Oligosaccharide Fractions Research Articles

Obtaining and application of increased food and biological value iodinated products from lentils sprouted grain

The choice of research direction is related to the actual problem of production and distribution of functional purpose food products due to the spread of nutritional diseases and the lack of micronutrients in ordinary people and athletes diet. As an object for enrichment with iodine, it was suggested to use lentils, which is famous for its high protein content, low lipid and oligosaccharide content, and low inhibitory effect. The iodine accumulation occurs during germination, due to the use of a nutrient solution of the iodine inorganic form. In addition, the biochemical composition of the grain and the biological value of lentils are significantly improved: an increase in the content of total amino acids and vitamins is found to be 1.5-2.0 times, a mass fraction of the oligosaccharide fraction is observed. To determine the effect of technological processing on the degree of iodine conservation in lentils the grains were exposed to the following impact: grinding, extrusion, frying. An insignificant decrease in the amount of iodine during extrusion was noted and more significant one - during grinding. The obtained results of the determination of biological safety by the method of studying the effect of the investigated product on the growth response of ciliates allowed to confirm the safety of both fresh and dried sprouted grain of lentils. When studying the microbiology of grain by sowing on agarized selective diagnostic environments with subsequent identification of the qualitative and quantitative composition of microflora, including colony-forming units, deviations from the normative indices were not revealed. Experimental production of the extrudate was carried out, possible ways of its use in meat systems for improving the functional and technological properties of minced meat, as well as for independent use as snacks for the nutrition of athletes were suggested.

Structural, functional, and biological properties of potato peel oligosaccharides

Enzymatic hydrolysis of water-soluble polysaccharides from potato peel waste (PPPW) generates low molecular weight oligosaccharides with a yield of 63%. The oligosaccharides generated from potato peel polysaccharides (OPPP) were purified by Superdex-30 column. The results showed the presence of 8 peaks (OPPP1–OPPP8). The identification of all the fractions by chromatography analysis (GC-FID) illustrated that the most prominent residues were glucose with traces of galactose, arabinose and rhamnose. Finally, mass spectrometry (MALDI-ToF-ToF) analysis showed that the generated oligosaccharides were heterogeneous and contained different degree of polymerization (DP). Indeed, the obtained oligosaccharides fractions OPPP3, OPPP4, OPPP5, OPPP6 and OPPP7 were compose of the following degree of polymerization DP5; DP4; DP2; DP1 and DP1, respectively. Potato peel oligosaccharides (OPPP) efficiency were tested using different concentrations in functional properties. The results showed good foaming and emulsion properties. This study also aimed to investigate the antioxidant activity of OPPP. The items explored included the DPPH radical-scavenging capacity (IC50 OPPP=2.5mg/mL), reducing power (OD: 0.622±0.032 at a concentration of 20mg/mL), β-carotene bleaching inhibition activity (45.335±3.653%), and also the ABTS radical scavenging activity (14.835±0.1%).These findings indicate that potato peel oligosaccharides have potent antioxidant activities. Hence, one can suggest that these oligosaccharides might contribute as additives in food, pharmaceutical and cosmetic preparations.

Swallow root (Decalepis hamiltonii) pectic oligosaccharide (SRO1) induces cancer cell death via modulation of galectin-3 and survivin

Swallow root pectic oligosaccharide fraction (SRO1) from swallow root pectic polysaccharide (SRPP) possessed a molecular size of 831 Da. Structural analysis revealed that it is a rhamnogalacturonan I type, bearing arabinogalactan side chain with β-d-(1→4) galactose along with α-l-Araf (1→5)-α-l-Araf (1→3) structure on α-d-GalA-OAc-(1→2)-α-l-Rha-(1→4)- linear backbone. β-d (1→4) linked galactose being the specific sugar for galectin-3, SRO1 had potentials in inhibiting galectin-3 mediated cancer progression. SRO1 inhibited galectin-3 mediated agglutination, in vitro, effectively with MIC of 1.08 μg/ mL and down regulated mRNA levels of galectin-3 (∼92%) along with its downstream key protein that inhibits apoptosis – survivin (∼78%) suggesting the capability of SRO1 in inhibiting galectin-3 mediated cancer promoting pathway. This is the first report, which highlights the inhibition of interplay of galectin-3 and survivin by a dietary pectic oligosaccharide.

Efficient solid-phase synthesis of meningococcal capsular oligosaccharides enables simple and fast chemoenzymatic vaccine production

Neisseria meningitidis serogroups A and X are among the leading causes of bacterial meningitis in the African meningitis belt. Glycoconjugate vaccines, consisting of an antigenic carrier protein coupled to the capsular polysaccharide of the bacterial pathogen, are the most effective strategy for prevention of meningococcal disease. However, the distribution of effective glycoconjugate vaccines in this region is limited by the high cost of cultivating pathogens and purification of their capsular polysaccharides. Moreover, chemical approaches to synthesize oligosaccharide antigens have proven challenging. In the current study, we present a chemoenzymatic approach for generating tailored oligosaccharide fractions ready for activation and coupling to the carrier protein. In a first step, the elongation modes of recombinant capsular polymerases from Neisseria meningitidis serogroups A (CsaB) and X (CsxA) were characterized. We observed that CsaB is a distributive enzyme, and CsxA is a processive enzyme. Sequence comparison of these two stealth family proteins revealed a C-terminal extension in CsxA, which conferred processivity because of the existence of a second product-binding site. Deletion of the C-terminal domain converted CsxA into a distributive enzyme, allowing facile control of product length by adjusting the ratio of donor to acceptor sugars. Solid-phase fixation of the engineered capsular polymerases enabled rapid production of capsular polysaccharides with high yield and purity. In summary, the tools developed here provide critical steps toward reducing the cost of conjugate vaccine production, which will increase access in regions with the greatest need. Our work also facilitates efforts to study the relationship between oligosaccharide size and antigenicity.

Insights Into Glucan Polysaccharide Recognition Using Glucooligosaccharide Microarrays With Oxime-Linked Neoglycolipid Probes.

Glucans are polysaccharides of increasing biomedical interest because of their involvement in mechanisms of pathogen recognition, modulation of the immune system and anticancer, and health-promoting activities. Most of these biological activities occur through specific interactions with glucan-recognizing proteins. However, detailed molecular studies of glucan recognition remain a challenge mainly due to the inherent sequence heterogeneity and polydispersity of glucan polysaccharides, and associated difficulties in their purification and sequence characterization. It is thus ideal to have a series of sequence-defined glucooligosaccharides to represent the sequence diversity of glucan polysaccharides and to apply these to gain insight into glucan recognition processes. In this chapter, we describe the the methods for developing of oligosaccharide microarrays derived from a collection of glucans with different linkages based on the neoglycolipid (NGL) microarray system. The microscale oxime-ligation method has provided access in microarrays to over 150 sequence-defined glucooligosaccharides with different chain lengths, linkages, and branching patterns. We focus on the essential steps in the preparation of NGL-based glucooligosaccharide microarrays, which include (1) the depolymerization and purification methods to obtain oligosaccharide fractions of defined chain lengths; (2) a mass spectrometry-based method for linkage and sequence analysis of glucooligosaccharides; (3) improved procedures for preparation of oxime-linked NGLs from glucooligosaccharides for construction of microarrays; and (4) analyses of the recognition of these oligosaccharide sequences by various glucan-recognizing proteins: monoclonal antibodies, other proteins of the immune system such as Dectin-1 and DC-SIGN, and carbohydrate-binding modules of bacterial glycoside hydrolases.

Preparation and prebiotic potential of pectin oligosaccharides obtained from citrus peel pectin

Pectin oligosaccharide (POS) fractions were obtained by controlled chemical degradation of citrus peel pectin. By adjusting trifluoroacetic acid (TFA) concentration, three oligosaccharides were obtained, of molecular weight (Mw) range 3000–4000 Da, 2000–3000 Da and lower than 2000 Da. Varying hydrogen peroxide (H2O2) concentration and reaction time produced oligosaccharides of 3000–4000 Da and 2000–3000 Da. The relative proportions of acidic monosaccharide increased from 68.58% to 89.93% (TFA) and from 63.74% to 83.26% (H2O2) as the reaction conditions intensified. Prebiotic activity scores were used to quantify POS ability to promote selective growth of specific probiotics. Sample POSH1 from H2O2 degradation showed the highest prebiotic potential with prebiotic activity score 0.41 for Lactobacillus paracasei LPC-37 and 0.92 for Bifidobacterium bifidum ATCC 29521.

Correction: Identification and Characterization of Sulfated Carbohydrate-Binding Protein from Lactobacillus reuteri

[This corrects the article DOI: 10.1371/journal.pone.0083703.].

Acid hydrolysis of xylan polysaccharides fractions isolated from argan (Argania spinosa) leaves

Xylan polysaccharides previously obtained from argan (Argania spinosa) leaves by sequential alkaline extractions and purified by chromatography on Sepharose CL-4B were fragmented by acid hydrolysis in 2 M HCl. The resulting fragments were separated by gel filtration on Biogel P2. The oligosaccharide fractions obtained were then characterized by gas–liquid chromatography (GLC) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). The results show the presence of acidic oligosaccharide motifs, some of which composed of xylose and 4-O-methylglucuronic acid and other ones comprising rhamnose and galacturonic acid.

Structure elucidation of an immunostimulatory arabinoxylan-type polysaccharide prepared from young barley leaves (Hordeum vulgare L.)

We recently isolated an immunostimulating polysaccharide (BLE-P-I), which possesses a large proportion of arabinoxylan, from young barley leaves. In the present study, to elucidate the structural details of BLE-P-I, it was fractionated into enzyme-resistant fraction (BLE-P-I-X1) and arabinoxylan-rich oligosaccharide fraction (BLE-P-I-X2) after endo-xylanase hydrolysis. Commercial wheat arabinoxylan was also fractionated into WAX-XI and WAX-X2 after the same treatment. BLE-P-I-X2 consisted of arabinose and xylose, including 11 types of neutral glycosidic linkages, whereas WAX-X2 had less, with 6 types of linkages. Mass spectrometric results indicated that WAX-X2 was composed of a xylan backbone bearing only arabinose. In contrast, BLE-P-I-X2 consisted of a xylan backbone with acetate, arabinose, galactose, glucuronic acid, and 4-O-methylglucuronic acid, resembling structural characteristics as glucuronoarabinoxylan. Macrophage-stimulatory activity showed that BLE-P-I-X2 has a role in the expression of the activity. These results indicate that the structural complexity of arabinoxylan seems to be responsible for the immunomodulatory activity in barley leaf.

Isolation and Structural Characterization of an Oligosaccharide Produced by Bacillus subtilis in a Maltose-Containing Medium

Among 116 bacterial strains isolated from Korean fermented foods, one strain (SS-76) was selected for producing new oligosaccharides in a basal medium containing maltose as the sole source of carbon. Upon morphological characterization using scanning electron microscopy, the cells of strain SS-76 appeared rod-shaped; subsequent 16S rRNA gene sequence analysis revealed that strain SS-76 was phylogenetically close to Bacillus subtilis. The main oligosaccharide fraction B extracted from the culture supernatant of B. subtilis SS-76 was purified by high performance liquid chromatography. Subsequent structural analysis revealed that this oligosaccharide consisted only of glucose, and methylation analysis indicated similar proportions of glucopyranosides in the 6-linkage, 4-linkage, and non-reducing terminal positions. Matrix-assisted laser-induced/ionization time-of-flight/mass spectrometry and electrospray ionization-based liquid chromatography-mass spectrometry/mass spectrometry analyses suggested that this oligosaccharide consisted of a trisaccharide unit with 1,6- and 1,4-glycosidic linkages. The anomeric signals in the 1H-nuclear magnetic resonance spectrum corresponded to α-anomeric configurations, and the trisaccharide was finally identified as panose (α-D-glucopyranosyl-1,6-α-D-glucopyranosyl-1,4-D-glucose). These results suggest that B. subtilis SS-76 converts maltose into panose; strain SS-76 may thus find industrial application in the production of panose.

Effect of cranberry (Vaccinium macrocarpon) oligosaccharides on the formation of advanced glycation end-products.

BACKGROUND: The formation and accumulation of advanced glycation end-products (AGEs) are implicated in several chronic human illnesses including type-2 diabetes, renal failure, and neurodegenerative diseases. The cranberry (Vaccinium macrocarpon) fruit has been previously reported to show anti-AGEs effects, attributed primarily to its phenolic constituents. However, there is lack of similar data on the non-phenolic constituents found in the cranberry fruit, in particular, its carbohydrate constituents. Herein, a chemically characterized oligosaccharide-enriched fraction purified from the cranberry fruit was evaluated for its potential anti-AGEs and free radical scavenging effects.OBJECTIVE: The aim of this study was to evaluate the in vitro anti-AGEs and free radical scavenging effects of a chemically characterized oligosaccharide-enriched fraction purified from the North American cranberry (Vaccinium macrocarpon) fruit.METHOD: The cranberry oligosaccharide-enriched fraction was purified from cranberry hull powder and characterized based on spectroscopic and spectrometric (NMR, MALDI-TOF-MS, and HPAEC-PAD) data. The oligosaccharide-enriched fraction was evaluated for its anti-AGEs and free radical scavenging effects by the bovine serum albumin-fructose, and DPPH assays, respectively.RESULTS: Fractionation of cranberry hull material yielded an oligosaccharide-enriched fraction named Cranf1b-CL. The 1H NMR and MALDI-TOF-MS revealed that Cranf1b-CL consists of oligosaccharides ranging primarily from 6-mers to 9-mers. The monosaccharide composition of Cranf1b-CL was arabinose (25%), galactose (5%), glucose (47%) and xylose (23%). In the bovine serum albumin-fructose assay, Cranf1b-CL inhibited AGEs formation in a concentration-dependent manner with comparable activity to the synthetic antiglycating agent, aminoguanidine, used as the positive control (57 vs. 75%; both at 500μg/mL). In the DPPH free radical scavenging assay, Cranf1b-CL showed superior activity to the synthetic commercial antioxidant, butylated hydroxytoluene, used as the positive control (IC50 = 680 vs. 2200μg/mL, respectively).CONCLUSION: The in vitro anti-AGEs and free radical scavenging effects of cranberry oligosaccharides support previous data suggesting that these constituents may also contribute to biological effects of the whole fruit beyond its phenolic constituents alone. Also, this is the first study to evaluate a chemically characterized oligosaccharide fraction purified from the North American cranberry fruit for anti-AGEs and free radical scavenging properties.

Fractionation and analysis of lipopolysaccharide-derived oligosaccharides by zwitterionic-type hydrophilic interaction liquid chromatography coupled with electrospray ionisation mass spectrometry

Lipopolysaccharide (LPS, endotoxin) is a main surface antigen and virulence factor of Gram-negative bacteria. Regardless of the source of LPS, this molecule, isolated from the smooth forms of bacteria, is characterised by a general structural layout encompassing three regions: (i) an O-specific polysaccharide (O-PS) – a polymer of repeating oligosaccharide units, (ii) core oligosaccharide (OS), and (iii) the lipid A anchoring LPS in the outer membrane of the cell envelope of Gram-negative bacteria. Structural analysis usually requires degradation of LPS and further efficient separation of various poly- and oligosaccharide glycoforms.The hydrophilic interaction liquid chromatography (HILIC) was shown as an efficient technique for separation of labelled or native neutral and acidic glycans, glycopeptides, sialylated glycans, glycosylated and nonglycosylated peptides. Herein we adopted ZIC® (zwitterionic stationary phase covalently attached to porous silica)-HILIC technology in combination with electrospray ionisation mass spectrometry to separate different LPS-derived oligosaccharides. As a result three effective procedures have been developed: (i) to separate different core oligosaccharides of Escherichia coli R1 LOS, (ii) to separate RU-[Hep]-Kdo oligosaccharides from core OS glycoforms of Hafnia alvei PCM 1200 LPS, and (iii) to separate Hep and Kdo-containing mono, di-, tri- and tetrasaccharides of H. alvei PCM 1200 LPS. Moreover, some of developed analytical procedures were scaled to semi-preparative protocols and used to obtain highly-purified fractions of the interest in larger quantities required for future evaluation, analysis, and biological applications.

Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9

We previously showed that galectin-9 suppresses degranulation of mast cells through protein-glycan interaction with IgE. To elucidate the mechanism of the interaction in detail, we focused on identification and structural analysis of IgE glycans responsible for the galectin-9-induced suppression using mouse monoclonal IgE (TIB-141). TIB-141 in combination with the antigen induced degranulation of RBL-2H3 cells, which was almost completely inhibited by human and mouse galectin-9. Sequential digestion of TIB-141 with lysyl endopeptidase and trypsin resulted in the identification of a glycopeptide (H-Lys13-Try3; 48 amino acid residues) with a single N-linked oligosaccharide near the N terminus capable of neutralizing the effect of galectin-9 and another glycopeptide with two N-linked oligosaccharides (H-Lys13-Try1; 16 amino acid residues) having lower activity. Enzymatic elimination of the oligosaccharide chain from H-Lys13-Try3 and H-Lys13-Try1 completely abolished the activity. Removal of the C-terminal 38 amino acid residues of H-Lys13-Try3 with glutamyl endopeptidase, however, also resulted in loss of the activity. We determined the structures of N-linked oligosaccharides of H-Lys13-Try1. The galectin-9-binding fraction of pyridylaminated oligosaccharides contained asialo- and monosialylated bi/tri-antennary complex type oligosaccharides with a core fucose residue. The structures of the oligosaccharides were consistent with the sugar-binding specificity of galectin-9, whereas the nonbinding fraction contained monosialylated and disialylated biantennary complex type oligosaccharides with a core fucose residue. Although the oligosaccharides linked to H-Lys13-Try3 could not be fully characterized, these results indicate the possibility that cooperative binding of oligosaccharide and neighboring polypeptide structures of TIB-141 to galectin-9 affects the overall affinity and specificity of the IgE-lectin interaction.

The Effect of Dry Yeast Fermentation on Chemical Composition and Protein Characteristics of Blue Lupin Seeds.

The effect of 24-hour fermentation of lupin seeds by different yeast strains on their chemical composition was determined. After fermentation, the mass fraction of proteins increased and their in vitro digestibility and biological activity significantly improved. The amino acid profile of fermented products was similar to that of raw lupin seeds. The significant reduction in the mass fraction of oligosaccharides and phytate, but not of alkaloids was found. The pH level of fermented products decreased as a consequence of the increase of lactic and propionic acid mass fractions. The most favourable changes in the chemical composition of blue lupin seeds were obtained in fermentation with Saccharomyces cerevisiae baker's yeast and Fermivin 7013 strain.

Isolation of oligosaccharide fraction from wheat cell culture and determination of its monosaccharide composition

Oligosaccharides, being a part of plant cell wall, can be secreted to the intercellular space and perform «signaling» activity on plant tissues – high physiological activity in very low concentrations.Oligosaccharide (OS) fraction was obtained from extracellular liquid wheat cell culture by size exclusion chromatography. Monosaccharide composition of extracellular OS has been determined by HPLC Ionic chromatography. It was shown that extracellular OS contain glucose, xylose, arabinose, galactose, fructose and rhamnose monosaccharide residues.

Factor affecting the 3′ sialyllactose, 6′ sialyllactose and disialyllactose content in caprine colostrum and milk: Breed and parity

The fraction of oligosaccharides (OS) in goat milk is becoming increasingly important for its bio-functional role. OS profile of goat milk shows more similarity to human milk in comparison to bovine and ovine milk, in addition goat milk contains sialylated OS which play an important role in brain development and increase immunity in infants.In the first study, in order to improve the knowledge on breed effect on sialyloligosaccharides (SOS), we have focused on three of the most representative SOS; 6′ sialyllactose (6′-SL), 3′ sialyllactose (3′-SL) and disialyllactose (DSL) in colostrum and milk from Saanen goats, a cosmopolitan breed, and from Garganica goats, native breed. Successively, we compared the SOS levels in colostrum and milk of Saanen goats in two different parity. The results showed a significant effect of breed on SOS content (P<0.05) and a significant interaction breed×sampling time occurred for 3′-SL (P<0.001) and 6′-SL (P<0.01). Concerning parity, a significant effect was found only for the 3′-SL content (P<0.05). The present finding is particularly relevant in order to preserve and improve native breed production in view of a sustainable land use.

Human plasma protein N-glycosylation.

Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.Electronic supplementary materialThe online version of this article (doi:10.1007/s10719-015-9626-2) contains supplementary material, which is available to authorized users.

Structural characterization of an intestinal immune system-modulating arabino-3,6-galactan-like polysaccharide from the above-ground part of Astragalus membranaceus (Bunge)

Arabino-3,6-galactan (AMA-1-b-PS2), an intestinal immunomodulatory compound, was purified from the above-ground portion of Astragalus membranaceus (Bunge). Its structure was characterized using sequential enzymatic digestion with exo-α-l-arabinofuranosidase (AFase) and exo-β-d-(1→3)-galactanase (GNase), producing small amounts of intermediate-sized and shorter oligosaccharide (AF-PS2-G2 and AF-PS2-G3) fractions, and a large GNase-resistant fraction (AF-PS2-G1). Simultaneous AFase and GNase digestion of the enzyme-resistant fraction produced two long fragments (AF3-PS2-G1-1-1 and AF3-PS2-G1-1-2). Products of GNase digestion of the upper fractions showed decreased intestinal immunomodulatory activity; the GNase-resistant fraction (AF-PS2-G1) retained significant activity. Sugar component, methylation, and FAB-MS analyses indicated that the oligosaccharides consisted of hexosyl tri- to hexa-decasaccharides and hexosyl di- to hepta-saccharides mainly comprising 6-linked Gal(f) and Gal(p); some were partially mono- or di-arabinosylated. These oligosaccharide fractions were attached to the non-reducing terminus of the β-d-(1→3)-galactan backbone as side chains at position 6. AMA-1-b-PS2 likely modulates both the systemic and gastric mucosal immune systems.

Lactobacillus rhamnosus GG SpaC pilin subunit binds to the carbohydrate moieties of intestinal glycoconjugates.

Lactobacillus rhamnosus GG (LGG) is a well-established probiotic strain. The beneficial properties of this strain are partially dependent on its prolonged residence in the gastrointestinal tract, and are likely influenced by its adhesion to the intestinal mucosa. The pilin SpaC subunit, located within the Spa pili structure, is the most well studied LGG adhesion factor. However, the binding epitopes of SpaC remain largely unknown. The aim of this study was to evaluate the binding properties of SpaC to the carbohydrate moieties of intestinal glycoconjugates using a recombinant SpaC protein. In a competitive enzyme-linked immunosorbent assay, SpaC binding was markedly reduced by addition of purified mucin and the mucin oligosaccharide fraction. Histochemical staining revealed that the binding of SpaC was drastically reduced by periodic acid treatment. Moreover, in the surface plasmon resonance-based Biacore assay, SpaC bound strongly to the carbohydrate moieties containing β-galactoside at the non-reducing terminus of glycolipids. We here provide the first demonstration that SpaC binds to the oligosaccharide chains of mucins, and that the carbohydrate moieties containing β-galactoside at the non-reducing termini of glycoconjugates play a crucial role in this binding. Our results demonstrate the importance of carbohydrates of SpaC for mucus interactions.

Anticoagulant and FGF/FGFR signal activating activities of the heparinoid propylene glycol alginate sodium sulfate and its oligosaccharides

Propylene glycol alginate sodium sulfate (PSS), prepared by chemical sulfation of alginate, has been used for treating cardiovascular diseases in China for nearly 30 years. In the current study, the PSS was hydrolyzed partially by an environment-friendly solid phase acid degradation method, and then separated by using a Bio-Gel P6 chromatographic column. Thirteen PSS oligosaccharide fractions were obtained and characterized by ESI-MS. The results of different coagulation assays showed that a high molecular weight and a higher degree of sulfation were essential for the anticoagulant activity of the PSS because the PSS oligosaccharides exhibited no detectable anticoagulant activity. In contrast, not only PSS but also certain oligosaccharides showed significant activities in stimulation of FGF1, 2, 7, 8, 9 or 10 induced cell proliferation in FGFR1c-expressing BaF3 cells. Such properties made the PSS and its oligosaccharides promising compounds in the regulation of FGF-dependent development, treatment of cancer, and wound healing processes.