The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Gordon D. Brown - One of the best experts on this subject based on the ideXlab platform.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate beta-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in beta1,3- or both beta1,3- and beta1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate "designer" microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumor necrosis factor-alpha secretion by a Dectin-1-expressing macrophage cell line.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Abstract Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate β-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in β1,3- or both β1,3- and β1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate “designer” microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular β-glucans and compete with zymosan binding and triggering of tumor necrosis factor-α secretion by a Dectin-1-expressing macrophage cell line.
Angelina S Palma - One of the best experts on this subject based on the ideXlab platform.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate beta-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in beta1,3- or both beta1,3- and beta1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate "designer" microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumor necrosis factor-alpha secretion by a Dectin-1-expressing macrophage cell line.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Abstract Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate β-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in β1,3- or both β1,3- and β1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate “designer” microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular β-glucans and compete with zymosan binding and triggering of tumor necrosis factor-α secretion by a Dectin-1-expressing macrophage cell line.
Ryuta Terada - One of the best experts on this subject based on the ideXlab platform.
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Effects of light quality and temperature on the photosynthesis and pigment content of a subtidal edible red alga Meristotheca Papulosa (Solieriaceae, Gigartinales) from Japan
Journal of Applied Phycology, 2020Co-Authors: Iris Ann Borlongan, Gregory N Nishihara, Sayuri Suzuki, Jumpei Kozono, Ryuta TeradaAbstract:This study investigated the effects of different light spectral qualities and temperature on the photosynthesis and pigment content of a subtidal edible red alga, Meristotheca Papulosa . Photosynthesis – irradiance ( P–E ) experiments were carried out under red (660 nm), blue (450 nm), green (525 nm, light-emitting diodes), and white light (visible light, metal halide lamp), and at 12, 20, and 28 °C, respectively. Maximum net photosynthetic rates ( NP _ max ) were highest under green light. Other P–E parameter estimates were similar among algae under red, blue, and green light, including their lower initial slope ( α ) and higher saturation irradiances ( E _ k ) as compared to those under white light. Additionally, NP _ max and E _ k under white light were highest at 28 °C, and lowest at 12 °C with characteristic photoinhibition at irradiances greater than 150 μmol photons m^−2 s^−1. Photosynthesis – temperature ( P–T ) experiment revealed that the maximum gross photosynthetic rate ( GP _ max ) occurred at 22.1 °C, which was within the optimal temperature range of F _ v /F _ m (21.5–23.6 °C). Exposures to the different light qualities at 100 μmol photons m^−2 s^−1 for 7 days showed increased phycoerythrin (PE) concentration of algae under blue and green light, while chlorophyll- a and phycocyanin (PC) showed little variation in all light qualities. Therefore, considering future management prospects for M. Papulosa mariculture, we suggest that green light could be utilized to enhance photosynthesis. Furthermore, if the aim is to achieve high PE content for an improved reddish-color fresh product, exposure to blue or green light could be a good alternative.
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effect of temperature and light on the photosynthetic performance of two edible seaweeds meristotheca coacta okamura and meristotheca Papulosa j agardh solieriaceae rhodophyta
Aquaculture Science, 2012Co-Authors: Gregory N Nishihara, Tadahide Noro, Ryuta TeradaAbstract:The photosynthetic performance of two species of Meristotheca (Solieriaceae, Rhodophyta), M. coacta and M. Papulosa, was investigated under a variety of temperature and light conditions to derive basic information regarding their physiology. A pulse amplitude modulated-chlorophyll fluorometer (Imaging-PAM) was used to generate rapid light curves (RLCs) to provide the relative electron transport rates (rETR) over 21 levels of photosynthetic active radiation (PAR), ranging from 0 to 1,078μmol photons m -2 s -1 at 14 temperatures (i.e., from 8 to 34℃). The initial slope (α), photoinhibition (β) and coefficient (γ) was calculated by fitting the RLCs to a nonlinear model of the form rETR =γ(1-exp(-α·PAR/γ)) (exp(-β· PAR/γ)) using a two-level hierarchical Bayesian model. Both species required temperatures ranging from 18 to 28℃ to maintain optimal photosyn- thetic activity, as revealed by the estimated model parameters. The optimal PAR (PARopt) increased with increasing temperature. Meristotheca coacta and M. Papulosa can be considered well-adapted to the current natural light and temperature conditions of southern Kyushu, Japan. Finding in this study should be useful to the design and manage mariculture programs to conserve the natural resources.
Yibing Zhang - One of the best experts on this subject based on the ideXlab platform.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate beta-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in beta1,3- or both beta1,3- and beta1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate "designer" microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumor necrosis factor-alpha secretion by a Dectin-1-expressing macrophage cell line.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Abstract Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate β-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in β1,3- or both β1,3- and β1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate “designer” microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular β-glucans and compete with zymosan binding and triggering of tumor necrosis factor-α secretion by a Dectin-1-expressing macrophage cell line.
Mark S Stoll - One of the best experts on this subject based on the ideXlab platform.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate beta-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in beta1,3- or both beta1,3- and beta1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate "designer" microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumor necrosis factor-alpha secretion by a Dectin-1-expressing macrophage cell line.
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ligands for the β glucan receptor dectin 1 assigned using designer microarrays of oligosaccharide probes neoglycolipids generated from glucan polysaccharides
Journal of Biological Chemistry, 2006Co-Authors: Angelina S Palma, Siamon Gordon, Ten Feizi, Yibing Zhang, Mark S Stoll, Alexander M Lawson, Esther Diazrodriguez, Maria A Campanerorhodes, Julia Costa, Gordon D. BrownAbstract:Abstract Dectin-1 is a C-type lectin-like receptor on leukocytes that mediates phagocytosis and inflammatory mediator production in innate immunity to fungal pathogens. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins; nevertheless, it binds zymosan, a particulate β-glucan-rich extract of Saccharomyces cerevisiae, and binding is inhibited by polysaccharides rich in β1,3- or both β1,3- and β1,6-linked glucose. The oligosaccharide ligands on glucans recognized by Dectin-1 have not yet been delineated precisely. It is also not known whether Dectin-1 can interact with other types of carbohydrates. We have investigated this, since Dectin-1 shows glucan-independent binding to a subset of T-lymphocytes and is involved in triggering their proliferation. Here we assign oligosaccharide ligands for Dectin-1 using the neoglycolipid-based oligosaccharide microarray technology, a unique approach for constructing microarrays of lipid-linked oligosaccharide probes from desired sources. We generate “designer” microarrays from three glucan polysaccharides, a neutral soluble glucan isolated from S. cerevisiae and two bacterial glucans, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, and use these in conjunction with 187 diverse, sequence-defined, predominantly mammalian-type, oligosaccharide probes. Among these, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer. Thus, the ligands assigned so far are exogenous rather than endogenous. We further show that Dectin-1 ligands, 11-13 gluco-oligomers, in clustered form (displayed on liposomes), mimic the macromolecular β-glucans and compete with zymosan binding and triggering of tumor necrosis factor-α secretion by a Dectin-1-expressing macrophage cell line.
