α2 3 specific neuraminidase  (New England Biolabs)


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    Name:
    alpha 2 3 Neuraminidase S
    Description:
    alpha 2 3 Neuraminidase S 2 000 units
    Catalog Number:
    P0743L
    Price:
    276
    Category:
    Glycosidases
    Size:
    2 000 units
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    Structured Review

    New England Biolabs α2 3 specific neuraminidase
    alpha 2 3 Neuraminidase S
    alpha 2 3 Neuraminidase S 2 000 units
    https://www.bioz.com/result/α2 3 specific neuraminidase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α2 3 specific neuraminidase - by Bioz Stars, 2021-09
    95/100 stars

    Images

    1) Product Images from "Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma"

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    Journal: Frontiers in Oncology

    doi: 10.3389/fonc.2018.00070

    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.
    Figure Legend Snippet: N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Techniques Used:

    Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).
    Figure Legend Snippet: Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Techniques Used: Nucleic Acid Electrophoresis, Fluorescence

    2) Product Images from "The human milk oligosaccharide disialyllacto-N-tetraose prevents necrotising enterocolitis in neonatal rats"

    Article Title: The human milk oligosaccharide disialyllacto-N-tetraose prevents necrotising enterocolitis in neonatal rats

    Journal: Gut

    doi: 10.1136/gutjnl-2011-301404

    The necrotising enterocolitis-protective human milk oligosaccharide (HMO) is disialyllacto-N-tetraose (DSLNT). (A) Linkage specific neuraminidase treatment shows the presence of one α2–3- and one α2–6-linked N-acetyl-neuraminic
    Figure Legend Snippet: The necrotising enterocolitis-protective human milk oligosaccharide (HMO) is disialyllacto-N-tetraose (DSLNT). (A) Linkage specific neuraminidase treatment shows the presence of one α2–3- and one α2–6-linked N-acetyl-neuraminic

    Techniques Used:

    3) Product Images from "Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma"

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    Journal: Frontiers in Oncology

    doi: 10.3389/fonc.2018.00070

    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.
    Figure Legend Snippet: N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Techniques Used:

    Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).
    Figure Legend Snippet: Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Techniques Used: Nucleic Acid Electrophoresis, Fluorescence

    Related Articles

    Modification:

    Article Title: Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
    Article Snippet: .. Removal of sialic acid modification on NCAM1Soluble or membrane fraction of HC and OB from BACE1+/+ and BACE1−/− mice was incubated with or without the α2-3,6,8,9 Neuraminidase A (Sialidase; P0722; New England Biolabs) in a reaction solution, which is provided by the manufacturer, to remove the sialic acid from NCAM1 proteins at 37 °C overnight. ..

    Mouse Assay:

    Article Title: Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
    Article Snippet: .. Removal of sialic acid modification on NCAM1Soluble or membrane fraction of HC and OB from BACE1+/+ and BACE1−/− mice was incubated with or without the α2-3,6,8,9 Neuraminidase A (Sialidase; P0722; New England Biolabs) in a reaction solution, which is provided by the manufacturer, to remove the sialic acid from NCAM1 proteins at 37 °C overnight. ..

    Incubation:

    Article Title: Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
    Article Snippet: .. Removal of sialic acid modification on NCAM1Soluble or membrane fraction of HC and OB from BACE1+/+ and BACE1−/− mice was incubated with or without the α2-3,6,8,9 Neuraminidase A (Sialidase; P0722; New England Biolabs) in a reaction solution, which is provided by the manufacturer, to remove the sialic acid from NCAM1 proteins at 37 °C overnight. ..

    Article Title: The Small t Antigen of JC Virus Antagonizes RIG-I-Mediated Innate Immunity by Inhibiting TRIM25’s RNA Binding Ability
    Article Snippet: .. Twenty-five units of Benzonase nuclease (Sigma)/ml and 20 U/ml of α2-3,6,8 neuraminidase (New England BioLabs) were added to the cell suspension and incubated overnight in a water bath at 37°C. ..

    Article Title: Measuring Site-specific Glycosylation Similarity between Influenza a Virus Variants with Statistical Certainty
    Article Snippet: .. Before HILIC enrichment, the digested AGP glycopeptides were incubated with 200 units of α2-3,6,8 Neuraminidase (New England Biolabs # P0720S) for every 20 μg of glycoprotein overnight at 37°C. ..

    Article Title: Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
    Article Snippet: .. After washing the beads with PBS, the beads were incubated with or without the α2-3,6,8,9 Neuraminidase A (Sialidase; P0722; New England Biolabs) in a reaction solution, which is provided by the manufacturer, to remove sialic acid from purified NCAM1 proteins at 37 °C overnight. ..

    Hydrophilic Interaction Liquid Chromatography:

    Article Title: Measuring Site-specific Glycosylation Similarity between Influenza a Virus Variants with Statistical Certainty
    Article Snippet: .. Before HILIC enrichment, the digested AGP glycopeptides were incubated with 200 units of α2-3,6,8 Neuraminidase (New England Biolabs # P0720S) for every 20 μg of glycoprotein overnight at 37°C. ..

    Purification:

    Article Title: Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
    Article Snippet: .. After washing the beads with PBS, the beads were incubated with or without the α2-3,6,8,9 Neuraminidase A (Sialidase; P0722; New England Biolabs) in a reaction solution, which is provided by the manufacturer, to remove sialic acid from purified NCAM1 proteins at 37 °C overnight. ..

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  • 95
    New England Biolabs α2 3 specific neuraminidase
    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with <t>α2-3</t> linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.
    α2 3 Specific Neuraminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α2 3 specific neuraminidase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α2 3 specific neuraminidase - by Bioz Stars, 2021-09
    95/100 stars
      Buy from Supplier

    94
    New England Biolabs alpha 2 3 6 8 9 neuraminidase a
    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with <t>α2-3</t> linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.
    Alpha 2 3 6 8 9 Neuraminidase A, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alpha 2 3 6 8 9 neuraminidase a/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    alpha 2 3 6 8 9 neuraminidase a - by Bioz Stars, 2021-09
    94/100 stars
      Buy from Supplier

    Image Search Results


    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Article Snippet: The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques:

    Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Article Snippet: The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques: Nucleic Acid Electrophoresis, Fluorescence

    The necrotising enterocolitis-protective human milk oligosaccharide (HMO) is disialyllacto-N-tetraose (DSLNT). (A) Linkage specific neuraminidase treatment shows the presence of one α2–3- and one α2–6-linked N-acetyl-neuraminic

    Journal: Gut

    Article Title: The human milk oligosaccharide disialyllacto-N-tetraose prevents necrotising enterocolitis in neonatal rats

    doi: 10.1136/gutjnl-2011-301404

    Figure Lengend Snippet: The necrotising enterocolitis-protective human milk oligosaccharide (HMO) is disialyllacto-N-tetraose (DSLNT). (A) Linkage specific neuraminidase treatment shows the presence of one α2–3- and one α2–6-linked N-acetyl-neuraminic

    Article Snippet: Linkage promiscuous neuraminidase (α2–3 > 6,8,9; Arthrobacter ureafaciens ) was purchased from Sigma Aldrich (St Louis, Missouri, USA); α2–3-specific neuraminidase ( Salmonella typhimurium ), β1–3 galactosidase ( Xanthomonas manihotis ), β1–4 galactosidase ( Bacteroides fragilis ) and β-N-acetyl-glucosaminidase (GlcNAcase, X manihotis ) were obtained from New England Biolabs (Ipswich, Massachusetts, USA).

    Techniques:

    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Article Snippet: Neuraminidase Digest for PGC-LC ESI-MS/MS Analysis The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques:

    Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Article Snippet: Neuraminidase Digest for PGC-LC ESI-MS/MS Analysis The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques: Nucleic Acid Electrophoresis, Fluorescence