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Special Issue "Oligosaccharides and Glyco-Conjugates"

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A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: closed (31 March 2014)

Special Issue Editors

Guest Editor
Prof. Dr. Marco Terreni (Website)

Department of Drug Sciences; School of Pharmacy; University of Pavia, Via Taramelli 12; 27100 Pavia, Italy
Interests: syndetic organic chemistry; medicinal chemistry; chemical biology; protein engineering; biocatalysis
Guest Editor
Dr. Caterina Temporini (Website)

Department of Drug Sciences; School of Pharmacy; University of Pavia, Via Taramelli 12; 27100 Pavia, Italy
Interests: analytical chemistry; medicinal chemistry; protein engeenering

Special Issue Information

Dear Colleagues,

Carbohydrates occur naturally as oligo- and polysaccharides and are often coupled to peptides. proteins and lipids. In particular, oligosaccharides and glyco-conjugates have key roles in a broad range of biological processes. In many cases, changes in the sugar structures can affect the biological properties of the parent compounds. Furthermore, functional properties of drugs such as solubility, pharmacokinetics or pharmacodynamics can be enhanced by the incorporation of carbohydrate moieties into the molecules.
Methods for synthesizing these molecules have, therefore, acquired immense importance, because it is not easy to isolate sufficient amounts of acceptable pure product from natural sources.
On the other hand, the structure of therapeutic bio-products is critically important for their efficacy and safety, and the ability to characterize it at various levels (from sequence to conformation) is critical not only at the quality control stage, but also throughout the discovery and design stages because these structural information enable to optimize and enhance their therapeutic profile in a rational fashion.
Many analytical technologies have been deeply improved in the last years for determining the exact structure of complex oligosaccharides and glyco-conjugates For example Liquid Chromatography coupled to mass spectrometry (LC-MS) offers a variety of approaches to study structure and behaviour of complex protein drugs and has already become a default tool for characterizing the covalent structure, including sequence and post-translational modifications such as glycosylation which is the most common PTM in currently developed biopharmaceuticals.
Research papers dealing with the study and development of new compounds as well as new synthetic approaches, including new enzymatic or chemoenzymatic methods, new methods for analytical and biological characterization of oligosaccharides and glyco-conjugates, are welcomed for inclusion into this Special Issue of Molecules. Review articles, particularly those dealing with retrospective analyses of prior successes in the discovery and/or development of new drugs based on oligosaccharides and glyco-conjugates, are also welcomed for inclusion.

Prof. Dr. Marco Terreni
Dr. Caterina Temporini
Guest Editors

Submission

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed Open Access monthly journal published by MDPI.

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Keywords

  • oligosaccharides
  • glycopeptides
  • glycoproteins
  • glycolipids
  • synthesis
  • analysis
  • structure characterization
  • biological activity
  • structure based drug design
  • drug discovery and development

Published Papers (12 papers)

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Research

Open AccessArticle Synthesis and Molecular Structure of the 5-Methoxycarbonylpentyl α-Glycoside of the Upstream, Terminal Moiety of the O-Specific Polysaccharide of Vibrio cholerae O1, Serotype Inaba
Molecules 2015, 20(2), 2892-2902; doi:10.3390/molecules20022892
Received: 14 January 2015 / Accepted: 5 February 2015 / Published: 11 February 2015
PDF Full-text (1919 KB) | HTML Full-text | XML Full-text
Abstract
The trimethylsilyl trifluoromethanesulfonate (TMSOTf)-catalyzed reaction of methyl 6-hydroxyhexanoate with 3-O-benzyl-4-(2,4-di-O-acetyl-3-deoxy-L-glycero-tetronamido)-4,6-dideoxy-2-O-levulinoyl-α-d-mannopyranosyl trichloroacetimidate followed by a two-step deprotection (hydrogenolysis over Pd/C catalyst and Zemplén deacylation, to simultaneously remove the acetyl and levulinoyl groups) gave 5-(methoxycarbonyl)pentyl 4-(3-deoxy-L-glycero-tetronamido)-4,6-dideoxy-α-D-mannopyranoside. [...] Read more.
The trimethylsilyl trifluoromethanesulfonate (TMSOTf)-catalyzed reaction of methyl 6-hydroxyhexanoate with 3-O-benzyl-4-(2,4-di-O-acetyl-3-deoxy-L-glycero-tetronamido)-4,6-dideoxy-2-O-levulinoyl-α-d-mannopyranosyl trichloroacetimidate followed by a two-step deprotection (hydrogenolysis over Pd/C catalyst and Zemplén deacylation, to simultaneously remove the acetyl and levulinoyl groups) gave 5-(methoxycarbonyl)pentyl 4-(3-deoxy-L-glycero-tetronamido)-4,6-dideoxy-α-D-mannopyranoside. The structure of the latter, for which crystals were obtained in the analytically pure state for the first time, followed from its NMR and high-resolution mass spectra and was confirmed by X-ray crystallography. The molecule has two approximately linear components; a line through the aglycon intersects a line through the mannosyl and tetronylamido groups at 120°. The crystal packing separates the aglycon groups from the tetronylamido and mannosyl groups, with only C-H…O hydrogen bonding among the aglycon groups and N-H…O, O-H…O and C-H…O links among the tetronylamido and mannosyl groups. A carbonyl oxygen atom accepts the strongest O-H…O hydrogen bond and two strong C-H…O hydrogen bonds. The geometric properties were compared with those of related molecules. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle A Combinatorial Approach to Biophysically Characterise Chemokine-Glycan Binding Affinities for Drug Development
Molecules 2014, 19(7), 10618-10634; doi:10.3390/molecules190710618
Received: 22 May 2014 / Revised: 7 July 2014 / Accepted: 16 July 2014 / Published: 22 July 2014
Cited by 10 | PDF Full-text (439 KB) | HTML Full-text | XML Full-text
Abstract
Chemokine binding to glycosaminoglycans (GAGs) is recognised to be an important step in inflammation and other pathological disorders like tumor growth and metastasis. Although different ways and strategies to interfere with these interactions are being pursued, no major breakthrough in the development [...] Read more.
Chemokine binding to glycosaminoglycans (GAGs) is recognised to be an important step in inflammation and other pathological disorders like tumor growth and metastasis. Although different ways and strategies to interfere with these interactions are being pursued, no major breakthrough in the development of glycan-targeting drugs has been reported so far. We have engineered CXCL8 towards a dominant-negative form of this chemokine (dnCXCL8) which was shown to be highly active in various inflammatory animal models due to its inability to bind/activate the cognate CXCL8 GPC receptors on neutrophils in combination with its significantly increased GAG-binding affinity [1]. For the development of GAG-targeting chemokine-based biopharmaceuticals, we have established a repertoire of methods which allow the quantification of protein-GAG interactions. Isothermal fluorescence titration (IFT), surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and a novel ELISA-like competition assay (ELICO) have been used to determine Kd and IC50 values for CXCL8 and dnCXCL8 interacting with heparin and heparan sulfate (HS), the proto-typical members of the GAG family. Although the different methods gave different absolute affinities for the four protein-ligand pairs, the relative increase in GAG-binding affinity of dnCXCL8 compared to the wild type chemokine was found by all methods. In combination, these biophysical methods allow to discriminate between unspecific and specific protein-GAG interactions. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle Relative Quantitation of Glycopeptides Based on Stable Isotope Labeling Using MALDI-TOF MS
Molecules 2014, 19(7), 9944-9961; doi:10.3390/molecules19079944
Received: 31 March 2014 / Revised: 1 July 2014 / Accepted: 7 July 2014 / Published: 9 July 2014
Cited by 2 | PDF Full-text (572 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
We have developed an effective, sensitive method for quantitative glycopeptide profiling using stable isotope labeling and MALDI-TOF mass spectrometry (MS). In this study, we synthesized benzoic acid-d0 N-succinimidyl ester (BzOSu) and benzoic acid-d5 N-succinimidyl ester (d-BzOSu) as light and heavy isotope reagents [...] Read more.
We have developed an effective, sensitive method for quantitative glycopeptide profiling using stable isotope labeling and MALDI-TOF mass spectrometry (MS). In this study, we synthesized benzoic acid-d0 N-succinimidyl ester (BzOSu) and benzoic acid-d5 N-succinimidyl ester (d-BzOSu) as light and heavy isotope reagents for stable isotope quantification for the comparative analysis of glycopeptides. Using this approach provided enhanced ionization efficiency in both positive and negative modes by MALDI-TOF MS. These reagents were quantitatively reacted with glycopeptides from human serum IgG (hIgG) at a wide range of concentrations; the labeling efficiency of the glycopeptides showed high reproducibility and a good calibration curve was obtained. To demonstrate the practical utility of this approach, we characterized the structures of glycopeptides from hIgG and from IgG1 produced by myeloma plasma. The glycopeptides were quantitatively analyzed by mixing Bz-labeled IgG1 glycopeptides with d-Bz-labeled hIgG glycopeptides. Glycan structural identification of the hIgG glycopeptides was demonstrated by combining the highly specific recognition of endo-β-N-acetyl glucosaminidases from Streptococcus pyogenes (endoS) or from Streptococcus pneumoniae (endo-D) with MALDI-TOF MS analysis. The obtained data revealed the glycan profile and the ratio of glycan structural isomers containing a galactosylated extension on IgG1, IgG2 and IgG3 glycopetides. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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Open AccessArticle Characterization of Intact Neo-Glycoproteins by Hydrophilic Interaction Liquid Chromatography
Molecules 2014, 19(7), 9070-9088; doi:10.3390/molecules19079070
Received: 12 May 2014 / Revised: 18 June 2014 / Accepted: 19 June 2014 / Published: 30 June 2014
Cited by 4 | PDF Full-text (2269 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
In this study, an HPLC HILIC-UV method was developed for the analysis of intact neo-glycoproteins. During method development the experimental conditions evaluated involved different HILIC columns (TSKgel Amide-80 and ZIC-pHILIC), and water-acetonitrile mixtures containing various types of acids and [...] Read more.
In this study, an HPLC HILIC-UV method was developed for the analysis of intact neo-glycoproteins. During method development the experimental conditions evaluated involved different HILIC columns (TSKgel Amide-80 and ZIC-pHILIC), and water-acetonitrile mixtures containing various types of acids and salts. The final selected method was based on a TSKgel Amide-80 column and a mobile phase composed of acetonitrile and water both containing 10 mM HClO4. The influence of temperature and sample preparation on the chromatographic performances of the HILIC method was also investigated. The method was applied to the separation of neo-glycoproteins prepared starting from the model protein RNase A by chemical conjugation of different glycans. Using the method here reported it was possible to monitor by UV detection the glycosylation reaction and assess the distribution of neo-glycoprotein isoforms without laborious sample workup prior to analysis. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle High-Throughput Assay of Levansucrase Variants in Search of Feasible Catalysts for the Synthesis of Fructooligosaccharides and Levan
Molecules 2014, 19(6), 8434-8455; doi:10.3390/molecules19068434
Received: 28 March 2014 / Revised: 10 June 2014 / Accepted: 10 June 2014 / Published: 20 June 2014
Cited by 6 | PDF Full-text (1822 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Bacterial levansucrases polymerize fructose residues of sucrose to β-2,6 linked fructans—fructooligosaccharides (FOS) and levan. While β-2,1-linked FOS are widely recognized as prebiotics, the health-related effects of β-2,6 linked FOS are scarcely studied as they are not commercially available. Levansucrase Lsc3 (Lsc-3) of [...] Read more.
Bacterial levansucrases polymerize fructose residues of sucrose to β-2,6 linked fructans—fructooligosaccharides (FOS) and levan. While β-2,1-linked FOS are widely recognized as prebiotics, the health-related effects of β-2,6 linked FOS are scarcely studied as they are not commercially available. Levansucrase Lsc3 (Lsc-3) of Pseudomonas syringae pv. tomato has very high catalytic activity and stability making it a promising biotechnological catalyst for FOS and levan synthesis. In this study we evaluate feasibility of several high-throughput methods for screening and preliminary characterization of levansucrases using 36 Lsc3 mutants as a test panel. Heterologously expressed and purified His-tagged levansucrase variants were studied for: (1) sucrose-splitting activity; (2) FOS production; (3) ability and kinetics of levan synthesis; (4) thermostability in a Thermofluor assay. Importantly, we show that sucrose-splitting activity as well as the ability to produce FOS can both be evaluated using permeabilized levansucrase-expressing E. coli transformants as catalysts. For the first time we demonstrate the key importance of Trp109, His113, Glu146 and Glu236 for the catalysis of Lsc3. Cost-effective and high-throughput methods presented here are applicable not only in the levansucrase assay, but have a potential to be adapted for high-throughput (automated) study of other enzymes. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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Open AccessArticle FACE Analysis as a Fast and Reliable Methodology to Monitor the Sulfation and Total Amount of Chondroitin Sulfate in Biological Samples of Clinical Importance
Molecules 2014, 19(6), 7959-7980; doi:10.3390/molecules19067959
Received: 15 April 2014 / Revised: 23 May 2014 / Accepted: 27 May 2014 / Published: 12 June 2014
Cited by 1 | PDF Full-text (1475 KB) | HTML Full-text | XML Full-text
Abstract
Glycosaminoglycans (GAGs) due to their hydrophilic character and high anionic charge densities play important roles in various (patho)physiological processes. The identification and quantification of GAGs in biological samples and tissues could be useful prognostic and diagnostic tools in pathological conditions. Despite the [...] Read more.
Glycosaminoglycans (GAGs) due to their hydrophilic character and high anionic charge densities play important roles in various (patho)physiological processes. The identification and quantification of GAGs in biological samples and tissues could be useful prognostic and diagnostic tools in pathological conditions. Despite the noteworthy progress in the development of sensitive and accurate methodologies for the determination of GAGs, there is a significant lack in methodologies regarding sample preparation and reliable fast analysis methods enabling the simultaneous analysis of several biological samples. In this report, developed protocols for the isolation of GAGs in biological samples were applied to analyze various sulfated chondroitin sulfate- and hyaluronan-derived disaccharides using fluorophore-assisted carbohydrate electrophoresis (FACE). Applications to biologic samples of clinical importance include blood serum, lens capsule tissue and urine. The sample preparation protocol followed by FACE analysis allows quantification with an optimal linearity over the concentration range 1.0–220.0 µg/mL, affording a limit of quantitation of 50 ng of disaccharides. Validation of FACE results was performed by capillary electrophoresis and high performance liquid chromatography techniques. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle Direct 2,3-O-Isopropylidenation of α-D-Mannopyranosides and the Preparation of 3,6-Branched Mannose Trisaccharides
Molecules 2014, 19(5), 6683-6693; doi:10.3390/molecules19056683
Received: 31 March 2014 / Revised: 9 May 2014 / Accepted: 19 May 2014 / Published: 22 May 2014
Cited by 3 | PDF Full-text (279 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
A highly efficient, regioselective method for the direct 2,3-O-isopropylidenation of α-D-mannopyranosides is reported. Treatment of various α-D-mannopyranosides with 0.12 equiv of the TsOH·H2O and 2-methoxypropene at 70 °C gave 2,3-O-isopropylidene-α-D-mannopyranosides directly in 80%~90% yields. Based on [...] Read more.
A highly efficient, regioselective method for the direct 2,3-O-isopropylidenation of α-D-mannopyranosides is reported. Treatment of various α-D-mannopyranosides with 0.12 equiv of the TsOH·H2O and 2-methoxypropene at 70 °C gave 2,3-O-isopropylidene-α-D-mannopyranosides directly in 80%~90% yields. Based on this method, a 3,6-branched α-D-mannosyl trisaccharide was prepared in 50.4% total yield using p-nitrophenyl 2,3-O-isopropylidene-α-D-mannopyranoside as the starting material. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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Open AccessArticle Conformational Characterization of Ipomotaosides and Their Recognition by COX-1 and 2
Molecules 2014, 19(4), 5421-5433; doi:10.3390/molecules19045421
Received: 5 March 2014 / Revised: 18 April 2014 / Accepted: 21 April 2014 / Published: 24 April 2014
Cited by 1 | PDF Full-text (1346 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The aerial parts of Ipomoea batatas are described herein to produce four new resin glycosides, designated as ipomotaosides A, B, C, and D. Ipomotaoside A was found to present inhibitory activity on both cyclooxygenases. However, the conformational elucidation of these molecules may [...] Read more.
The aerial parts of Ipomoea batatas are described herein to produce four new resin glycosides, designated as ipomotaosides A, B, C, and D. Ipomotaoside A was found to present inhibitory activity on both cyclooxygenases. However, the conformational elucidation of these molecules may be difficult due to their high flexibility. In this context, the current work presents a conformational characterization of ipomotaosides A–D in aqueous and nonaqueous solvents. The employed protocol includes metadynamics evaluation and unrestrained molecular dynamics simulations (MD). The obtained data provided structural models for the ipomotaosides in good agreement with previous ROESY distances measured in pyridine. Accordingly, the most abundant conformation of ipomotaoside A in solution was employed in flexible docking studies, providing a structural basis for the compound’s inhibition of COX enzymes. The so-obtained complex supports resin glycosides’ role as original scaffolds for future studies, aiming at structural optimization and development of potential new anti-inflammatory agents. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle MALDI-TOF MS Analysis of Cellodextrins and Xylo-oligosaccharides Produced by Hindgut Homogenates of Reticulitermes santonensis
Molecules 2014, 19(4), 4578-4594; doi:10.3390/molecules19044578
Received: 11 February 2014 / Revised: 2 April 2014 / Accepted: 4 April 2014 / Published: 11 April 2014
PDF Full-text (812 KB) | HTML Full-text | XML Full-text
Abstract
Hindgut homogenates of the termite Reticulitermes santonensis were incubated with carboxymethyl cellulose (CMC), crystalline celluloses or xylan substrates. Hydrolysates were analyzed with matrix-assisted laser desorption/ionization coupled to time-of-flight mass spectrometry (MALDI-TOF MS). The method was first set up using acid hydrolysis analysis [...] Read more.
Hindgut homogenates of the termite Reticulitermes santonensis were incubated with carboxymethyl cellulose (CMC), crystalline celluloses or xylan substrates. Hydrolysates were analyzed with matrix-assisted laser desorption/ionization coupled to time-of-flight mass spectrometry (MALDI-TOF MS). The method was first set up using acid hydrolysis analysis to characterize non-enzymatic profiles. Commercial enzymes of Trichoderma reesei or T. longibrachiatum were also tested to validate the enzymatic hydrolysis analysis. For CMC hydrolysis, data processing and visual display were optimized to obtain comprehensive profiles and allow rapid comparison and evaluation of enzymatic selectivity, according to the number of substituents of each hydrolysis product. Oligosaccharides with degrees of polymerization (DPs) ranging from three to 12 were measured from CMC and the enzymatic selectivity was demonstrated. Neutral and acidic xylo-oligosaccharides with DPs ranging from three to 11 were measured from xylan substrate. These results are of interest for lignocellulose biomass valorization and demonstrated the potential of termites and their symbiotic microbiota as a source of interesting enzymes for oligosaccharides production. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle Atomic Model and Micelle Dynamics of QS-21 Saponin
Molecules 2014, 19(3), 3744-3760; doi:10.3390/molecules19033744
Received: 27 January 2014 / Revised: 28 February 2014 / Accepted: 5 March 2014 / Published: 24 March 2014
Cited by 2 | PDF Full-text (2340 KB) | HTML Full-text | XML Full-text
Abstract
QS-21 is a saponin extracted from Quillaja saponaria, widely investigated as a vaccine immunoadjuvant. However, QS-21 use is mainly limited by its chemical instability, significant variety in molecular composition and low tolerance dose in mammals. Also, this compound tends to form [...] Read more.
QS-21 is a saponin extracted from Quillaja saponaria, widely investigated as a vaccine immunoadjuvant. However, QS-21 use is mainly limited by its chemical instability, significant variety in molecular composition and low tolerance dose in mammals. Also, this compound tends to form micelles in a concentration-dependent manner. Here, we aimed to characterize its conformation and the process of micelle formation, both experimentally and computationally. Therefore, molecular dynamics (MD) simulations were performed in systems containing different numbers of QS-21 molecules in aqueous solution, in order to evaluate the spontaneous micelle formation. The applied methodology allowed the generation of micelles whose sizes were shown to be in high agreement with small-angle X-ray scattering (SAXS). Furthermore, the ester linkage between fucose and acyl chain was less solvated in the micellar form, suggesting a reduction in hydrolysis. This is the first atomistic interpretation of previous experimental data, the first micellar characterization of saponin micelles by SAXS and first tridimensional model of a micelle constituted of saponins, contributing to the understanding of the molecular basis of these compounds. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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Open AccessArticle EGF Receptor-Dependent Mechanism May be Involved in the Tamm–Horsfall Glycoprotein-Enhanced PMN Phagocytosis via Activating Rho Family and MAPK Signaling Pathway
Molecules 2014, 19(1), 1328-1343; doi:10.3390/molecules19011328
Received: 3 December 2013 / Revised: 13 January 2014 / Accepted: 16 January 2014 / Published: 21 January 2014
Cited by 1 | PDF Full-text (2126 KB) | HTML Full-text | XML Full-text
Abstract
Our previous studies showed that urinary Tamm–Horsfall glycoprotein (THP) potently enhanced polymorphonuclear neutrophil (PMN) phagocytosis. However, the domain structure(s), signaling pathway and the intracellular events responsible for THP-enhanced PMN phagocytosis remain to be elucidated. THP was purified from normal human urine. The [...] Read more.
Our previous studies showed that urinary Tamm–Horsfall glycoprotein (THP) potently enhanced polymorphonuclear neutrophil (PMN) phagocytosis. However, the domain structure(s), signaling pathway and the intracellular events responsible for THP-enhanced PMN phagocytosis remain to be elucidated. THP was purified from normal human urine. The human promyelocytic leukemia cell line HL-60 was induced to differentiate into PMNs by all-trans retinoid acid. Pretreatment with different MAPK and PI3K inhibitors was used to delineate signaling pathways in THP-enhanced PMN phagocytosis. Phosphorylation of molecules responsible for PMN phagocytosis induced by bacterial lipopolysaccharide (LPS), THP, or human recombinant epidermal growth factor (EGF) was evaluated by western blot. A p38 MAPK inhibitor, SB203580, effectively inhibited both spontaneous and LPS- and THP-induced PMN phagocytosis. Both THP and LPS enhanced the expression of the Rho family proteins Cdc42 and Rac that may lead to F-actin re-arrangement. Further studies suggested that THP and EGF enhance PMN and differentiated HL-60 cell phagocytosis in a similar pattern. Furthermore, the EGF receptor inhibitor GW2974 significantly suppressed THP- and EGF-enhanced PMN phagocytosis and p38 and ERK1/2 phosphorylation in differentiated HL-60 cells. We conclude that EGF receptor-dependent signaling may be involved in THP-enhanced PMN phagocytosis by activating Rho family and MAP kinase. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
Open AccessArticle A New Chemical Approach to Human ABO Histo-Blood Group Type 2 Antigens
Molecules 2014, 19(1), 414-437; doi:10.3390/molecules19010414
Received: 13 December 2013 / Revised: 24 December 2013 / Accepted: 25 December 2013 / Published: 31 December 2013
Cited by 8 | PDF Full-text (402 KB) | HTML Full-text | XML Full-text
Abstract
A new chemical approach to synthesizing human ABO histo-blood type 2 antigenic determinants was developed. N-Phthaloyl-protected lactosaminyl thioglycoside derived from lactulose via the Heyns rearrangement was employed to obtain a type 2 core disaccharide. Use of this scheme lowered the overall [...] Read more.
A new chemical approach to synthesizing human ABO histo-blood type 2 antigenic determinants was developed. N-Phthaloyl-protected lactosaminyl thioglycoside derived from lactulose via the Heyns rearrangement was employed to obtain a type 2 core disaccharide. Use of this scheme lowered the overall number of reaction steps. Stereoselective construction of the α-galactosaminide/galactoside found in A- and B-antigens, respectively, was achieved by using a unique di-tert-butylsilylene-directed α-glycosylation method. The proposed synthetic scheme provides an alternative to existing procedures for preparing ABO blood group antigens. Full article
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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