 8 (August 12, 2020): 329. http://dx.doi.org/10.3390/metabo10080329.
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Natural phenolic compounds are known to be metabolized by phase II metabolic reactions. In this study, we examined the in vitro sulfation of the main constituents of silymarin, an herbal remedy produced from the fruits of the milk thistle. The study focused on major flavonolignan constituents, including silybin A, silybin B, isosilybin A, isosilybin B, silychristin, and silydianin, as well as the flavonoid taxifolin. Using ultra-high-performance liquid chromatography coupled with tandem mass spectrometry (UHPLC-MS), individual flavonolignans and taxifolin were found to be sulfated by human liver and human intestinal cytosols. Moreover, experiments with recombinant enzymes revealed that human sulfotransferases (SULTs) 1A1*1, 1A1*2, 1A2, 1A3, 1B1, 1C4, and 1E1 catalyzed the sulfation of all of the tested compounds, with the exception of silydianin, which was not sulfated by SULT1B1 and SULT1C4. The sulfation products detected were monosulfates, of which some of the major ones were identified as silybin A 20-O-sulfate, silybin B 20-O-sulfate, and isosilybin A 20-O-sulfate. Further, we also observed the sulfation of the tested compounds when they were tested in the silymarin mixture. Sulfates of flavonolignans and of taxifolin were produced by incubating silymarin with all of the above SULT enzymes, with human liver and intestinal cytosols, and also with human hepatocytes, even though the spectrum and amount of the sulfates varied among the metabolic models. Considering our results and the expression patterns of human sulfotransferases in metabolic tissues, we conclude that flavonolignans and taxifolin can potentially undergo both intestinal and hepatic sulfation, and that SULTs 1A1, 1A3, 1B1, and 1E1 could be involved in the biotransformation of the constituents of silymarin.
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Olczyk, Pawel, Katarzyna Komosinska-Vassev, Katarzyna Winsz-Szczotka, Jerzy Stojko, Katarzyna Klimek, and Ewa M. Kozma. "Propolis Induces Chondroitin/Dermatan Sulphate and Hyaluronic Acid Accumulation in the Skin of Burned Wound." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/290675.
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Changes in extracellular matrix glycosaminoglycans during the wound repair allowed us to apply the burn model in which therapeutic efficacy of propolis and silver sulfadiazine was compared. Burns were inflicted on four pigs. Glycosaminoglycans isolated from healthy and burned skin were quantified using a hexuronic acid assay, electrophoretic fractionation, and densitometric analyses. Using the reverse-phase HPLC the profile of sulfated disaccharides released by chondroitinase ABC from chondroitin/dermatan sulfates was estimated. Chondroitin/dermatan sulfates and hyaluronic acid were found in all samples. Propolis stimulated significant changes in the content of particular glycosaminoglycan types during burn healing. Glycosaminoglycans alterations after silver sulfadiazine application were less expressed. Propolis maintained high contribution of 4-O-sulfated disaccharides to chondroitin/dermatan sulfates structure and low level of 6-O-sulfated ones throughout the observed period of healing. Propolis led to preservation of significant contribution of disulfated disaccharides especially 2,4-O-disulfated ones to chondroitin sulfates/dermatan sulfates structure throughout the observed period of healing. Our findings demonstrate that propolis accelerates the burned tissue repair by stimulation of the wound bed glycosaminoglycan accumulation needed for granulation, tissue growth, and wound closure. Moreover, propolis accelerates chondroitin/dermatan sulfates structure modification responsible for binding growth factors playing the crucial role in the tissue repair.
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Townsend, Guy E., Lennart S. Forsberg, and David H. Keating. "Mesorhizobium loti Produces nodPQ-Dependent Sulfated Cell Surface Polysaccharides." Journal of Bacteriology 188, no. 24 (October 6, 2006): 8560–72. http://dx.doi.org/10.1128/jb.01035-06.
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ABSTRACT Leguminous plants and bacteria from the family Rhizobiaceae form a symbiotic relationship, which culminates in novel plant structures called root nodules. The indeterminate symbiosis that forms between Sinorhizobium meliloti and alfalfa requires biosynthesis of Nod factor, a β-1,4-linked lipochitooligosaccharide that contains an essential 6-O-sulfate modification. S. meliloti also produces sulfated cell surface polysaccharides, such as lipopolysaccharide (LPS). The physiological function of sulfated cell surface polysaccharides is unclear, although mutants of S. meliloti with reduced LPS sulfation exhibit symbiotic abnormalities. Using a bioinformatic approach, we identified a homolog of the S. meliloti carbohydrate sulfotransferase, LpsS, in Mesorhizobium loti. M. loti participates in a determinate symbiosis with the legume Lotus japonicus. We showed that M. loti produces sulfated forms of LPS and capsular polysaccharide (KPS). To investigate the physiological function of sulfated polysaccharides in M. loti, we identified and disabled an M. loti homolog of the sulfate-activating genes, nodPQ, which resulted in undetectable amounts of sulfated cell surface polysaccharides and a cysteine auxotrophy. We concomitantly disabled an M. loti cysH homolog, which disrupted cysteine biosynthesis without reducing cell surface polysaccharide sulfation. Our experiments demonstrated that the nodPQ mutant, but not the cysH mutant, showed an altered KPS structure and a diminished ability to elicit nodules on its host legume, Lotus japonicus. Interestingly, the nodPQ mutant also exhibited a more rapid growth rate and appeared to outcompete wild-type M. loti for nodule colonization. These results suggest that sulfated cell surface polysaccharides are required for optimum nodule formation but limit growth rate and nodule colonization in M. loti.
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Panin, G., S. Naia, R. Dall'Amico, L. Chiandetti, F. Zachello, C. Catassi, L. Felici, and G. V. Coppa. "Simple spectrophotometric quantification of urinary excretion of glycosaminoglycan sulfates." Clinical Chemistry 32, no. 11 (November 1, 1986): 2073–76. http://dx.doi.org/10.1093/clinchem/32.11.2073.
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Abstract We describe a simple, rapid, precise, and sensitive spectrophotometric method for measuring urinary glycosaminoglycan (GAG) sulfate excretion. The GAG sulfates are precipitated with cetylpyridinium chloride, resuspended in water, and mixed with the basic dye 1,9-dimethylmethylene blue to produce a complex with the polyanionic molecule of sulfated GAGs. Absorbance is read at 535 nm. The standard curve for reaction was linear up to 12 micrograms of the different GAGs: dermatan sulfate, heparan sulfate, keratan sulfate, chondroitin 4-sulfate, and chondroitin 6-sulfate. Within- and between-run precision (CV), measured at three different GAG concentrations (normal and pathological), varied from 1.6% to 2.5% and from 1.8% to 4.5%, respectively. Analytical recovery ranged from 71% to 107%. Urinary GAG excretion, measured by this procedure, correlates (r = 0.837; p less than 0.001) with the values obtained with the borate-carbazole reaction (Anal Biochem 1962;4:330-4).
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Bai, Shiming, Davaanyam Budragchaa, Shuqin Han, Taisei Kanamoto, Hideki Nakashima, and Takashi Yoshida. "Sulfated Alkyl Glucopyranans with Potent Antiviral Activity Synthesized by Ring-Opening Copolymerization of Anhydroglucose and Alkyl Anhydroglucose Monomers." International Journal of Polymer Science 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/317420.
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Sulfated glucopyranans having long alkyl groups were prepared by the ring-opening copolymerization of benzylated 1,6-anhydroglucopyranose with 3-O-octadecyl 1,6-anhydro-β-d-glucopyranose monomers, and subsequent deprotection and sulfation. Water-soluble sulfated glucopyranans with 2.8 and 4.7 mol% of 3-O-octadecyl group and lower molecular weights ofM-n= 2.5 × 103–5.1 × 103have potent anti-HIV activity at 0.05–1.25 μg/mL, even though sulfated polysaccharides with molecular weights belowM-n= 6 × 103had low anti-HIV activity. The interaction with poly-l-lysine as a model compound of proteins was analyzed by SPR, DSL, and zeta potential, indicating that the sulfated 3-O-octadecyl glucopyranans had high association and low dissociation rate constants, and the particle size increased after addition of poly-l-lysine. The anti-HIV activity was induced by electrostatic interaction between sulfate groups and amino groups of poly-l-lysine and by the synergistic effect of the hydrophobic long alkyl chain and hydrophilic sulfated group.