β-glucan Search Results


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  • 99
    Millipore β glucan
    a , SDS-PAGE and Western-blot analysis of rCfLec-3. Lane 1: protein molecular standard; lane 2: negative control (without induction); lane 3: induced rCfLec-3; lane 4: purified rCfLec-3; lane 5: Western-blot of rCfLec-3 with anti-CfLec-3 antibody. b , Localization of endogenous CfLec-3 in different tissues by immunohistochemistry. CfLec-3 was detected by anti-CfLec-3 antibody, and stained in red. The tissues were counterstained with haematoxylin (blue). c-f , Temporal expression of CfLec-3 mRNA relative to β-actin was analyzed by realtime PCR in scallop hemocytes after LPS ( c ), PGN ( d ), <t>β-glucan</t> ( e ), poly I:C ( f ) and PBS challenge ( c, d, e, f ) for 3, 6, 12, 24 and 48 h. The values are shown as mean ± SE (N = 4), student’s t -test, error-bars represent biological repeats. (*: P
    β Glucan, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 388 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Megazyme β glucan
    TLC analysis of the action patterns of Cpin_6279rC on <t>β-1,2-glucan</t> and Sop n s. β-1,2-Glucan (average DP 64) ( A ), cyclic β-1,2-glucan (DP 17–24) ( B ), Sop 5 ( C ), Sop 6 ( D ), and Sop 7 ( E ) were used as substrates. Lane M contains markers (0.2% each sugar). Asterisks represent the origins of the TLC plates.
    β Glucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 93/100, based on 261 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Megazyme barley glucan
    Thin layer chromatography analysis of hydrolysis products released by Cel01. Degradation of <t>CMC</t> ( a ) and barley <t>glucan</t> ( b ) was analyzed at the indicated time points. Lane M , mixed standard sugars: glucose (G1), cellobiose (G2), cellotriose (G3), and cellotetraose (G4); lane -, control containing substrate without enzyme
    Barley Glucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 89/100, based on 66 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore saccharomyces cerevisiae
    Effects of phagocytosis impairment on the response of human monocytes toward whole Candida albicans and the cell wall fraction composed of branched β-glucan. (A and B) Human monocytes were left untreated (ctrl) or stimulated with either heat-killed Candida albicans (HK-C.a., A) or heat-killed Saccharomyces <t>cerevisiae</t> (HK-S.c., B) in the presence (Cyt D) or in the absence (DMSO) of cytochalasin D. (C) Cells were stimulated with the Alkali-Soluble (AS) and Insoluble (AI) fractions, β-(1–6)-glucan and β-(1–3)/(1–6) glucan fractions from the cell wall of Saccharomyces cerevisiae after being treated with DMSO or Cyt D. (D) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or from S. cerevisiae (β-glucan S.c.) in the presence or in the absence of Cyt D. (E) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of insoluble linear β- (1–3)-glucan (curdlan) or of soluble branched β-(1–3)-glucan (laminarin) in the presence or in the absence of Cyt D. (F) The particulate branched β-(1–3)-glucan isolated from the cell wall of C. albicans was sonicated (Sonifier cell Disruptor B-30. Outputcontrol 4, Duty cycle 40%; 2 times 10 cycle with 5min on ice in between the two sets). Monocytes were then exposed to either sonicated or not-sonicated β–glucan in the presence or in the absence of Cyt D. (G) Cells pre-treated with DMSO or Cyt D were stimulated for 24 h with the indicated concentrations of β-glucan from C. albicans (β-glucan C.a.), HK-C.a., AS and AI fractions from S.c., or the combination of AS+AI (10+10 μg/mL). (H) Monocytes were pre-treated with either DMSO (control), or with cytochalasin D (Cyt D) or latrunculin B (Lat B) (actin polymerization inhibitors), or with jasplakinolide (Jsp, actin polymerization inducer), or with chlorpromazine (CLP, clathrin-mediated endocytic inhibitor) or the lysosomal inhibitor cloroquine (CLQ). Cells were then stimulated with either branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or with heat-killed Candida albicans (HK-C.a.). For all the experiments, culture supernatants were collected after 24h and concentration of secreted TNF-α, IL-6, IL-1β and IL-10 was determined by ELISA. Data were reproducible for all the four cytokines tested even if histograms are not shown. Graphs show the mean ± SEM of at least three independent experiments. For (A, H), n = 8; for (B–G), n = 6; * p
    Saccharomyces Cerevisiae, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1263 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Megazyme mixed linkage β glucan assay kit
    In vitro inhibitory activities of Qingke β-glucans on α-amylase ( A ) and pancreatic lipase ( B ). BG , Qingke <t>β-glucan;</t> BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; the error bars are standard deviations; significant ( p
    Mixed Linkage β Glucan Assay Kit, supplied by Megazyme, used in various techniques. Bioz Stars score: 88/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Megazyme β glucan assay kit
    Changes in <t>glucan</t> concentrations by elicitor treatments in the cultivation of Sparassis latifolia on a Pinus densiflora sawdust-based medium. G, glucuronidase; Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The values were not significantly different at the 5% level by ANOVA ( p = 0.2993 for <t>β-glucan).</t>
    β Glucan Assay Kit, supplied by Megazyme, used in various techniques. Bioz Stars score: 88/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore β d glucan
    Quantitative real-time PCR analysis of select targets regulated by <t>β-D-glucan</t> in MCF-7 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle control), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S rRNA and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment.
    β D Glucan, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Immuno Research Inc pgg beta glucan
    Quantitative real-time PCR analysis of select targets regulated by <t>β-D-glucan</t> in MCF-7 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle control), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S rRNA and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment.
    Pgg Beta Glucan, supplied by Immuno Research Inc, used in various techniques. Bioz Stars score: 88/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Novozymes glucan
    <t>Glucan</t> and xylan conversion during the hydrolysis of EA pretreated newspaper waste by using <t>MIX</t> 1 (15 mg/g of glucan of commercial enzymatic preparation Novozymes Cellic ® —60 % CTec3 and 40 % HTec3; MIX 2 (adding 3.32 mg/g glucan of endoglucanase rCelStrep to MIX 1); MIX 3 (adding 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 4 (adding 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX A’); MIX 5 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 6 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1)
    Glucan, supplied by Novozymes, used in various techniques. Bioz Stars score: 91/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology 3 glucan
    Increased expression of ATF4-stimulated HCECs and THP-1 macrophages. (a) With the stimulation of LPS, β -1, <t>3-glucan,</t> TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in HCECs were not changed significantly at 8 hours. (b) ATF4 protein levels in HCECs did not change significantly at 16 hours with the stimulation of LPS, β -1, 3-glucan, TGF- β , and IL-1 β , but significantly increased with A. fumigatus conidia. (c) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in THP-1 macrophages did not change significantly at 8 hours. (d) ATF4 protein levels in HCECs were higher after stimulation with LPS, TGF- β , IL-1 β , and A. fumigatus conidia at 16 hours, but did not change significantly with β -1, 3-glucan. The mean values and standard deviations of two independent experiments are shown; ∗∗ P
    3 Glucan, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Mustafa Nevzat beta glucan
    Increased expression of ATF4-stimulated HCECs and THP-1 macrophages. (a) With the stimulation of LPS, β -1, <t>3-glucan,</t> TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in HCECs were not changed significantly at 8 hours. (b) ATF4 protein levels in HCECs did not change significantly at 16 hours with the stimulation of LPS, β -1, 3-glucan, TGF- β , and IL-1 β , but significantly increased with A. fumigatus conidia. (c) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in THP-1 macrophages did not change significantly at 8 hours. (d) ATF4 protein levels in HCECs were higher after stimulation with LPS, TGF- β , IL-1 β , and A. fumigatus conidia at 16 hours, but did not change significantly with β -1, 3-glucan. The mean values and standard deviations of two independent experiments are shown; ∗∗ P
    Beta Glucan, supplied by Mustafa Nevzat, used in various techniques. Bioz Stars score: 89/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Associates of Cape Cod Inc β d glucan
    Echinocandin inhibition profiles for product-entrapped <t>1,3-β-</t> d <t>-glucan</t> synthase enzyme complexes assessed by the incorporation of [ 3 H]glucose into radiolabeled product. (A) CSF titration curves for enzymes isolated from strains ATCC 90030 (wild
    β D Glucan, supplied by Associates of Cape Cod Inc, used in various techniques. Bioz Stars score: 89/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Charles River Laboratories β glucan
    (a) Serum IL-10 in relation to the amount of <t>β</t> -glucan (BAL) pg/mL ( n = 70) and (b) NAHA in homes ( n = 60) of subjects with sarcoidosis.
    β Glucan, supplied by Charles River Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    FUJIFILM β glucan
    Silent fungal infections under non-SPF trigger arthritis in SKG mice. (A) PCRs of fungal 18SrDNA or mouse Rag 1 gene from esophagus (Es), lung (Lg), liver (Lv), or foot including ankle joint (Ft) of BALB/c or SKG mice in non-SPF. (B) Lungs of BALB/c or SKG mice in non-SPF or SPF were assessed for fungi by real-time quantitative PCR. (C–F) Methenamine silver (C and E) or hematoxylin and eosin (D and F) stainings of lungs from SKG mice (C and D) or BALB/c (E and F) of non-SPF. Arrows indicate argyrophilic fungal cysts. (G) Male SKG mice of 10 wk of age in the non-SPF facility were treated with four cycles of four daily i.p. injections of 75 μg amphotericin B (arrows) at 10-d intervals. (H) SKG mice in the SPF facility received the same protocol of antifungal treatment 10 d after i.p. administration of 2 mg zymosan (open inverted triangle). (I) Concentration of serum <t>β-glucan</t> in non-SPF or SPF 12-wk-old SKG mice.
    β Glucan, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 92/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Seikagaku β glucan
    (a to f) Content of <t>β-glucan</t> or NAGase in aerosols from Botrytis cinerea -colonized gypsum boards, floor paper, or slices of aubergines. The total column is the inhalable fraction sampled with the GSP sampler, the middle fraction of the column
    β Glucan, supplied by Seikagaku, used in various techniques. Bioz Stars score: 93/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Immuno Research Inc β glucan
    Display of <t>β-glucan</t> during different stages of C. albicans mucosal biofilm growth. Panels depict representative confocal images of tissue sections from mice with oropharyngeal candidiasis (A–D) or from a three-dimensional in vitro model of the oral mucosa (F). Panels A–D and F depict sections stained for β-glucan with a BFDiv monoclonal antibody (red), C. albicans with a polyclonal anti- Candida Ab (green) and counterstained with the nucleic acid stain TO-PRO-3, which stains tissue cells blue. Panel E depicts a section stained with an IgM isotype control antibody for the BFDiv stain. Notice that β-glucan becomes more uniformly present on the surface of fungal cells invading the tongue mucosa (arrows). Scale bar = 20 µm.
    β Glucan, supplied by Immuno Research Inc, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Megazyme mixed linkage beta glucan assay kit
    Display of <t>β-glucan</t> during different stages of C. albicans mucosal biofilm growth. Panels depict representative confocal images of tissue sections from mice with oropharyngeal candidiasis (A–D) or from a three-dimensional in vitro model of the oral mucosa (F). Panels A–D and F depict sections stained for β-glucan with a BFDiv monoclonal antibody (red), C. albicans with a polyclonal anti- Candida Ab (green) and counterstained with the nucleic acid stain TO-PRO-3, which stains tissue cells blue. Panel E depicts a section stained with an IgM isotype control antibody for the BFDiv stain. Notice that β-glucan becomes more uniformly present on the surface of fungal cells invading the tongue mucosa (arrows). Scale bar = 20 µm.
    Mixed Linkage Beta Glucan Assay Kit, supplied by Megazyme, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Megazyme mushroom β glucan kit
    Display of <t>β-glucan</t> during different stages of C. albicans mucosal biofilm growth. Panels depict representative confocal images of tissue sections from mice with oropharyngeal candidiasis (A–D) or from a three-dimensional in vitro model of the oral mucosa (F). Panels A–D and F depict sections stained for β-glucan with a BFDiv monoclonal antibody (red), C. albicans with a polyclonal anti- Candida Ab (green) and counterstained with the nucleic acid stain TO-PRO-3, which stains tissue cells blue. Panel E depicts a section stained with an IgM isotype control antibody for the BFDiv stain. Notice that β-glucan becomes more uniformly present on the surface of fungal cells invading the tongue mucosa (arrows). Scale bar = 20 µm.
    Mushroom β Glucan Kit, supplied by Megazyme, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Associates of Cape Cod Inc 1 3 β d glucan
    Dust borne endotoxin, dust borne <t>(1–3)-β-D-glucan,</t> airborne endotoxin, airborne (1–3)-β-D-glucan, and airborne fungal spores in homes divided into two levels of mold burden based on ERMI index: low (ERMI ≤5; n=135) and high (ERMI > 5; n=48). Histograms show geometric means and error bars show 95% confidence intervals. *** p
    1 3 β D Glucan, supplied by Associates of Cape Cod Inc, used in various techniques. Bioz Stars score: 88/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    a , SDS-PAGE and Western-blot analysis of rCfLec-3. Lane 1: protein molecular standard; lane 2: negative control (without induction); lane 3: induced rCfLec-3; lane 4: purified rCfLec-3; lane 5: Western-blot of rCfLec-3 with anti-CfLec-3 antibody. b , Localization of endogenous CfLec-3 in different tissues by immunohistochemistry. CfLec-3 was detected by anti-CfLec-3 antibody, and stained in red. The tissues were counterstained with haematoxylin (blue). c-f , Temporal expression of CfLec-3 mRNA relative to β-actin was analyzed by realtime PCR in scallop hemocytes after LPS ( c ), PGN ( d ), β-glucan ( e ), poly I:C ( f ) and PBS challenge ( c, d, e, f ) for 3, 6, 12, 24 and 48 h. The values are shown as mean ± SE (N = 4), student’s t -test, error-bars represent biological repeats. (*: P

    Journal: Scientific Reports

    Article Title: CfLec-3 from scallop: an entrance to non-self recognition mechanism of invertebrate C-type lectin

    doi: 10.1038/srep10068

    Figure Lengend Snippet: a , SDS-PAGE and Western-blot analysis of rCfLec-3. Lane 1: protein molecular standard; lane 2: negative control (without induction); lane 3: induced rCfLec-3; lane 4: purified rCfLec-3; lane 5: Western-blot of rCfLec-3 with anti-CfLec-3 antibody. b , Localization of endogenous CfLec-3 in different tissues by immunohistochemistry. CfLec-3 was detected by anti-CfLec-3 antibody, and stained in red. The tissues were counterstained with haematoxylin (blue). c-f , Temporal expression of CfLec-3 mRNA relative to β-actin was analyzed by realtime PCR in scallop hemocytes after LPS ( c ), PGN ( d ), β-glucan ( e ), poly I:C ( f ) and PBS challenge ( c, d, e, f ) for 3, 6, 12, 24 and 48 h. The values are shown as mean ± SE (N = 4), student’s t -test, error-bars represent biological repeats. (*: P

    Article Snippet: The scallops in five groups received an intramuscular injection of 50 μL phosphate buffered saline (PBS, 0.14 M sodium chloride, 3 mM potassium chloride, 8 mM disodium hydrogenphosphate dodecahydrate, 1.5 mM potassium phosphate monobasic, pH 7.4), LPS from E. coli 0111:B4 (Sigma-Aldrich, 0.5 mg mL−1 in PBS), PGN from S. aureus (Sigma-Aldrich, 0.8 mg mL−1 in PBS), β-glucan from Saccharomyces cerevisiae (Sigma-Aldrich, 1.0 mg mL−1 in PBS), and Ploy I:C (Sigma-Aldrich, 1.0 mg mL−1 in PBS), respectively.

    Techniques: SDS Page, Western Blot, Negative Control, Purification, Immunohistochemistry, Staining, Expressing, Polymerase Chain Reaction

    Adsorption of CBM30 to insoluble (I) and soluble (II) polysaccharides. In the experiment in panel I, CBM30 was incubated with insoluble polysaccharides including Avicel (A), ASC (B), BMC (C), insoluble fraction of oat spelt xylan (D), lichenan (E), agar (F), starch (G), Sephadex G-150 (H), and chitin (I). After centrifugation, proteins in the supernatant (lane 1) and the precipitate (lane 2) were analyzed by SDS-PAGE. In the experiment in panel II, affinities of CBM30-Ig (lane 1) and CBM30 (CBM30) for various soluble polysaccharides including hydroxyethylcellulose (b), methylcellulose (c), soluble fraction of oat spelt xylan (d), birchwood xylan (e), barley β-glucan (f), lichenan (g), and soluble starch (h) were analyzed by native affinity gel electrophoresis. Lane M contains bovine serum albumin as a control protein. A gel without a polysaccharide served as a reference (a).

    Journal: Journal of Bacteriology

    Article Title: Characterization of a Cellulase Containing a Family 30 Carbohydrate-Binding Module (CBM) Derived from Clostridium thermocellum CelJ: Importance of the CBM to Cellulose Hydrolysis

    doi: 10.1128/JB.185.2.504-512.2003

    Figure Lengend Snippet: Adsorption of CBM30 to insoluble (I) and soluble (II) polysaccharides. In the experiment in panel I, CBM30 was incubated with insoluble polysaccharides including Avicel (A), ASC (B), BMC (C), insoluble fraction of oat spelt xylan (D), lichenan (E), agar (F), starch (G), Sephadex G-150 (H), and chitin (I). After centrifugation, proteins in the supernatant (lane 1) and the precipitate (lane 2) were analyzed by SDS-PAGE. In the experiment in panel II, affinities of CBM30-Ig (lane 1) and CBM30 (CBM30) for various soluble polysaccharides including hydroxyethylcellulose (b), methylcellulose (c), soluble fraction of oat spelt xylan (d), birchwood xylan (e), barley β-glucan (f), lichenan (g), and soluble starch (h) were analyzed by native affinity gel electrophoresis. Lane M contains bovine serum albumin as a control protein. A gel without a polysaccharide served as a reference (a).

    Article Snippet: The affinities of these proteins for soluble polysaccharides, i.e., CMC (low viscosity [Sigma]), hydroxyethylcellulose (Fluka), methylcellulose (Nacalai Tesque), barley β-glucan (Sigma), and birchwood xylan (Sigma), were examined by native affinity gel electrophoresis as described by Meissner et al. , with some simplifications.

    Techniques: Adsorption, Incubation, Centrifugation, SDS Page, Nucleic Acid Electrophoresis

    TLC analysis of the action patterns of Cpin_6279rC on β-1,2-glucan and Sop n s. β-1,2-Glucan (average DP 64) ( A ), cyclic β-1,2-glucan (DP 17–24) ( B ), Sop 5 ( C ), Sop 6 ( D ), and Sop 7 ( E ) were used as substrates. Lane M contains markers (0.2% each sugar). Asterisks represent the origins of the TLC plates.

    Journal: The Journal of Biological Chemistry

    Article Title: Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family

    doi: 10.1074/jbc.M116.762724

    Figure Lengend Snippet: TLC analysis of the action patterns of Cpin_6279rC on β-1,2-glucan and Sop n s. β-1,2-Glucan (average DP 64) ( A ), cyclic β-1,2-glucan (DP 17–24) ( B ), Sop 5 ( C ), Sop 6 ( D ), and Sop 7 ( E ) were used as substrates. Lane M contains markers (0.2% each sugar). Asterisks represent the origins of the TLC plates.

    Article Snippet: CM-pachyman, CM-curdlan, lichenan, β-glucan from barley, xyloglucan (tamarind), glucomannan, arabinogalactan, arabinan, and polygalacturonate were purchased from Megazyme (Wicklow, Ireland).

    Techniques: Thin Layer Chromatography

    Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on histologic dam age score in dextran sulfate sodium (DSS)-induced colitis. DSS was administrated for 7 days and mill and glucan extract treatment started with DSS treatment and continued until day 16 when all mice were sacrificed and tissue samples were taken for analysis. Data represent mean ± SD of six mice per group. Different letters indicate significantly different values at p

    Journal: International Journal of Molecular Sciences

    Article Title: Spatial Distribution of Glucan Type and Content between Caps and Stalks in Pleurotus eryngii: Impact on the Anti-inflammatory Functionality

    doi: 10.3390/ijms19113371

    Figure Lengend Snippet: Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on histologic dam age score in dextran sulfate sodium (DSS)-induced colitis. DSS was administrated for 7 days and mill and glucan extract treatment started with DSS treatment and continued until day 16 when all mice were sacrificed and tissue samples were taken for analysis. Data represent mean ± SD of six mice per group. Different letters indicate significantly different values at p

    Article Snippet: Glucan Content Mushroom Stalk and Cap The glucan content of the P. eryngii was assessed using the Megazyme kit.

    Techniques: Isolation, Mouse Assay

    Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on ( a ) INF-γ mRNA levels ( b ) Mip-2 levels mRNA levels and ( c ) CXCL1 mRNA levels in colonic samples relative to negative control (no treatment). DSS was administrated for 7 days and mill and glucan extract treatment started with DSS treatment and continued until day 16 when all mice were sacrificed and tissue samples were taken for analysis. Data represent mean ± SD of six mice per group. Different letters indicate significantly different values at p

    Journal: International Journal of Molecular Sciences

    Article Title: Spatial Distribution of Glucan Type and Content between Caps and Stalks in Pleurotus eryngii: Impact on the Anti-inflammatory Functionality

    doi: 10.3390/ijms19113371

    Figure Lengend Snippet: Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on ( a ) INF-γ mRNA levels ( b ) Mip-2 levels mRNA levels and ( c ) CXCL1 mRNA levels in colonic samples relative to negative control (no treatment). DSS was administrated for 7 days and mill and glucan extract treatment started with DSS treatment and continued until day 16 when all mice were sacrificed and tissue samples were taken for analysis. Data represent mean ± SD of six mice per group. Different letters indicate significantly different values at p

    Article Snippet: Glucan Content Mushroom Stalk and Cap The glucan content of the P. eryngii was assessed using the Megazyme kit.

    Techniques: Isolation, Mouse Assay, Negative Control

    Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on ( a ) percent of CD14 + /CD16 + monocytes and ( b ) on secretory IgA in feces harvested from mice who underwent DSS-induced colitis. Data represent mean ± SD of six mice per group; data were compared between DSS and mill and isolated glucans from caps and stalks of P. eryngii mushrooms treated groups. Different letters indicate significantly different values at p

    Journal: International Journal of Molecular Sciences

    Article Title: Spatial Distribution of Glucan Type and Content between Caps and Stalks in Pleurotus eryngii: Impact on the Anti-inflammatory Functionality

    doi: 10.3390/ijms19113371

    Figure Lengend Snippet: Effect of mill and isolated glucans from caps and stalks of P. eryngii mushrooms (1 mg glucan/kg mice BW) on ( a ) percent of CD14 + /CD16 + monocytes and ( b ) on secretory IgA in feces harvested from mice who underwent DSS-induced colitis. Data represent mean ± SD of six mice per group; data were compared between DSS and mill and isolated glucans from caps and stalks of P. eryngii mushrooms treated groups. Different letters indicate significantly different values at p

    Article Snippet: Glucan Content Mushroom Stalk and Cap The glucan content of the P. eryngii was assessed using the Megazyme kit.

    Techniques: Isolation, Mouse Assay

    The isoleucine-to-leucine change alters the fine structure of (1-3,1-4)-β-glucan. ( A ) Changing the native isoleucine in TMH4 of CslF6 protein (dark blue bars) to a leucine (red bars) increases the proportion of β1-4 bonds in (1-3,1-4)-β-glucan, similar to that produced from those native CslF6 proteins that have a leucine at the same position (light blue bars). ( B ) The increase in β1-4 bond frequency changes the (1-3,1-4)-β-glucan structure, decreasing the proportion of DP3 and DP4 oligosaccharides. ( C ) The increase in longer-chain oligosaccharides is largely explained by an increase in DP5 and DP6. Dashed lines are shown to indicate the trends in change of oligosaccharide profiles between the independent experimental measurements. Error bars from duplicate measurements are indicated.

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: The isoleucine-to-leucine change alters the fine structure of (1-3,1-4)-β-glucan. ( A ) Changing the native isoleucine in TMH4 of CslF6 protein (dark blue bars) to a leucine (red bars) increases the proportion of β1-4 bonds in (1-3,1-4)-β-glucan, similar to that produced from those native CslF6 proteins that have a leucine at the same position (light blue bars). ( B ) The increase in β1-4 bond frequency changes the (1-3,1-4)-β-glucan structure, decreasing the proportion of DP3 and DP4 oligosaccharides. ( C ) The increase in longer-chain oligosaccharides is largely explained by an increase in DP5 and DP6. Dashed lines are shown to indicate the trends in change of oligosaccharide profiles between the independent experimental measurements. Error bars from duplicate measurements are indicated.

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Produced

    Single amino acid differences in the predicted TMH4 of CslF6 control (1-3,1-4)-β-glucan structure. The amino acid sequence of the TMH4 region of HvCslF6 and ZmCslF6 proteins is shown. Each of the four different single amino acids (underlined) in the HvCslF6 protein was changed to the corresponding ZmCslF6 amino acid, and the effect on the DP3/DP4 ratio and the amount (% dry weight of leaf) of the (1-3,1-4)-β-glucan are shown at the right. Results are means ± SD from replicates of at least two transformation experiments.

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: Single amino acid differences in the predicted TMH4 of CslF6 control (1-3,1-4)-β-glucan structure. The amino acid sequence of the TMH4 region of HvCslF6 and ZmCslF6 proteins is shown. Each of the four different single amino acids (underlined) in the HvCslF6 protein was changed to the corresponding ZmCslF6 amino acid, and the effect on the DP3/DP4 ratio and the amount (% dry weight of leaf) of the (1-3,1-4)-β-glucan are shown at the right. Results are means ± SD from replicates of at least two transformation experiments.

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Sequencing, Transformation Assay

    Characterization of (1-3,1-4)-β-glucan structure in Nicotiana benthamiana leaves. ( A ) Structure of (1-3,1-4)-β-glucan. Glucose molecules are represented by black dots with β1-4 linkages (straight lines) or β1-3 linkages (angled lines). The bacterial enzyme lichenase specifically cleaves (1-3,1-4)-β-glucan at a β1-4 linkage after a β1-3 linkage as indicated by dashed red lines, producing short oligosaccharides with a DP from DP3 to DP9. ( B ) Oligosaccharides released by lichenase digestion of betaglucan were fluorescently labeled with APTS and separated by capillary electrophoresis. ( C ) The source of the CslF6 gene affects the DP3/DP4 ratio of the (1-3,1-4)-β-glucan produced in N. benthamiana leaves. The CslF6 proteins can be classified into two groups: those that produce a (1-3,1-4)-β-glucan with a high ( > 1.3) DP3/DP4 ratio (Bd, Brachypodum distachyon ; Ta, Triticum aestivum ; Hv, Hordeum vulgare ; shown in blue) or a low (

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: Characterization of (1-3,1-4)-β-glucan structure in Nicotiana benthamiana leaves. ( A ) Structure of (1-3,1-4)-β-glucan. Glucose molecules are represented by black dots with β1-4 linkages (straight lines) or β1-3 linkages (angled lines). The bacterial enzyme lichenase specifically cleaves (1-3,1-4)-β-glucan at a β1-4 linkage after a β1-3 linkage as indicated by dashed red lines, producing short oligosaccharides with a DP from DP3 to DP9. ( B ) Oligosaccharides released by lichenase digestion of betaglucan were fluorescently labeled with APTS and separated by capillary electrophoresis. ( C ) The source of the CslF6 gene affects the DP3/DP4 ratio of the (1-3,1-4)-β-glucan produced in N. benthamiana leaves. The CslF6 proteins can be classified into two groups: those that produce a (1-3,1-4)-β-glucan with a high ( > 1.3) DP3/DP4 ratio (Bd, Brachypodum distachyon ; Ta, Triticum aestivum ; Hv, Hordeum vulgare ; shown in blue) or a low (

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Labeling, Electrophoresis, Produced

    The effect of chimeric HvCslF6/ZmCslF6 genes on (1-3,1-4)-β-glucan structure. Restriction sites used in cloning are shown as vertical lines. The HvCslF6 gene is represented by blue rectangle, and the ZmCslF6-2 gene as a yellow rectangle. ( Right ) DP3/DP4 ratio of the lichenase digested (1-3,1-4)-β-glucan averaged from the indicated number of independent transformation experiments with SDs shown.

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: The effect of chimeric HvCslF6/ZmCslF6 genes on (1-3,1-4)-β-glucan structure. Restriction sites used in cloning are shown as vertical lines. The HvCslF6 gene is represented by blue rectangle, and the ZmCslF6-2 gene as a yellow rectangle. ( Right ) DP3/DP4 ratio of the lichenase digested (1-3,1-4)-β-glucan averaged from the indicated number of independent transformation experiments with SDs shown.

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Clone Assay, Transformation Assay

    The Bgl II – Eco RI fragment of CslF6 genes controls (1-3,1-4)-β-glucan structure. Restriction sites used in cloning are shown as vertical lines. The blue or red rectangles represent the CslF6 genes that produce (1-3,1-4)-β-glucan with a high DP3/DP4 ratio, and the yellow or gray rectangles represent those that produce a (1-3,1-4)-β-glucan with a low DP3/DP4 ratio as indicated on the right. All chimeric constructs show a high ( > 1.4) or a low (

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: The Bgl II – Eco RI fragment of CslF6 genes controls (1-3,1-4)-β-glucan structure. Restriction sites used in cloning are shown as vertical lines. The blue or red rectangles represent the CslF6 genes that produce (1-3,1-4)-β-glucan with a high DP3/DP4 ratio, and the yellow or gray rectangles represent those that produce a (1-3,1-4)-β-glucan with a low DP3/DP4 ratio as indicated on the right. All chimeric constructs show a high ( > 1.4) or a low (

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Clone Assay, Construct

    The effect of amino acid changes in predicted TMH4 on (1-3,1-4)-β-glucan structure across species. The DP3/DP4 ratio of (1-3,1-4)-β-glucan produced in N. benthamiana leaf from wild-type CslF6 proteins with an isoleucine in predicted TMH4 is shown as black bars. When the indicated isoleucine is changed to a leucine, the DP3/DP4 ratio of the (1-3,1-4)-β-glucan is decreased (light gray bars). A further decrease in the DP3/DP4 ratio is observed when a second amino acid substitution is made in the HvCslF6 TMH4 region (HvCslF6 S752G,I757L ). Shown are averages and SDs of replicates from at least two transformation experiments. The amount of (1-3,1-4)-β-glucan produced for the respective constructs was 1.8, 2.2, 0.4, 0.6, 1.8, 2.4, and 1.8% of the dry weight of the freeze-dried leaf tissue.

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: The effect of amino acid changes in predicted TMH4 on (1-3,1-4)-β-glucan structure across species. The DP3/DP4 ratio of (1-3,1-4)-β-glucan produced in N. benthamiana leaf from wild-type CslF6 proteins with an isoleucine in predicted TMH4 is shown as black bars. When the indicated isoleucine is changed to a leucine, the DP3/DP4 ratio of the (1-3,1-4)-β-glucan is decreased (light gray bars). A further decrease in the DP3/DP4 ratio is observed when a second amino acid substitution is made in the HvCslF6 TMH4 region (HvCslF6 S752G,I757L ). Shown are averages and SDs of replicates from at least two transformation experiments. The amount of (1-3,1-4)-β-glucan produced for the respective constructs was 1.8, 2.2, 0.4, 0.6, 1.8, 2.4, and 1.8% of the dry weight of the freeze-dried leaf tissue.

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Produced, Transformation Assay, Construct

    The predicted TMH4 of CslF6 controls (1-3,1-4)-β-glucan structure. ( A ) Diagrammatic representation of the full-length CslF6 protein sequence (gray rectangle; 1 to 947 amino acids; numbers refer to the HvCslF6 protein), with predicted TMHs shown as thin dark barrels and the approximate positions of the conserved amino acids of the active site in single-letter code. Red lines indicate approximate positions of restriction sites used in construction of chimeric genes shown below as blue or yellow rectangles (representing barley HvCslF6 and maize ZmCslF6, respectively). The numbers within the rectangles are the DP3/DP4 ratios of the (1-3,1-4)-β-glucan produced by the corresponding chimeric proteins in N. benthamiana leaf, and the boxed area indicates the region controlling this ratio (that is, blue area has a high and yellow area has a low DP3/DP4 ratio). Genes were fused at the Bgl II site. ( B ) The region controlling (1-3,1-4)-β-glucan structure was further defined to be between the Bgl II and Xba I sites encompassing TMH3 to TMH6 of the CslF6 protein. ( C ) Expanded view of this region with the protein shown as a gray rectangle; numbers refer to the boundaries of the predicted TMHs of the HvCslF6 protein; and the positions of the Bgl II, Pst I, and Xba I sites are shown on top. The hash marks (#) represent the position of the 13 amino acid differences between the HvCslF6 and ZmCslF6 proteins in this region. By comparing the four Bgl II–Xba I chimeras and the single Pst I chimera, the region controlling the DP3/DP4 ratio is further limited to the four amino acid differences in TMH4 of the CslF6 protein.

    Journal: Science Advances

    Article Title: Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

    doi: 10.1126/sciadv.1500069

    Figure Lengend Snippet: The predicted TMH4 of CslF6 controls (1-3,1-4)-β-glucan structure. ( A ) Diagrammatic representation of the full-length CslF6 protein sequence (gray rectangle; 1 to 947 amino acids; numbers refer to the HvCslF6 protein), with predicted TMHs shown as thin dark barrels and the approximate positions of the conserved amino acids of the active site in single-letter code. Red lines indicate approximate positions of restriction sites used in construction of chimeric genes shown below as blue or yellow rectangles (representing barley HvCslF6 and maize ZmCslF6, respectively). The numbers within the rectangles are the DP3/DP4 ratios of the (1-3,1-4)-β-glucan produced by the corresponding chimeric proteins in N. benthamiana leaf, and the boxed area indicates the region controlling this ratio (that is, blue area has a high and yellow area has a low DP3/DP4 ratio). Genes were fused at the Bgl II site. ( B ) The region controlling (1-3,1-4)-β-glucan structure was further defined to be between the Bgl II and Xba I sites encompassing TMH3 to TMH6 of the CslF6 protein. ( C ) Expanded view of this region with the protein shown as a gray rectangle; numbers refer to the boundaries of the predicted TMHs of the HvCslF6 protein; and the positions of the Bgl II, Pst I, and Xba I sites are shown on top. The hash marks (#) represent the position of the 13 amino acid differences between the HvCslF6 and ZmCslF6 proteins in this region. By comparing the four Bgl II–Xba I chimeras and the single Pst I chimera, the region controlling the DP3/DP4 ratio is further limited to the four amino acid differences in TMH4 of the CslF6 protein.

    Article Snippet: Briefly, the sample was incubated for 2 hours with 20 μl (1 U) of lichenase (Megazyme) to digest the (1-3,1-4)-β-glucan into oligosaccharides of DP3-DP9 and centrifuged at 10,000 rpm for 5 min; triplicate 10-μl samples were removed for (1-3,1-4)-β-glucan assay by further digestion with β-glucosidase; and the glucose released was measured spectrophotometrically against glucose standards as described in the Megazyme kit protocol.

    Techniques: Sequencing, Produced

    Moisture adsorption isotherm of ( a ) control and ( b ) beta glucan-rich biscuits at various temperatures

    Journal: Journal of Food Science and Technology

    Article Title: Beta-glucan rich composite flour biscuits: modelling of moisture sorption isotherms and determination of sorption heat

    doi: 10.1007/s13197-014-1658-2

    Figure Lengend Snippet: Moisture adsorption isotherm of ( a ) control and ( b ) beta glucan-rich biscuits at various temperatures

    Article Snippet: Chemical composition of biscuits in terms of moisture, fat, protein, crude fibre and total ash was determined using standard methods (IS 12711 ; AOAC ) while beta-glucan was estimated by using a kit (Megazyme International, Ireland).

    Techniques: Adsorption

    Netisosteric heat of sorption of beta glucan-rich biscuit at different moisture contents

    Journal: Journal of Food Science and Technology

    Article Title: Beta-glucan rich composite flour biscuits: modelling of moisture sorption isotherms and determination of sorption heat

    doi: 10.1007/s13197-014-1658-2

    Figure Lengend Snippet: Netisosteric heat of sorption of beta glucan-rich biscuit at different moisture contents

    Article Snippet: Chemical composition of biscuits in terms of moisture, fat, protein, crude fibre and total ash was determined using standard methods (IS 12711 ; AOAC ) while beta-glucan was estimated by using a kit (Megazyme International, Ireland).

    Techniques:

    Sorption isosters of beta glucan-rich biscuit at different moisture contents

    Journal: Journal of Food Science and Technology

    Article Title: Beta-glucan rich composite flour biscuits: modelling of moisture sorption isotherms and determination of sorption heat

    doi: 10.1007/s13197-014-1658-2

    Figure Lengend Snippet: Sorption isosters of beta glucan-rich biscuit at different moisture contents

    Article Snippet: Chemical composition of biscuits in terms of moisture, fat, protein, crude fibre and total ash was determined using standard methods (IS 12711 ; AOAC ) while beta-glucan was estimated by using a kit (Megazyme International, Ireland).

    Techniques:

    Thin layer chromatography analysis of hydrolysis products released by Cel01. Degradation of CMC ( a ) and barley glucan ( b ) was analyzed at the indicated time points. Lane M , mixed standard sugars: glucose (G1), cellobiose (G2), cellotriose (G3), and cellotetraose (G4); lane -, control containing substrate without enzyme

    Journal: Biotechnology Letters

    Article Title: Identification and characterization of novel cellulolytic and hemicellulolytic genes and enzymes derived from German grassland soil metagenomes

    doi: 10.1007/s10529-011-0830-2

    Figure Lengend Snippet: Thin layer chromatography analysis of hydrolysis products released by Cel01. Degradation of CMC ( a ) and barley glucan ( b ) was analyzed at the indicated time points. Lane M , mixed standard sugars: glucose (G1), cellobiose (G2), cellotriose (G3), and cellotetraose (G4); lane -, control containing substrate without enzyme

    Article Snippet: Both xylanases exhibited activity with different xylans as substrates, but no activity was recorded by employing barley glucan, CMC, HEC, laminarin, lichenan, or microcrystalline cellulose as substrates.

    Techniques: Thin Layer Chromatography

    Effects of phagocytosis impairment on the response of human monocytes toward whole Candida albicans and the cell wall fraction composed of branched β-glucan. (A and B) Human monocytes were left untreated (ctrl) or stimulated with either heat-killed Candida albicans (HK-C.a., A) or heat-killed Saccharomyces cerevisiae (HK-S.c., B) in the presence (Cyt D) or in the absence (DMSO) of cytochalasin D. (C) Cells were stimulated with the Alkali-Soluble (AS) and Insoluble (AI) fractions, β-(1–6)-glucan and β-(1–3)/(1–6) glucan fractions from the cell wall of Saccharomyces cerevisiae after being treated with DMSO or Cyt D. (D) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or from S. cerevisiae (β-glucan S.c.) in the presence or in the absence of Cyt D. (E) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of insoluble linear β- (1–3)-glucan (curdlan) or of soluble branched β-(1–3)-glucan (laminarin) in the presence or in the absence of Cyt D. (F) The particulate branched β-(1–3)-glucan isolated from the cell wall of C. albicans was sonicated (Sonifier cell Disruptor B-30. Outputcontrol 4, Duty cycle 40%; 2 times 10 cycle with 5min on ice in between the two sets). Monocytes were then exposed to either sonicated or not-sonicated β–glucan in the presence or in the absence of Cyt D. (G) Cells pre-treated with DMSO or Cyt D were stimulated for 24 h with the indicated concentrations of β-glucan from C. albicans (β-glucan C.a.), HK-C.a., AS and AI fractions from S.c., or the combination of AS+AI (10+10 μg/mL). (H) Monocytes were pre-treated with either DMSO (control), or with cytochalasin D (Cyt D) or latrunculin B (Lat B) (actin polymerization inhibitors), or with jasplakinolide (Jsp, actin polymerization inducer), or with chlorpromazine (CLP, clathrin-mediated endocytic inhibitor) or the lysosomal inhibitor cloroquine (CLQ). Cells were then stimulated with either branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or with heat-killed Candida albicans (HK-C.a.). For all the experiments, culture supernatants were collected after 24h and concentration of secreted TNF-α, IL-6, IL-1β and IL-10 was determined by ELISA. Data were reproducible for all the four cytokines tested even if histograms are not shown. Graphs show the mean ± SEM of at least three independent experiments. For (A, H), n = 8; for (B–G), n = 6; * p

    Journal: European journal of immunology

    Article Title: Impaired phagocytosis directs human monocyte activation in response to fungal derived β-glucan particles

    doi: 10.1002/eji.201747224

    Figure Lengend Snippet: Effects of phagocytosis impairment on the response of human monocytes toward whole Candida albicans and the cell wall fraction composed of branched β-glucan. (A and B) Human monocytes were left untreated (ctrl) or stimulated with either heat-killed Candida albicans (HK-C.a., A) or heat-killed Saccharomyces cerevisiae (HK-S.c., B) in the presence (Cyt D) or in the absence (DMSO) of cytochalasin D. (C) Cells were stimulated with the Alkali-Soluble (AS) and Insoluble (AI) fractions, β-(1–6)-glucan and β-(1–3)/(1–6) glucan fractions from the cell wall of Saccharomyces cerevisiae after being treated with DMSO or Cyt D. (D) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or from S. cerevisiae (β-glucan S.c.) in the presence or in the absence of Cyt D. (E) Data show the stimulation experiments of monocytes with two doses (1 or 10 μg/mL) of insoluble linear β- (1–3)-glucan (curdlan) or of soluble branched β-(1–3)-glucan (laminarin) in the presence or in the absence of Cyt D. (F) The particulate branched β-(1–3)-glucan isolated from the cell wall of C. albicans was sonicated (Sonifier cell Disruptor B-30. Outputcontrol 4, Duty cycle 40%; 2 times 10 cycle with 5min on ice in between the two sets). Monocytes were then exposed to either sonicated or not-sonicated β–glucan in the presence or in the absence of Cyt D. (G) Cells pre-treated with DMSO or Cyt D were stimulated for 24 h with the indicated concentrations of β-glucan from C. albicans (β-glucan C.a.), HK-C.a., AS and AI fractions from S.c., or the combination of AS+AI (10+10 μg/mL). (H) Monocytes were pre-treated with either DMSO (control), or with cytochalasin D (Cyt D) or latrunculin B (Lat B) (actin polymerization inhibitors), or with jasplakinolide (Jsp, actin polymerization inducer), or with chlorpromazine (CLP, clathrin-mediated endocytic inhibitor) or the lysosomal inhibitor cloroquine (CLQ). Cells were then stimulated with either branched β-(1–3)-glucan isolated from C. albicans (β-glucan C.a.) or with heat-killed Candida albicans (HK-C.a.). For all the experiments, culture supernatants were collected after 24h and concentration of secreted TNF-α, IL-6, IL-1β and IL-10 was determined by ELISA. Data were reproducible for all the four cytokines tested even if histograms are not shown. Graphs show the mean ± SEM of at least three independent experiments. For (A, H), n = 8; for (B–G), n = 6; * p

    Article Snippet: Different stimuli were then added to the cells: heat-inactivated Candida albicans (UC820 strain, 30 min at 95 degrees, 105 /mL unless otherwise stated), heat-inactivated Saccharomyces cerevisiae (BY471 strain, 30 min at 95 degrees, 106 /mL unless otherwise stated), purified β–glucan from Candida albicans (1 μg/mL unless otherwise stated; depyrogenated was provided by Dr. David L. Williams, East Tennessee State University) (β–glucan from Candida albicans was purified as described [ ]); purified β–glucan from Saccharomyces cerevisiae (1 or 10 μg/mL, G5011, SIGMA); Laminarin from Laminaria digitata (1 or 10 μg/mL, L9634, SIGMA); curdlan from Alcaligenes faecalis (1 or 10 μg/mL, Wako); alkali-soluble and insoluble fractions from Saccharomyces cerevisiae (1, 10 or 50 μg/mL); β-(1–6)-glucan from Saccharomyces cerevisiae (1 or 10 μg/mL); β-(1–3)/(1–6)-glucan from Saccharomyces cerevisiae (1 or 10 μg/mL).

    Techniques: Isolation, Sonication, Concentration Assay, Enzyme-linked Immunosorbent Assay

    In vitro inhibitory activities of Qingke β-glucans on α-amylase ( A ) and pancreatic lipase ( B ). BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; the error bars are standard deviations; significant ( p

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Correlations of Molecular Weights of β-Glucans from Qingke (Tibetan Hulless Barley) to Their Multiple Bioactivities

    doi: 10.3390/molecules23071710

    Figure Lengend Snippet: In vitro inhibitory activities of Qingke β-glucans on α-amylase ( A ) and pancreatic lipase ( B ). BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; the error bars are standard deviations; significant ( p

    Article Snippet: The mixed-linkage β-glucan assay kit and endo-1,4-β-xylanase were obtained from Megazyme (Wicklow, Ireland).

    Techniques: In Vitro

    Cell viability ( A ) and NO production ( B ) of RAW264.7 macrophages treated with Qingke β-glucans. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; The error bars are standard deviations; the differences of cell viability between sample and control are significant at * p

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Correlations of Molecular Weights of β-Glucans from Qingke (Tibetan Hulless Barley) to Their Multiple Bioactivities

    doi: 10.3390/molecules23071710

    Figure Lengend Snippet: Cell viability ( A ) and NO production ( B ) of RAW264.7 macrophages treated with Qingke β-glucans. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; The error bars are standard deviations; the differences of cell viability between sample and control are significant at * p

    Article Snippet: The mixed-linkage β-glucan assay kit and endo-1,4-β-xylanase were obtained from Megazyme (Wicklow, Ireland).

    Techniques:

    In vitro anti-cancer activities of Qingke β-glucans against A549 ( A ); HCT116 ( B ); and MDA-MB-231 ( C ) cells. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; The error bars are standard deviations; the differences of cell viability between sample and control groups are significant at * p

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Correlations of Molecular Weights of β-Glucans from Qingke (Tibetan Hulless Barley) to Their Multiple Bioactivities

    doi: 10.3390/molecules23071710

    Figure Lengend Snippet: In vitro anti-cancer activities of Qingke β-glucans against A549 ( A ); HCT116 ( B ); and MDA-MB-231 ( C ) cells. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min; The error bars are standard deviations; the differences of cell viability between sample and control groups are significant at * p

    Article Snippet: The mixed-linkage β-glucan assay kit and endo-1,4-β-xylanase were obtained from Megazyme (Wicklow, Ireland).

    Techniques: In Vitro, Multiple Displacement Amplification

    HPSEC-RID chromatograms and molecular weights of Qingke β-glucans. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Correlations of Molecular Weights of β-Glucans from Qingke (Tibetan Hulless Barley) to Their Multiple Bioactivities

    doi: 10.3390/molecules23071710

    Figure Lengend Snippet: HPSEC-RID chromatograms and molecular weights of Qingke β-glucans. BG , Qingke β-glucan; BGD1 , Qingke β-glucan with acid hydrolysis for 10 min; BGD2 , Qingke β-glucan with acid hydrolysis for 20 min.

    Article Snippet: The mixed-linkage β-glucan assay kit and endo-1,4-β-xylanase were obtained from Megazyme (Wicklow, Ireland).

    Techniques:

    Response surface plots for bioactive compounds content in germinated barley flour as a function of two independent variables (time and temperature). ( a ) β-glucan; ( b ) GABA; ( c ) TPC. BS: barley seed flour (non-germinated).

    Journal: Foods

    Article Title: Sprouted Barley Flour as a Nutritious and Functional Ingredient

    doi: 10.3390/foods9030296

    Figure Lengend Snippet: Response surface plots for bioactive compounds content in germinated barley flour as a function of two independent variables (time and temperature). ( a ) β-glucan; ( b ) GABA; ( c ) TPC. BS: barley seed flour (non-germinated).

    Article Snippet: Content of β-Glucan The β-glucan content was quantified by 1.3:1.4 mixed-linkage β-glucan kit (Megazyme, Ireland), following the manufacturer instructions.

    Techniques:

    Changes in glucan concentrations by elicitor treatments in the cultivation of Sparassis latifolia on a Pinus densiflora sawdust-based medium. G, glucuronidase; Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The values were not significantly different at the 5% level by ANOVA ( p = 0.2993 for β-glucan).

    Journal: Mycobiology

    Article Title: Enhancement of ?-Glucan Content in the Cultivation of Cauliflower Mushroom (Sparassis latifolia) by Elicitation

    doi: 10.5941/MYCO.2014.42.1.41

    Figure Lengend Snippet: Changes in glucan concentrations by elicitor treatments in the cultivation of Sparassis latifolia on a Pinus densiflora sawdust-based medium. G, glucuronidase; Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The values were not significantly different at the 5% level by ANOVA ( p = 0.2993 for β-glucan).

    Article Snippet: Assay for the glucan contents A β-glucan assay kit (Megazyme International, Wicklow, Ireland) was used to determine total, α-, and β-glucan.

    Techniques:

    Concentration of glucan in the fruit body of Sparassis latifolia cultivated on a sawdust-based medium from three kinds of conifers. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3).

    Journal: Mycobiology

    Article Title: Enhancement of ?-Glucan Content in the Cultivation of Cauliflower Mushroom (Sparassis latifolia) by Elicitation

    doi: 10.5941/MYCO.2014.42.1.41

    Figure Lengend Snippet: Concentration of glucan in the fruit body of Sparassis latifolia cultivated on a sawdust-based medium from three kinds of conifers. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3).

    Article Snippet: Assay for the glucan contents A β-glucan assay kit (Megazyme International, Wicklow, Ireland) was used to determine total, α-, and β-glucan.

    Techniques: Concentration Assay

    Changes in glucan concentrations by the elicitor treatments in the cultivation of Sparassis latifolia on a Larix kaempferi sawdust-based medium. G, glucuronidase; Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3, p = 0.0066).

    Journal: Mycobiology

    Article Title: Enhancement of ?-Glucan Content in the Cultivation of Cauliflower Mushroom (Sparassis latifolia) by Elicitation

    doi: 10.5941/MYCO.2014.42.1.41

    Figure Lengend Snippet: Changes in glucan concentrations by the elicitor treatments in the cultivation of Sparassis latifolia on a Larix kaempferi sawdust-based medium. G, glucuronidase; Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3, p = 0.0066).

    Article Snippet: Assay for the glucan contents A β-glucan assay kit (Megazyme International, Wicklow, Ireland) was used to determine total, α-, and β-glucan.

    Techniques:

    Changes in glucan concentrations by elicitor treatments in the cultivation of Sparassis latifolia on a Pinus koraiensis sawdust-based medium. G, glucuronidase, Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3, p = 0.0394).

    Journal: Mycobiology

    Article Title: Enhancement of ?-Glucan Content in the Cultivation of Cauliflower Mushroom (Sparassis latifolia) by Elicitation

    doi: 10.5941/MYCO.2014.42.1.41

    Figure Lengend Snippet: Changes in glucan concentrations by elicitor treatments in the cultivation of Sparassis latifolia on a Pinus koraiensis sawdust-based medium. G, glucuronidase, Ly, lysing enzyme; Ch, chitinase. The numbers indicate the amount of each enzyme for each bottle in mL. The same letters on each bar indicate that the values were not significantly different by the least significant difference test at the 5% level (n = 3, p = 0.0394).

    Article Snippet: Assay for the glucan contents A β-glucan assay kit (Megazyme International, Wicklow, Ireland) was used to determine total, α-, and β-glucan.

    Techniques:

    α ( A ), β ( B ), and total ( C ) glucan concentrations in glucan extracts prepared from caps and stalks from Pleurotus eryngii mushrooms cultivated in various relative amounts of eucalyptus sawdust and OMSW. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Olive Mill Waste Enhances α-Glucan Content in the Edible Mushroom Pleurotus eryngii

    doi: 10.3390/ijms18071564

    Figure Lengend Snippet: α ( A ), β ( B ), and total ( C ) glucan concentrations in glucan extracts prepared from caps and stalks from Pleurotus eryngii mushrooms cultivated in various relative amounts of eucalyptus sawdust and OMSW. * p

    Article Snippet: Glucans Analysis The glucan content of the dried Pleurotus fruiting bodies ( ) or extracted glucans ( ) was determined using a mushroom and yeast specific β-glucan kit (Megazyme International, Wicklow, Ireland) based on a colorimetric reaction [ , ].

    Techniques:

    α ( A ), β ( B ), and total ( C ) glucan concentrations in whole mill mushrooms prepared from caps and stalks from Pleurotus eryngii mushrooms cultivated in various relative amounts of eucalyptus sawdust and OMSW. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Olive Mill Waste Enhances α-Glucan Content in the Edible Mushroom Pleurotus eryngii

    doi: 10.3390/ijms18071564

    Figure Lengend Snippet: α ( A ), β ( B ), and total ( C ) glucan concentrations in whole mill mushrooms prepared from caps and stalks from Pleurotus eryngii mushrooms cultivated in various relative amounts of eucalyptus sawdust and OMSW. * p

    Article Snippet: Glucans Analysis The glucan content of the dried Pleurotus fruiting bodies ( ) or extracted glucans ( ) was determined using a mushroom and yeast specific β-glucan kit (Megazyme International, Wicklow, Ireland) based on a colorimetric reaction [ , ].

    Techniques:

    α, β, and total glucan concentrations in caps and stalks of the mushroom strain Pleurotus eryngii . * p

    Journal: International Journal of Molecular Sciences

    Article Title: Olive Mill Waste Enhances α-Glucan Content in the Edible Mushroom Pleurotus eryngii

    doi: 10.3390/ijms18071564

    Figure Lengend Snippet: α, β, and total glucan concentrations in caps and stalks of the mushroom strain Pleurotus eryngii . * p

    Article Snippet: Glucans Analysis The glucan content of the dried Pleurotus fruiting bodies ( ) or extracted glucans ( ) was determined using a mushroom and yeast specific β-glucan kit (Megazyme International, Wicklow, Ireland) based on a colorimetric reaction [ , ].

    Techniques:

    ( A ) α-glucan concentration in various Pleurotus strains; ( B ) β-glucan concentration in various Pleurotus strains and ( C ) Total glucan concentration. All concentrations are related to the percentage of dried weight. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Olive Mill Waste Enhances α-Glucan Content in the Edible Mushroom Pleurotus eryngii

    doi: 10.3390/ijms18071564

    Figure Lengend Snippet: ( A ) α-glucan concentration in various Pleurotus strains; ( B ) β-glucan concentration in various Pleurotus strains and ( C ) Total glucan concentration. All concentrations are related to the percentage of dried weight. * p

    Article Snippet: Glucans Analysis The glucan content of the dried Pleurotus fruiting bodies ( ) or extracted glucans ( ) was determined using a mushroom and yeast specific β-glucan kit (Megazyme International, Wicklow, Ireland) based on a colorimetric reaction [ , ].

    Techniques: Concentration Assay

    Quantitative real-time PCR analysis of select targets regulated by β-D-glucan in MCF-7 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle control), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S rRNA and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment.

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: Quantitative real-time PCR analysis of select targets regulated by β-D-glucan in MCF-7 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle control), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S rRNA and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment.

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Real-time Polymerase Chain Reaction, Droplet Countercurrent Chromatography, Expressing

    β-D-glucan dissolved in DMSO but not water inhibits MCF-7 cell proliferation. MCF-7 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in water or DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the mean ± SEM for 4 separate values in one experiment for β-D-glucan in water and 6 separate experiments (biological replicates) for β-D-glucan in DMSO. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan dissolved in DMSO but not water inhibits MCF-7 cell proliferation. MCF-7 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in water or DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the mean ± SEM for 4 separate values in one experiment for β-D-glucan in water and 6 separate experiments (biological replicates) for β-D-glucan in DMSO. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Incubation, Droplet Countercurrent Chromatography

    β-D-glucan increases apoptosis and cell death in MCF-7 and LCC9 cells. (A) MCF-7 tamoxifen-sensitive and LCC9 tamoxifen-resistant breast cancer cells were incubated in phenol red-free IMEM + 5% DCC for 48 h prior to addition of the indicated concentrations of β-D-glucan dissolved in DMSO or DMSO as vehicle control for 24 h. BAX and BCL2 mRNA transcript expression was normalized by GAPDH (B) and the fold relative to DMSO (vehicle control) was set to one. (B) qPCR for GAPDH expression is given as CT values. For (A) and (B), the values are the average ± SEM of triplicate determinations within one experiment. (C) MCF-7 and LCC9 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO or DMSO as vehicle control for 72 h with a medium/treatment change after 48 h. Live/Dead Viability/Cytotoxicity assay was performed as described in Materials and methods. Values are the % of dead cells measured by uptake of ethidium homodimer-1 and fluorescence emission at 645 nm. Values are the average of 4 replicates within one experiment. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan increases apoptosis and cell death in MCF-7 and LCC9 cells. (A) MCF-7 tamoxifen-sensitive and LCC9 tamoxifen-resistant breast cancer cells were incubated in phenol red-free IMEM + 5% DCC for 48 h prior to addition of the indicated concentrations of β-D-glucan dissolved in DMSO or DMSO as vehicle control for 24 h. BAX and BCL2 mRNA transcript expression was normalized by GAPDH (B) and the fold relative to DMSO (vehicle control) was set to one. (B) qPCR for GAPDH expression is given as CT values. For (A) and (B), the values are the average ± SEM of triplicate determinations within one experiment. (C) MCF-7 and LCC9 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO or DMSO as vehicle control for 72 h with a medium/treatment change after 48 h. Live/Dead Viability/Cytotoxicity assay was performed as described in Materials and methods. Values are the % of dead cells measured by uptake of ethidium homodimer-1 and fluorescence emission at 645 nm. Values are the average of 4 replicates within one experiment. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Incubation, Droplet Countercurrent Chromatography, Expressing, Real-time Polymerase Chain Reaction, Cytotoxicity Assay, Fluorescence

    Quantitative real-time PCR analysis of select targets regulated by β-D-glucan in MCF-7 and LCC9 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment. (A) RASSF1, CTNNB1, IGFBP3, AR and NRF1 transcript expression in MCF-7 cells relative to DMSO control. (B) CTNNB1 , (C) IGFBP3 , (D) RASSF1 and (E) ESR2 (ERβ) transcript expression in MCF-7 and LCC9 cells relative to DMSO control.

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: Quantitative real-time PCR analysis of select targets regulated by β-D-glucan in MCF-7 and LCC9 cells. Cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of DMSO (vehicle), 10 nM E 2 , 100 nM 4-OHT or the indicated concentrations of DMSO-dissolved β-D-glucan for 24 h. qPCR for each target gene was normalized to 18S and values were compared to fold expression in vehicle (DMSO)-treated MCF-7 cells. Values are the average of triplicate determinations ± SEM within one experiment. (A) RASSF1, CTNNB1, IGFBP3, AR and NRF1 transcript expression in MCF-7 cells relative to DMSO control. (B) CTNNB1 , (C) IGFBP3 , (D) RASSF1 and (E) ESR2 (ERβ) transcript expression in MCF-7 and LCC9 cells relative to DMSO control.

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Real-time Polymerase Chain Reaction, Droplet Countercurrent Chromatography, Expressing

    β-D-glucan inhibits MCF-10A but not HEK-293 cell proliferation. MCF-10A and HEK-293 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 4 separate values in one experiment. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan inhibits MCF-10A but not HEK-293 cell proliferation. MCF-10A and HEK-293 cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 4 separate values in one experiment. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Incubation, Droplet Countercurrent Chromatography, BrdU Incorporation Assay

    β-D-glucan inhibits the proliferation of endocrine-resistant breast cancer cells. LCC9 and LY2 endocrine-resistant breast cancer cells (A) and MDA-MB-231 triple negative breast cancer cells (B) were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 3 separate experiments. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan inhibits the proliferation of endocrine-resistant breast cancer cells. LCC9 and LY2 endocrine-resistant breast cancer cells (A) and MDA-MB-231 triple negative breast cancer cells (B) were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 3 separate experiments. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Multiple Displacement Amplification, Incubation, Droplet Countercurrent Chromatography, BrdU Incorporation Assay

    β-D-glucan rapidly inhibits NRF1 expression in MCF-7 cells. MCF-7 cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of the indicated concentrations of DMSO-dissolved β-D-glucan for 45 min. (A) qPCR for NRF1 mRNA expression was normalized to 18S rRNA. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan rapidly inhibits NRF1 expression in MCF-7 cells. MCF-7 cells were grown in phenol red-free IMEM + 5% DCC for 48 h prior to addition of the indicated concentrations of DMSO-dissolved β-D-glucan for 45 min. (A) qPCR for NRF1 mRNA expression was normalized to 18S rRNA. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Expressing, Droplet Countercurrent Chromatography, Real-time Polymerase Chain Reaction

    β-D-glucan does not synergize with 4-hydroxytamoxifen to inhibit cell proliferation. MCF-7 tamoxifen-sensitive and LY2 tamoxifen-resistant breast cancer cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO, 1 μ M 4-OHT, or the combination of 1 μ M 4-OHT + 10 or 50 μ g/ml β-D-glucan, as indicated, for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 3 separate experiments. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan does not synergize with 4-hydroxytamoxifen to inhibit cell proliferation. MCF-7 tamoxifen-sensitive and LY2 tamoxifen-resistant breast cancer cells were incubated in phenol red-free IMEM + 5% DCC and the indicated concentrations of β-D-glucan dissolved in DMSO, 1 μ M 4-OHT, or the combination of 1 μ M 4-OHT + 10 or 50 μ g/ml β-D-glucan, as indicated, for a total of 72 h with a medium/treatment change after 48 h. Values are the BrdU incorporation absorbances normalized to DMSO (zero) and are the mean ± SEM for 3 separate experiments. Values of β-D-glucan in DMSO were corrected for the inhibitory effect of DMSO on cell proliferation. * p

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Incubation, Droplet Countercurrent Chromatography, BrdU Incorporation Assay

    β-D-glucan affects ERα expression in MCF-7 and LCC9 cells. Cells were grown in phenol red-free IMEM + 5% DCC-stripped FBS for 48 h prior to addition of DMSO (vehicle control) or 10 or 50 μ g/ml β-D-glucan dissolved in DMSO for 24 h. (A) ESR1 transcript levels were measured by qPCR relative to 18S and are the average of triplicate determinations ± SEM within one experiment. Values are relative to MCF-7 cells treated with DMSO showing that ERα mRNA expression is lower in LCC9 relative to MCF-7 cells. (B) Whole cell extracts (30 μ g protein) were separated on 10% SDS-PAGE gels and the resulting western blot was probed with ERα antibody and the full length 66 kDa ERα band is shown. The PVDF membrane was stripped and re-probed for β-actin for normalization. Values are the ERα/β-actin ratio.

    Journal: International Journal of Oncology

    Article Title: ?-D-glucan inhibits endocrine-resistant breast cancer cell proliferation and alters gene expression

    doi: 10.3892/ijo.2014.2294

    Figure Lengend Snippet: β-D-glucan affects ERα expression in MCF-7 and LCC9 cells. Cells were grown in phenol red-free IMEM + 5% DCC-stripped FBS for 48 h prior to addition of DMSO (vehicle control) or 10 or 50 μ g/ml β-D-glucan dissolved in DMSO for 24 h. (A) ESR1 transcript levels were measured by qPCR relative to 18S and are the average of triplicate determinations ± SEM within one experiment. Values are relative to MCF-7 cells treated with DMSO showing that ERα mRNA expression is lower in LCC9 relative to MCF-7 cells. (B) Whole cell extracts (30 μ g protein) were separated on 10% SDS-PAGE gels and the resulting western blot was probed with ERα antibody and the full length 66 kDa ERα band is shown. The PVDF membrane was stripped and re-probed for β-actin for normalization. Values are the ERα/β-actin ratio.

    Article Snippet: ICI 182,780 was from Tocris (Ellisville, MO, USA). β-D-glucan was purchased from Sigma (cat. no. G6513, purity ∼97%). β-D-glucan was dissolved either in water or in DMSO (Sigma) by heating in a waterbath at 90°C for 4–5 min. Once dissolved, the β-D-glucan stocks were stored at −20°C until use.

    Techniques: Expressing, Droplet Countercurrent Chromatography, Real-time Polymerase Chain Reaction, SDS Page, Western Blot

    Glucan and xylan conversion during the hydrolysis of EA pretreated newspaper waste by using MIX 1 (15 mg/g of glucan of commercial enzymatic preparation Novozymes Cellic ® —60 % CTec3 and 40 % HTec3; MIX 2 (adding 3.32 mg/g glucan of endoglucanase rCelStrep to MIX 1); MIX 3 (adding 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 4 (adding 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX A’); MIX 5 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 6 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1)

    Journal: AMB Express

    Article Title: Saccharification of newspaper waste after ammonia fiber expansion or extractive ammonia

    doi: 10.1186/s13568-016-0189-9

    Figure Lengend Snippet: Glucan and xylan conversion during the hydrolysis of EA pretreated newspaper waste by using MIX 1 (15 mg/g of glucan of commercial enzymatic preparation Novozymes Cellic ® —60 % CTec3 and 40 % HTec3; MIX 2 (adding 3.32 mg/g glucan of endoglucanase rCelStrep to MIX 1); MIX 3 (adding 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 4 (adding 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX A’); MIX 5 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 6 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1)

    Article Snippet: Moreover, rCelStrep, rPoAbf or rPoAbf F435Y/Y446F were added alternatively or in combination to the MIX 1 containing 15 mg/g glucan of commercial preparation mix (60 % Cellic® CTec3 and 40 % Cellic® HTec3 from Novozymes).

    Techniques: Mutagenesis

    Glucan and xylan conversion during the hydrolysis of AFEX pretreated newspaper waste by using MIX A: CBH I, CBH II and EG I (3.32 mg/g glucan each), βG (2 mg/g glucan), LX3 and LX4 (1.66 mg/g glucan each), LβX and LArb (0.6 mg/g glucan each); MIX B (replacing EG I with endoglucanase rCelStrep); MIX C (replacing LArb with the α- l -arabinofuranosidase rPoAbf); MIX D (replacing LArb with mutant rPoAbf F435Y/Y446F)

    Journal: AMB Express

    Article Title: Saccharification of newspaper waste after ammonia fiber expansion or extractive ammonia

    doi: 10.1186/s13568-016-0189-9

    Figure Lengend Snippet: Glucan and xylan conversion during the hydrolysis of AFEX pretreated newspaper waste by using MIX A: CBH I, CBH II and EG I (3.32 mg/g glucan each), βG (2 mg/g glucan), LX3 and LX4 (1.66 mg/g glucan each), LβX and LArb (0.6 mg/g glucan each); MIX B (replacing EG I with endoglucanase rCelStrep); MIX C (replacing LArb with the α- l -arabinofuranosidase rPoAbf); MIX D (replacing LArb with mutant rPoAbf F435Y/Y446F)

    Article Snippet: Moreover, rCelStrep, rPoAbf or rPoAbf F435Y/Y446F were added alternatively or in combination to the MIX 1 containing 15 mg/g glucan of commercial preparation mix (60 % Cellic® CTec3 and 40 % Cellic® HTec3 from Novozymes).

    Techniques: Mutagenesis

    Glucan and xylan conversion during the hydrolysis of AFEX pretreated newspaper waste by using MIX 1 (15 mg/g of glucan of commercial enzymatic preparation Novozymes Cellic ® —60 % CTec3 and 40 % HTec3; MIX 2 (adding 3.32 mg/g glucan of endoglucanase rCelStrep to MIX 1); MIX 3 (adding 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 4 (adding 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1); MIX 5 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 6 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1)

    Journal: AMB Express

    Article Title: Saccharification of newspaper waste after ammonia fiber expansion or extractive ammonia

    doi: 10.1186/s13568-016-0189-9

    Figure Lengend Snippet: Glucan and xylan conversion during the hydrolysis of AFEX pretreated newspaper waste by using MIX 1 (15 mg/g of glucan of commercial enzymatic preparation Novozymes Cellic ® —60 % CTec3 and 40 % HTec3; MIX 2 (adding 3.32 mg/g glucan of endoglucanase rCelStrep to MIX 1); MIX 3 (adding 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 4 (adding 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1); MIX 5 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the α- l -arabinofuranosidase rPoAbf to MIX 1); MIX 6 (adding 3.32 mg/g glucan of endoglucanase rCelStrep and 0.6 mg/g glucan of the mutant rPoAbf F435Y/Y446F to MIX 1)

    Article Snippet: Moreover, rCelStrep, rPoAbf or rPoAbf F435Y/Y446F were added alternatively or in combination to the MIX 1 containing 15 mg/g glucan of commercial preparation mix (60 % Cellic® CTec3 and 40 % Cellic® HTec3 from Novozymes).

    Techniques: Mutagenesis

    Glucan and xylan conversion during the hydrolysis of EA pretreated newspaper waste by using MIX A: CBH I, CBH II and EG I (3.32 mg/g glucan each), βG (2 mg/g glucan), LX3 and LX4 (1.66 mg/g glucan each), LβX and LArb (0.6 mg/g glucan each); MIX B (replacing EG I with endoglucanase rCelStrep); MIX C (replacing LArb with the α- l -arabinofuranosidase rPoAbf); MIX D (replacing LArb with mutant rPoAbf F435Y/Y446F)

    Journal: AMB Express

    Article Title: Saccharification of newspaper waste after ammonia fiber expansion or extractive ammonia

    doi: 10.1186/s13568-016-0189-9

    Figure Lengend Snippet: Glucan and xylan conversion during the hydrolysis of EA pretreated newspaper waste by using MIX A: CBH I, CBH II and EG I (3.32 mg/g glucan each), βG (2 mg/g glucan), LX3 and LX4 (1.66 mg/g glucan each), LβX and LArb (0.6 mg/g glucan each); MIX B (replacing EG I with endoglucanase rCelStrep); MIX C (replacing LArb with the α- l -arabinofuranosidase rPoAbf); MIX D (replacing LArb with mutant rPoAbf F435Y/Y446F)

    Article Snippet: Moreover, rCelStrep, rPoAbf or rPoAbf F435Y/Y446F were added alternatively or in combination to the MIX 1 containing 15 mg/g glucan of commercial preparation mix (60 % Cellic® CTec3 and 40 % Cellic® HTec3 from Novozymes).

    Techniques: Mutagenesis

    Increased expression of ATF4-stimulated HCECs and THP-1 macrophages. (a) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in HCECs were not changed significantly at 8 hours. (b) ATF4 protein levels in HCECs did not change significantly at 16 hours with the stimulation of LPS, β -1, 3-glucan, TGF- β , and IL-1 β , but significantly increased with A. fumigatus conidia. (c) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in THP-1 macrophages did not change significantly at 8 hours. (d) ATF4 protein levels in HCECs were higher after stimulation with LPS, TGF- β , IL-1 β , and A. fumigatus conidia at 16 hours, but did not change significantly with β -1, 3-glucan. The mean values and standard deviations of two independent experiments are shown; ∗∗ P

    Journal: Journal of Ophthalmology

    Article Title: ATF4 Involvement in TLR4 and LOX-1-Induced Host Inflammatory Response to Aspergillus fumigatus Keratitis

    doi: 10.1155/2018/5830202

    Figure Lengend Snippet: Increased expression of ATF4-stimulated HCECs and THP-1 macrophages. (a) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in HCECs were not changed significantly at 8 hours. (b) ATF4 protein levels in HCECs did not change significantly at 16 hours with the stimulation of LPS, β -1, 3-glucan, TGF- β , and IL-1 β , but significantly increased with A. fumigatus conidia. (c) With the stimulation of LPS, β -1, 3-glucan, TGF- β , IL-1 β , and A. fumigatus conidia, ATF4 protein levels in THP-1 macrophages did not change significantly at 8 hours. (d) ATF4 protein levels in HCECs were higher after stimulation with LPS, TGF- β , IL-1 β , and A. fumigatus conidia at 16 hours, but did not change significantly with β -1, 3-glucan. The mean values and standard deviations of two independent experiments are shown; ∗∗ P

    Article Snippet: With the stimulation of LPS, β -1, 3-glucan, TGF-β , IL-1β , and A. fumigatus conidia, ATF4 protein levels in THP-1 macrophages were not changed significantly at 8 hours after stimulation (P > 0.05, respectively) ( ).

    Techniques: Expressing

    Echinocandin inhibition profiles for product-entrapped 1,3-β- d -glucan synthase enzyme complexes assessed by the incorporation of [ 3 H]glucose into radiolabeled product. (A) CSF titration curves for enzymes isolated from strains ATCC 90030 (wild

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Effect of Candida glabrata FKS1 and FKS2 Mutations on Echinocandin Sensitivity and Kinetics of 1,3-\u03b2-d-Glucan Synthase: Implication for the Existing Susceptibility Breakpoint

    doi: 10.1128/AAC.00443-09

    Figure Lengend Snippet: Echinocandin inhibition profiles for product-entrapped 1,3-β- d -glucan synthase enzyme complexes assessed by the incorporation of [ 3 H]glucose into radiolabeled product. (A) CSF titration curves for enzymes isolated from strains ATCC 90030 (wild

    Article Snippet: The product of the reaction mixtures was verified as 1,3-β- d -glucan by using a Glucatell kit (Associates of Cape Cod, Inc., Falmouth, MA), following the procedure previously described ( ).

    Techniques: Inhibition, Titration, Isolation

    Lineweaver-Burke double-reciprocal plots used to determine the maximum velocity ( V max ) and the Michaelis-Menten constant ( K m ) for product-entrapped 1,3-β- d -glucan synthase complexes by varying the amount of [ 3 H]UDPG. (A) Comparison of the kinetic

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Effect of Candida glabrata FKS1 and FKS2 Mutations on Echinocandin Sensitivity and Kinetics of 1,3-\u03b2-d-Glucan Synthase: Implication for the Existing Susceptibility Breakpoint

    doi: 10.1128/AAC.00443-09

    Figure Lengend Snippet: Lineweaver-Burke double-reciprocal plots used to determine the maximum velocity ( V max ) and the Michaelis-Menten constant ( K m ) for product-entrapped 1,3-β- d -glucan synthase complexes by varying the amount of [ 3 H]UDPG. (A) Comparison of the kinetic

    Article Snippet: The product of the reaction mixtures was verified as 1,3-β- d -glucan by using a Glucatell kit (Associates of Cape Cod, Inc., Falmouth, MA), following the procedure previously described ( ).

    Techniques:

    C. glabrata 1,3-β- d -glucan synthase enzyme kinetics.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Effect of Candida glabrata FKS1 and FKS2 Mutations on Echinocandin Sensitivity and Kinetics of 1,3-\u03b2-d-Glucan Synthase: Implication for the Existing Susceptibility Breakpoint

    doi: 10.1128/AAC.00443-09

    Figure Lengend Snippet: C. glabrata 1,3-β- d -glucan synthase enzyme kinetics.

    Article Snippet: The product of the reaction mixtures was verified as 1,3-β- d -glucan by using a Glucatell kit (Associates of Cape Cod, Inc., Falmouth, MA), following the procedure previously described ( ).

    Techniques:

    (a) Serum IL-10 in relation to the amount of β -glucan (BAL) pg/mL ( n = 70) and (b) NAHA in homes ( n = 60) of subjects with sarcoidosis.

    Journal: Pulmonary Medicine

    Article Title: Fungal Exposure and Low Levels of IL-10 in Patients with Sarcoidosis

    doi: 10.1155/2014/164565

    Figure Lengend Snippet: (a) Serum IL-10 in relation to the amount of β -glucan (BAL) pg/mL ( n = 70) and (b) NAHA in homes ( n = 60) of subjects with sarcoidosis.

    Article Snippet: Thereafter, 25 μ L was added to each of the four wells in a plate preprepared with a Limulus reagent specific for β -glucan and read in an automatic analyser (Endosafe PTS, Charles River).

    Techniques:

    Silent fungal infections under non-SPF trigger arthritis in SKG mice. (A) PCRs of fungal 18SrDNA or mouse Rag 1 gene from esophagus (Es), lung (Lg), liver (Lv), or foot including ankle joint (Ft) of BALB/c or SKG mice in non-SPF. (B) Lungs of BALB/c or SKG mice in non-SPF or SPF were assessed for fungi by real-time quantitative PCR. (C–F) Methenamine silver (C and E) or hematoxylin and eosin (D and F) stainings of lungs from SKG mice (C and D) or BALB/c (E and F) of non-SPF. Arrows indicate argyrophilic fungal cysts. (G) Male SKG mice of 10 wk of age in the non-SPF facility were treated with four cycles of four daily i.p. injections of 75 μg amphotericin B (arrows) at 10-d intervals. (H) SKG mice in the SPF facility received the same protocol of antifungal treatment 10 d after i.p. administration of 2 mg zymosan (open inverted triangle). (I) Concentration of serum β-glucan in non-SPF or SPF 12-wk-old SKG mice.

    Journal: The Journal of Experimental Medicine

    Article Title: A role for fungal ?-glucans and their receptor Dectin-1 in the induction of autoimmune arthritis in genetically susceptible mice

    doi: 10.1084/jem.20041758

    Figure Lengend Snippet: Silent fungal infections under non-SPF trigger arthritis in SKG mice. (A) PCRs of fungal 18SrDNA or mouse Rag 1 gene from esophagus (Es), lung (Lg), liver (Lv), or foot including ankle joint (Ft) of BALB/c or SKG mice in non-SPF. (B) Lungs of BALB/c or SKG mice in non-SPF or SPF were assessed for fungi by real-time quantitative PCR. (C–F) Methenamine silver (C and E) or hematoxylin and eosin (D and F) stainings of lungs from SKG mice (C and D) or BALB/c (E and F) of non-SPF. Arrows indicate argyrophilic fungal cysts. (G) Male SKG mice of 10 wk of age in the non-SPF facility were treated with four cycles of four daily i.p. injections of 75 μg amphotericin B (arrows) at 10-d intervals. (H) SKG mice in the SPF facility received the same protocol of antifungal treatment 10 d after i.p. administration of 2 mg zymosan (open inverted triangle). (I) Concentration of serum β-glucan in non-SPF or SPF 12-wk-old SKG mice.

    Article Snippet: The concentration of β-glucan was measured by BGSTAR KIT (Wako), a limulus test specific for β-glucan, according to manufacturer's instruction ( ).

    Techniques: Mouse Assay, Real-time Polymerase Chain Reaction, Concentration Assay

    Production of TNF-α by β-glucan–stimulated DCs. (A) BM-DCs were incubated with 10 mg/ml laminarin, 100 μg/ml curdlan, 100 μg/ml zymosan, or 1 μg/ml LPS from day 5 for 24 h and the amount of TNF-α was assessed by ELISA. (B) TNF-α production by BM-DCs that were incubated with 10 μg/ml of 2A11 mAb or control IgG2b for 1 h before culture with 100 μg/ml curdlan or 100 μg/ml zymosan. (C) TNF-α production by MyD88-deficient or wild-type BM-DCs that were cultured with 100 μg/ml curdlan, 100 μg/ml zymosan, or 10 μg/ml LPS. Vertical bars represent the means ± SD of triplicates.

    Journal: The Journal of Experimental Medicine

    Article Title: A role for fungal ?-glucans and their receptor Dectin-1 in the induction of autoimmune arthritis in genetically susceptible mice

    doi: 10.1084/jem.20041758

    Figure Lengend Snippet: Production of TNF-α by β-glucan–stimulated DCs. (A) BM-DCs were incubated with 10 mg/ml laminarin, 100 μg/ml curdlan, 100 μg/ml zymosan, or 1 μg/ml LPS from day 5 for 24 h and the amount of TNF-α was assessed by ELISA. (B) TNF-α production by BM-DCs that were incubated with 10 μg/ml of 2A11 mAb or control IgG2b for 1 h before culture with 100 μg/ml curdlan or 100 μg/ml zymosan. (C) TNF-α production by MyD88-deficient or wild-type BM-DCs that were cultured with 100 μg/ml curdlan, 100 μg/ml zymosan, or 10 μg/ml LPS. Vertical bars represent the means ± SD of triplicates.

    Article Snippet: The concentration of β-glucan was measured by BGSTAR KIT (Wako), a limulus test specific for β-glucan, according to manufacturer's instruction ( ).

    Techniques: Incubation, Enzyme-linked Immunosorbent Assay, Cell Culture

    (a to f) Content of β-glucan or NAGase in aerosols from Botrytis cinerea -colonized gypsum boards, floor paper, or slices of aubergines. The total column is the inhalable fraction sampled with the GSP sampler, the middle fraction of the column

    Journal: Applied and Environmental Microbiology

    Article Title: Effects of Airflow and Changing Humidity on the Aerosolization of Respirable Fungal Fragments and Conidia of Botrytis cinerea

    doi: 10.1128/AEM.07879-11

    Figure Lengend Snippet: (a to f) Content of β-glucan or NAGase in aerosols from Botrytis cinerea -colonized gypsum boards, floor paper, or slices of aubergines. The total column is the inhalable fraction sampled with the GSP sampler, the middle fraction of the column

    Article Snippet: After extraction with NaOH, β-glucan was quantified in duplicate using the kinetic Fungitic G test (Seikagaku Co., Tokyo, Japan).

    Techniques:

    Display of β-glucan during different stages of C. albicans mucosal biofilm growth. Panels depict representative confocal images of tissue sections from mice with oropharyngeal candidiasis (A–D) or from a three-dimensional in vitro model of the oral mucosa (F). Panels A–D and F depict sections stained for β-glucan with a BFDiv monoclonal antibody (red), C. albicans with a polyclonal anti- Candida Ab (green) and counterstained with the nucleic acid stain TO-PRO-3, which stains tissue cells blue. Panel E depicts a section stained with an IgM isotype control antibody for the BFDiv stain. Notice that β-glucan becomes more uniformly present on the surface of fungal cells invading the tongue mucosa (arrows). Scale bar = 20 µm.

    Journal: PLoS ONE

    Article Title: Characterization of Mucosal Candida albicans Biofilms

    doi: 10.1371/journal.pone.0007967

    Figure Lengend Snippet: Display of β-glucan during different stages of C. albicans mucosal biofilm growth. Panels depict representative confocal images of tissue sections from mice with oropharyngeal candidiasis (A–D) or from a three-dimensional in vitro model of the oral mucosa (F). Panels A–D and F depict sections stained for β-glucan with a BFDiv monoclonal antibody (red), C. albicans with a polyclonal anti- Candida Ab (green) and counterstained with the nucleic acid stain TO-PRO-3, which stains tissue cells blue. Panel E depicts a section stained with an IgM isotype control antibody for the BFDiv stain. Notice that β-glucan becomes more uniformly present on the surface of fungal cells invading the tongue mucosa (arrows). Scale bar = 20 µm.

    Article Snippet: To detect β-glucan we used a monoclonal antibody highly specific for (1→6) branched, (1→3)-β-D-glucans (BFDiv, Biothera) found on fungal cell walls, which does not recognize linear, essentially homogeneous glucans .

    Techniques: Mouse Assay, In Vitro, Staining

    β-glucan and extracellular material staining during C. albicans SC5314 in vitro biofilm growth on glass. Panels depict 3D reconstructions of confocal stacks of images of 24h (A), 48h (B) and 72h (C) biofilms of C. albicans grown on cover slips and stained for β-glucan with BFDiv mAb (red) and ConA-Alexa 488 (green). Notice that regardless of biofilm thickness β-glucan is localized in the growing end of the biofilm (arrows).

    Journal: PLoS ONE

    Article Title: Characterization of Mucosal Candida albicans Biofilms

    doi: 10.1371/journal.pone.0007967

    Figure Lengend Snippet: β-glucan and extracellular material staining during C. albicans SC5314 in vitro biofilm growth on glass. Panels depict 3D reconstructions of confocal stacks of images of 24h (A), 48h (B) and 72h (C) biofilms of C. albicans grown on cover slips and stained for β-glucan with BFDiv mAb (red) and ConA-Alexa 488 (green). Notice that regardless of biofilm thickness β-glucan is localized in the growing end of the biofilm (arrows).

    Article Snippet: To detect β-glucan we used a monoclonal antibody highly specific for (1→6) branched, (1→3)-β-D-glucans (BFDiv, Biothera) found on fungal cell walls, which does not recognize linear, essentially homogeneous glucans .

    Techniques: Staining, In Vitro

    β-glucan and extracellular material staining in C. albicans biofilms forming on glass. Panel A depicts a 2h biofilm and panel B depicts a 48h biofilm. Biofilms of the GFP-expressing C. albicans strain (green) were stained for β-glucan with a BFDiv monoclonal antibody (red) and the extracellular material was stained with ConA-Alexa 350 (blue). In 2h biofilms there is partial co-localization of the BFDiv mAb and ConA (pink). BFDiv stains parts of the fungal cell, but not the germinating buds, and ConA stains the entire fungal cell surface (3A). In 48h biofilms deposits of cell-dissociated ECM stained with ConA but not with BFDiv (3B, arrows). Scale bar = 20 µm.

    Journal: PLoS ONE

    Article Title: Characterization of Mucosal Candida albicans Biofilms

    doi: 10.1371/journal.pone.0007967

    Figure Lengend Snippet: β-glucan and extracellular material staining in C. albicans biofilms forming on glass. Panel A depicts a 2h biofilm and panel B depicts a 48h biofilm. Biofilms of the GFP-expressing C. albicans strain (green) were stained for β-glucan with a BFDiv monoclonal antibody (red) and the extracellular material was stained with ConA-Alexa 350 (blue). In 2h biofilms there is partial co-localization of the BFDiv mAb and ConA (pink). BFDiv stains parts of the fungal cell, but not the germinating buds, and ConA stains the entire fungal cell surface (3A). In 48h biofilms deposits of cell-dissociated ECM stained with ConA but not with BFDiv (3B, arrows). Scale bar = 20 µm.

    Article Snippet: To detect β-glucan we used a monoclonal antibody highly specific for (1→6) branched, (1→3)-β-D-glucans (BFDiv, Biothera) found on fungal cell walls, which does not recognize linear, essentially homogeneous glucans .

    Techniques: Staining, Expressing

    Dust borne endotoxin, dust borne (1–3)-β-D-glucan, airborne endotoxin, airborne (1–3)-β-D-glucan, and airborne fungal spores in homes divided into two levels of mold burden based on ERMI index: low (ERMI ≤5; n=135) and high (ERMI > 5; n=48). Histograms show geometric means and error bars show 95% confidence intervals. *** p

    Journal: The Science of the total environment

    Article Title: Visually observed mold and moldy odor versus quantitatively measured microbial exposure in homes

    doi: 10.1016/j.scitotenv.2010.07.090

    Figure Lengend Snippet: Dust borne endotoxin, dust borne (1–3)-β-D-glucan, airborne endotoxin, airborne (1–3)-β-D-glucan, and airborne fungal spores in homes divided into two levels of mold burden based on ERMI index: low (ERMI ≤5; n=135) and high (ERMI > 5; n=48). Histograms show geometric means and error bars show 95% confidence intervals. *** p

    Article Snippet: The air and dust samples were analyzed for endotoxin and (1–3)-β-D-glucan using the Limulus Amebocyte Lysate assay; Pyrochrome for endotoxin and Glucatell for (1–3)-β-D-glucan (LAL; Associates of Cape Cod Inc, Falmouth, MA) as described earlier ( ; ).

    Techniques:

    Dust borne endotoxin, dust borne (1–3)-β-D-glucan, ERMI, airborne endotoxin, airborne (1–3)-β-D-glucan, and airborne fungal spores in homes divided into with two levels of moldy odor: with (n=25) and without moldy odor (n=159). Histograms show geometric means, except arithmetic mean for ERMI, and error bars show 95% confidence intervals. *** p

    Journal: The Science of the total environment

    Article Title: Visually observed mold and moldy odor versus quantitatively measured microbial exposure in homes

    doi: 10.1016/j.scitotenv.2010.07.090

    Figure Lengend Snippet: Dust borne endotoxin, dust borne (1–3)-β-D-glucan, ERMI, airborne endotoxin, airborne (1–3)-β-D-glucan, and airborne fungal spores in homes divided into with two levels of moldy odor: with (n=25) and without moldy odor (n=159). Histograms show geometric means, except arithmetic mean for ERMI, and error bars show 95% confidence intervals. *** p

    Article Snippet: The air and dust samples were analyzed for endotoxin and (1–3)-β-D-glucan using the Limulus Amebocyte Lysate assay; Pyrochrome for endotoxin and Glucatell for (1–3)-β-D-glucan (LAL; Associates of Cape Cod Inc, Falmouth, MA) as described earlier ( ; ).

    Techniques: