Structured Review

Millipore chondroitinase abc
A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, <t>chondroitinase</t> <t>ABC</t> digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated
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1) Product Images from "Mass spectrometric analysis of chondroitin sulfate-linked peptides"

Article Title: Mass spectrometric analysis of chondroitin sulfate-linked peptides

Journal: Journal of Proteins and Proteomics

doi: 10.1007/s42485-022-00092-3

A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated
Figure Legend Snippet: A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated

Techniques Used: Liquid Chromatography with Mass Spectroscopy

2) Product Images from "Mass spectrometric analysis of chondroitin sulfate-linked peptides"

Article Title: Mass spectrometric analysis of chondroitin sulfate-linked peptides

Journal: Journal of Proteins and Proteomics

doi: 10.1007/s42485-022-00092-3

A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated
Figure Legend Snippet: A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated

Techniques Used: Liquid Chromatography with Mass Spectroscopy

3) Product Images from "Temporal enzymatic treatment to enhance the remodelling of multiple cartilage microtissues into a structurally organised tissue"

Article Title: Temporal enzymatic treatment to enhance the remodelling of multiple cartilage microtissues into a structurally organised tissue

Journal: bioRxiv

doi: 10.1101/2022.09.07.506986

Study Schematic. Two different cellular self-organisation strategies are employed in this study. The first involves the self-organisation of 3 × 10 6 bMSCs within a non-adherent hydrogel well. The second uses 1 × 10 3 early-cartilage microtissues, each containing 3 × 10 3 MSCs, as biological building blocks. A study timeline is also provided that indicates the weekly endpoints used to map tissue maturation. In one arm of the study, a 4 hour chondroitinase-ABC (cABC) treatment was undertaken on day 14. Finally, a schematic representation of the analytical techniques employed to determine the quality of the self-organised cartilages generated within this study is provided. Collectively, this work aims to provide a comprehensive timeline for tissue growth and maturation of self-organised cartilages, as well as determining the effect enzymatic treatment has on the quality of cartilage macrotissues bioassembled using single cells and cartilage microtissues as biological building blocks.
Figure Legend Snippet: Study Schematic. Two different cellular self-organisation strategies are employed in this study. The first involves the self-organisation of 3 × 10 6 bMSCs within a non-adherent hydrogel well. The second uses 1 × 10 3 early-cartilage microtissues, each containing 3 × 10 3 MSCs, as biological building blocks. A study timeline is also provided that indicates the weekly endpoints used to map tissue maturation. In one arm of the study, a 4 hour chondroitinase-ABC (cABC) treatment was undertaken on day 14. Finally, a schematic representation of the analytical techniques employed to determine the quality of the self-organised cartilages generated within this study is provided. Collectively, this work aims to provide a comprehensive timeline for tissue growth and maturation of self-organised cartilages, as well as determining the effect enzymatic treatment has on the quality of cartilage macrotissues bioassembled using single cells and cartilage microtissues as biological building blocks.

Techniques Used: Generated

4) Product Images from "Radiation induces ESCRT pathway dependent CD44v3+ extracellular vesicle production stimulating pro-tumor fibroblast activity in breast cancer"

Article Title: Radiation induces ESCRT pathway dependent CD44v3+ extracellular vesicle production stimulating pro-tumor fibroblast activity in breast cancer

Journal: Frontiers in Oncology

doi: 10.3389/fonc.2022.913656

Radiation stimulates vesicular CD44v3 expression. (A, B) tEVs from breast cancer cells were assessed for CD44v3 (A) and HS (B) expression via flow cytometry. Control represents unbound beads incubated with antibody cocktail. (C) tEVs from MDA-MB-231 cells were treated overnight with either heparanase, chondroitinase ABC, or both. Gag levels were assessed via blyscan assay. Data points represent technical replicates. (D) MRC5 were incubated with tEVs collected from WT or CD44 KO MDA-MB-231. IL-6 levels were measured via ELISA. (E) MDA-MB-231 were exposed to fresh media containing FCM described in (D) and radioresistance was assessed via clonogenic assay. X axis indicates which fibroblast CM from (D) was used in the incubation. Statistical significance for (A-E) assessed with ANOVA * = P
Figure Legend Snippet: Radiation stimulates vesicular CD44v3 expression. (A, B) tEVs from breast cancer cells were assessed for CD44v3 (A) and HS (B) expression via flow cytometry. Control represents unbound beads incubated with antibody cocktail. (C) tEVs from MDA-MB-231 cells were treated overnight with either heparanase, chondroitinase ABC, or both. Gag levels were assessed via blyscan assay. Data points represent technical replicates. (D) MRC5 were incubated with tEVs collected from WT or CD44 KO MDA-MB-231. IL-6 levels were measured via ELISA. (E) MDA-MB-231 were exposed to fresh media containing FCM described in (D) and radioresistance was assessed via clonogenic assay. X axis indicates which fibroblast CM from (D) was used in the incubation. Statistical significance for (A-E) assessed with ANOVA * = P

Techniques Used: Expressing, Flow Cytometry, Incubation, Multiple Displacement Amplification, Enzyme-linked Immunosorbent Assay, Clonogenic Assay

5) Product Images from "The aberrant cancer metabolic gene carbohydrate sulfotransferase 11 promotes non-small cell lung cancer cell metastasis via dysregulation of ceruloplasmin and intracellular iron balance"

Article Title: The aberrant cancer metabolic gene carbohydrate sulfotransferase 11 promotes non-small cell lung cancer cell metastasis via dysregulation of ceruloplasmin and intracellular iron balance

Journal: Translational Oncology

doi: 10.1016/j.tranon.2022.101508

EMT promotes GAG biosynthesis pathway activation and NSCLC cancer progression. (A–C) CDH1 reporter assay (A), western blotting of proteins involved in GAG biosynthesis pathway (B), and sulfotransferase activity assay (C) in TGF-β-induced NSCLC EMT models. (D) Boyden chamber migration ( left ) and invasion ( right ) abilities of A549 cells with or without TGF-β or chondroitinase ABC (Chase) treatment. CT, control. (E,F) The metastatic potential induced by the constitutive activation of TGF-β receptor I (TGFBR1-T204D) expression in A549 (E) and NCI-H358 cells (F). The left panel is the migration ability, and the right panel is the invasion ability. VC, vector control. (G) NSG xenograft lung pictures of A549 cells with or without TGFBR1-T204D expression. Each square indicates 0.5 cm 2 . (H,I) Hematoxylin and eosin (H), and Alcian blue (pH 1.0) (I) staining results from (G). In A and C to F, the data represent mean ± SEM derived from three independent experiments. * p
Figure Legend Snippet: EMT promotes GAG biosynthesis pathway activation and NSCLC cancer progression. (A–C) CDH1 reporter assay (A), western blotting of proteins involved in GAG biosynthesis pathway (B), and sulfotransferase activity assay (C) in TGF-β-induced NSCLC EMT models. (D) Boyden chamber migration ( left ) and invasion ( right ) abilities of A549 cells with or without TGF-β or chondroitinase ABC (Chase) treatment. CT, control. (E,F) The metastatic potential induced by the constitutive activation of TGF-β receptor I (TGFBR1-T204D) expression in A549 (E) and NCI-H358 cells (F). The left panel is the migration ability, and the right panel is the invasion ability. VC, vector control. (G) NSG xenograft lung pictures of A549 cells with or without TGFBR1-T204D expression. Each square indicates 0.5 cm 2 . (H,I) Hematoxylin and eosin (H), and Alcian blue (pH 1.0) (I) staining results from (G). In A and C to F, the data represent mean ± SEM derived from three independent experiments. * p

Techniques Used: Activation Assay, Reporter Assay, Western Blot, Activity Assay, Migration, Expressing, Plasmid Preparation, Staining, Derivative Assay

CHST11 promotes EMT and metastasis potential in NSCLC cells. (A–C) Sulfotransferase activity (A), CDH1 reporter activity (B), and SMAD4 reporter activity assays of NSCLC cells with or without ectopic CHST11 expression. VC, vector control. (D,E) qRT-PCR (D) and western blotting (E) of CHST11 and EMT markers in A549 cells with or without ectopic CHST11 expression. (F–H) Boyden chamber migration ( left ) and invasion ( right ) abilities of NCI-H358 cells with or without CHST11 expression (F), A549 cells with wild-type CHST11 or enzyme-inactivated clone (CHST11mt) (G), or chondroitinase ABC (Chase) treatment (H). (I) NSG xenograft lung images of A549 cells with or without CHST11 expression. Each square indicates 0.5 cm 2 . (J,K) Hematoxylin and eosin (J) and Alcian blue (pH 1.0) (K) staining results from (I). Data represent mean ± SEM derived from three independent experiments. * p
Figure Legend Snippet: CHST11 promotes EMT and metastasis potential in NSCLC cells. (A–C) Sulfotransferase activity (A), CDH1 reporter activity (B), and SMAD4 reporter activity assays of NSCLC cells with or without ectopic CHST11 expression. VC, vector control. (D,E) qRT-PCR (D) and western blotting (E) of CHST11 and EMT markers in A549 cells with or without ectopic CHST11 expression. (F–H) Boyden chamber migration ( left ) and invasion ( right ) abilities of NCI-H358 cells with or without CHST11 expression (F), A549 cells with wild-type CHST11 or enzyme-inactivated clone (CHST11mt) (G), or chondroitinase ABC (Chase) treatment (H). (I) NSG xenograft lung images of A549 cells with or without CHST11 expression. Each square indicates 0.5 cm 2 . (J,K) Hematoxylin and eosin (J) and Alcian blue (pH 1.0) (K) staining results from (I). Data represent mean ± SEM derived from three independent experiments. * p

Techniques Used: Activity Assay, Expressing, Plasmid Preparation, Quantitative RT-PCR, Western Blot, Migration, Staining, Derivative Assay

6) Product Images from "TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis"

Article Title: TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis

Journal: Journal of Clinical Medicine

doi: 10.3390/jcm11144213

Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.
Figure Legend Snippet: Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.

Techniques Used: Isolation, Electrophoresis

7) Product Images from "TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis"

Article Title: TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis

Journal: Journal of Clinical Medicine

doi: 10.3390/jcm11144213

Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.
Figure Legend Snippet: Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.

Techniques Used: Isolation, Electrophoresis

8) Product Images from "TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis"

Article Title: TNF-α Inhibitors in Combination with MTX Reduce Circulating Levels of Heparan Sulfate/Heparin and Endothelial Dysfunction Biomarkers (sVCAM-1, MCP-1, MMP-9 and ADMA) in Women with Rheumatoid Arthritis

Journal: Journal of Clinical Medicine

doi: 10.3390/jcm11144213

Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.
Figure Legend Snippet: Typical electrophoretic patterns of plasma sulfated glycosaminoglycans (sGAGs) in healthy subjects ( a ) and patients with rheumatoid arthritis (RA) before ( b ) and after 3 ( c ), 9 ( d ) and 15 ( e ) months of anti-TNF-α therapy. GAGs were isolated from plasma samples and submitted to electrophoresis on cellulose acetate in 0.034 M Al 2 (SO 4 ) 3 before and after specific enzymatic degradation. Lane 1, untreated GAG sample (CS/DS, HS/H); lane 2, GAG sample resistant to the action of chondroitinase ABC (HS/H); lane 3, material resistant to the combined action of chondroitinase ABC and heparinase I and III. Comparison of electrophoretic patterns of intact material containing CS/DS and HS/H (line 1) with those obtained after chondroitinase ABC digestion (line 2) allowed to localize CS/DS in electrophoregrams (line 1–line 2 = CS/DS). Material resistant to chondroitinase ABC but susceptible to heparinase I and III digestion was identified as HS/H (line 2–line 3 = HS/H). CS/DS, chondroitin/dermatan sulfate; sGAGs, sulfated glycosaminoglycans; HS/H, heparan sulfate/heparin; RA, rheumatoid arthritis; anti-TNF-α, anti-tumor necrosis factor-α.

Techniques Used: Isolation, Electrophoresis

9) Product Images from "Enzymatic Production of Chondroitin Oligosaccharides and Its Sulfate Derivatives"

Article Title: Enzymatic Production of Chondroitin Oligosaccharides and Its Sulfate Derivatives

Journal: Frontiers in Bioengineering and Biotechnology

doi: 10.3389/fbioe.2022.951740

Chondroitinase ABC I depolymerizes chondroitin chain by breaking the β-1,4 glycoside bond.
Figure Legend Snippet: Chondroitinase ABC I depolymerizes chondroitin chain by breaking the β-1,4 glycoside bond.

Techniques Used:

10) Product Images from "Sex-specific regulation of inhibition and network activity by local aromatase in the mouse hippocampus"

Article Title: Sex-specific regulation of inhibition and network activity by local aromatase in the mouse hippocampus

Journal: Nature Communications

doi: 10.1038/s41467-022-31635-3

PNNs are required for extragonadal aromatase regulation of CA1 synaptic inhibition. A Adult intact female mice received daily intraperitoneal (i.p.) injections of aromatase blocker letrozole (LTZ, Arom Block). After 5 days of treatment, perineuronal nets (PNNs) were evaluated quantifying WFA staining intensity. B Representative images showing WFA staining of PNNs (green) surrounding CA1 parvalbumin PV-INs (red) of vehicle (Control) and aromatase blocker letrozole (Arom Block) treated female mice. Scale bar: 20 μm. Graph shows frequency distribution analysis of WFA staining intensities around PV-INs, arbitrary units (arb. units). Aromatase blockade increases WFA staining intensity around female CA1 PV-IN. Two-way ANOVA, Treatment F (1, 12) = 14.88, p = 0.0023; n = 6, 8 mice. C Adult female mice received a single intrahippocampal injection of Chondroitinase ABC (ChABC) or vehicle (Sham) 14 days after ovariectomy (OVX). On the same day of the ChABC or vehicle intracerebral injection, mice received the first intraperitoneal (i.p.) daily injection of aromatase blocker letrozole (Arom Block) or vehicle (C). After 5 days of treatment, CA1 PYR neuron spontaneous Inhibitory Post-Synaptic Currents (sIPSCs) frequency and amplitude were determined. D ChABC treatment prevented the increase of sIPSCs frequency caused by Aromatase blockade (Left graph). Two-way ANOVA, Treatment Arom block F (1, 60) = 8.432, p = 0.0052; treatment ChABC, F (1, 60) = 3.715 × 10 −7 , p = 0.9995. Bonferroni’s comparison tests, C vs. Arom Block (Sham) p = 0.0045, C vs. Arom Block (ChABC) p > 0,99. No significant changes were observed in sIPSCs amplitude (right graph). Two-way ANOVA, Treatment Arom block F (1, 60) = 0.72, p = 0.4; treatment ChABC, F (1, 60) = 2.78, p = 0.1. Bonferroni’s comparison tests, C-Arom Block (Sham) p = 0.22, C-Arom Block (ChABC) p = 0.97; n = 11, 13, 19, 21 cells from 3 mice per group. Graphs represent mean ± SEM (symbols and bars) and individual values (gray circles). * p
Figure Legend Snippet: PNNs are required for extragonadal aromatase regulation of CA1 synaptic inhibition. A Adult intact female mice received daily intraperitoneal (i.p.) injections of aromatase blocker letrozole (LTZ, Arom Block). After 5 days of treatment, perineuronal nets (PNNs) were evaluated quantifying WFA staining intensity. B Representative images showing WFA staining of PNNs (green) surrounding CA1 parvalbumin PV-INs (red) of vehicle (Control) and aromatase blocker letrozole (Arom Block) treated female mice. Scale bar: 20 μm. Graph shows frequency distribution analysis of WFA staining intensities around PV-INs, arbitrary units (arb. units). Aromatase blockade increases WFA staining intensity around female CA1 PV-IN. Two-way ANOVA, Treatment F (1, 12) = 14.88, p = 0.0023; n = 6, 8 mice. C Adult female mice received a single intrahippocampal injection of Chondroitinase ABC (ChABC) or vehicle (Sham) 14 days after ovariectomy (OVX). On the same day of the ChABC or vehicle intracerebral injection, mice received the first intraperitoneal (i.p.) daily injection of aromatase blocker letrozole (Arom Block) or vehicle (C). After 5 days of treatment, CA1 PYR neuron spontaneous Inhibitory Post-Synaptic Currents (sIPSCs) frequency and amplitude were determined. D ChABC treatment prevented the increase of sIPSCs frequency caused by Aromatase blockade (Left graph). Two-way ANOVA, Treatment Arom block F (1, 60) = 8.432, p = 0.0052; treatment ChABC, F (1, 60) = 3.715 × 10 −7 , p = 0.9995. Bonferroni’s comparison tests, C vs. Arom Block (Sham) p = 0.0045, C vs. Arom Block (ChABC) p > 0,99. No significant changes were observed in sIPSCs amplitude (right graph). Two-way ANOVA, Treatment Arom block F (1, 60) = 0.72, p = 0.4; treatment ChABC, F (1, 60) = 2.78, p = 0.1. Bonferroni’s comparison tests, C-Arom Block (Sham) p = 0.22, C-Arom Block (ChABC) p = 0.97; n = 11, 13, 19, 21 cells from 3 mice per group. Graphs represent mean ± SEM (symbols and bars) and individual values (gray circles). * p

Techniques Used: Inhibition, Mouse Assay, Blocking Assay, Staining, Injection

11) Product Images from "Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices"

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

Journal: bioRxiv

doi: 10.1101/2022.03.27.485990

Versican interacts with collagen via its G3 domain. A) Plates were coated with versican (Ver, red) or the V3 isoform (V3, blue) at 0.05, 0.1, 0.25, 0.5 and 1 μg/ml. The absorbance of collagen, added at 2.5 μg/ml and detected via a biotin-conjugated antibody, was measured colorimetrically. B) Plates were coated with 0.25 μg/ml versican (red), V3 (blue) or versican after chondroitinase ABC digestion (Ver-ChABC, orange). The binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was assayed. C) Plates were coated with 0.25 μg/ml recombinant G1 (teal) or G3 (pink) and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was assayed. D) Plates were coated with 0.25 μg/ml versican (red), V3 (blue), decorin (Dec, green), lumican (Lum, orange dash line) or aggrecan (Agg, purple) and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was measured. E) Plates were coated with 0.25 μg/ml V3 to which was added collagen (1 μg/ml) mixed with increasing concentrations of HA (0.1, 0.5, 1, 5 and 10 ng/ml). F) Plates were coated with 0.25 μg/ml V3 to which was added HA (10 mg/ml) mixed with increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml). Three independent experiments were carried out for each condition; each line in an individual graph is from the same trio of experiments. Data represent mean ± SD.
Figure Legend Snippet: Versican interacts with collagen via its G3 domain. A) Plates were coated with versican (Ver, red) or the V3 isoform (V3, blue) at 0.05, 0.1, 0.25, 0.5 and 1 μg/ml. The absorbance of collagen, added at 2.5 μg/ml and detected via a biotin-conjugated antibody, was measured colorimetrically. B) Plates were coated with 0.25 μg/ml versican (red), V3 (blue) or versican after chondroitinase ABC digestion (Ver-ChABC, orange). The binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was assayed. C) Plates were coated with 0.25 μg/ml recombinant G1 (teal) or G3 (pink) and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was assayed. D) Plates were coated with 0.25 μg/ml versican (red), V3 (blue), decorin (Dec, green), lumican (Lum, orange dash line) or aggrecan (Agg, purple) and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml) was measured. E) Plates were coated with 0.25 μg/ml V3 to which was added collagen (1 μg/ml) mixed with increasing concentrations of HA (0.1, 0.5, 1, 5 and 10 ng/ml). F) Plates were coated with 0.25 μg/ml V3 to which was added HA (10 mg/ml) mixed with increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5 and 5 μg/ml). Three independent experiments were carried out for each condition; each line in an individual graph is from the same trio of experiments. Data represent mean ± SD.

Techniques Used: Binding Assay, Recombinant

ADAMTS-5 and chondroitinase ABC treatment of rat livers alters compression stiffening behavior. A) Sulfated GAG quantification after perfusion with either enzyme. B) Representative confocal imaging of immunostaining using an antibody against DPEAAE, the epitope exposed by ADAMTS-5 cleavage of versican. DPEAAE (green), DAPI (blue). C) G’ was measured under 0%, 10%, 15%, 20% and 25% compression (with HBSS perfusion as a control). There is a significant difference at 25% compression. D) Young’s modulus ( E ) was calculated from normal force and gap changes and plotted at 5%, 12.5%, 17.5% and 22.5% compression (significance shown for 22.5% compression). E) G’ measured at increasing strain from 1% to 50%. N=3 for HBSS, N=4 for ADAMTS-5 and for ChABC perfused livers. Data did not show statistical differences. Compression and strain sweep experiments were done on the same liver samples, as was the assay for sulfated GAGs (A). Scale bar = 200 μm. Data represent mean ± SD; A was analyzed using one-way ANOVA, C, D, and E using two-way ANOVA with repeated measurements; *P
Figure Legend Snippet: ADAMTS-5 and chondroitinase ABC treatment of rat livers alters compression stiffening behavior. A) Sulfated GAG quantification after perfusion with either enzyme. B) Representative confocal imaging of immunostaining using an antibody against DPEAAE, the epitope exposed by ADAMTS-5 cleavage of versican. DPEAAE (green), DAPI (blue). C) G’ was measured under 0%, 10%, 15%, 20% and 25% compression (with HBSS perfusion as a control). There is a significant difference at 25% compression. D) Young’s modulus ( E ) was calculated from normal force and gap changes and plotted at 5%, 12.5%, 17.5% and 22.5% compression (significance shown for 22.5% compression). E) G’ measured at increasing strain from 1% to 50%. N=3 for HBSS, N=4 for ADAMTS-5 and for ChABC perfused livers. Data did not show statistical differences. Compression and strain sweep experiments were done on the same liver samples, as was the assay for sulfated GAGs (A). Scale bar = 200 μm. Data represent mean ± SD; A was analyzed using one-way ANOVA, C, D, and E using two-way ANOVA with repeated measurements; *P

Techniques Used: Imaging, Immunostaining

12) Product Images from "Bacteria associated with acne use glycosaminoglycans as cell adhesion receptors and promote changes in the expression of the genes involved in their biosynthesis"

Article Title: Bacteria associated with acne use glycosaminoglycans as cell adhesion receptors and promote changes in the expression of the genes involved in their biosynthesis

Journal: BMC Microbiology

doi: 10.1186/s12866-022-02477-2

Effect of enzymatic degradation of cell GAGs on bacterial adherence to skin cells. Inhibition of bacterial attachment to ( a ) keratinocytes and ( b ) fibroblasts treated with heparinases I and III (grey bars) or chondroitinase ABC (white bars). Data were normalized using the adhesion values of bacteria to non-treated cells, which was given the arbitrary value of 1. The spreads represent the standard deviations
Figure Legend Snippet: Effect of enzymatic degradation of cell GAGs on bacterial adherence to skin cells. Inhibition of bacterial attachment to ( a ) keratinocytes and ( b ) fibroblasts treated with heparinases I and III (grey bars) or chondroitinase ABC (white bars). Data were normalized using the adhesion values of bacteria to non-treated cells, which was given the arbitrary value of 1. The spreads represent the standard deviations

Techniques Used: Inhibition

13) Product Images from "Aberrant Gamma-Band Oscillations in Mice with Vitamin D Deficiency: Implications on Schizophrenia and its Cognitive Symptoms"

Article Title: Aberrant Gamma-Band Oscillations in Mice with Vitamin D Deficiency: Implications on Schizophrenia and its Cognitive Symptoms

Journal: Journal of Personalized Medicine

doi: 10.3390/jpm12020318

Scheme of the experimental schedules and the various methods for measuring frontal gamma-band oscillations (GBO). ( A ) Experimental timeline of the vitamin D-deficient diet group vs. normal diet group (VDD vs. ND, top) and the chondroitinase ABC-injected group vs. vehicle-injected group (ChABC vs. vehicle, bottom). ( B) Stimulation protocol for 40 Hz optogenetically-evoked GBO. One trial was composed of pre-stimulation, stimulation, and post-stimulation (0.5 s each). During stimulation, a pulse occurs every 25 ms, and each pulse had a duration of 10 ms. A total of 200 trains were averaged and used for the power spectrum analysis. ( C ) Stimulation protocol for 40 Hz auditory-evoked GBO. The same protocol as for the optogenetically-evoked GBO was followed, except that each pulse had a duration of 5 ms. The sound was delivered with a sound pressure of 90 dB. ( D ) Stimulation protocol for the prepulse inhibition test. One train composed of two pulses (S1, S2) and 100 trains were averaged and used for power spectrum analysis. Each pulse continued for 50 ms, and a 5 kHz sound was delivered with 90 dB (6 s inter-trial interval, ITI; 250 ms inter-pulse interval, IPI).
Figure Legend Snippet: Scheme of the experimental schedules and the various methods for measuring frontal gamma-band oscillations (GBO). ( A ) Experimental timeline of the vitamin D-deficient diet group vs. normal diet group (VDD vs. ND, top) and the chondroitinase ABC-injected group vs. vehicle-injected group (ChABC vs. vehicle, bottom). ( B) Stimulation protocol for 40 Hz optogenetically-evoked GBO. One trial was composed of pre-stimulation, stimulation, and post-stimulation (0.5 s each). During stimulation, a pulse occurs every 25 ms, and each pulse had a duration of 10 ms. A total of 200 trains were averaged and used for the power spectrum analysis. ( C ) Stimulation protocol for 40 Hz auditory-evoked GBO. The same protocol as for the optogenetically-evoked GBO was followed, except that each pulse had a duration of 5 ms. The sound was delivered with a sound pressure of 90 dB. ( D ) Stimulation protocol for the prepulse inhibition test. One train composed of two pulses (S1, S2) and 100 trains were averaged and used for power spectrum analysis. Each pulse continued for 50 ms, and a 5 kHz sound was delivered with 90 dB (6 s inter-trial interval, ITI; 250 ms inter-pulse interval, IPI).

Techniques Used: Injection, Inhibition

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    Millipore chondroitinase abc
    Chondroitinase Abc, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chondroitinase abc/product/Millipore
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    92
    Millipore chondroitinase abc from proteusvulgaris
    A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, <t>chondroitinase</t> <t>ABC</t> digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated
    Chondroitinase Abc From Proteusvulgaris, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chondroitinase abc from proteusvulgaris/product/Millipore
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chondroitinase abc from proteusvulgaris - by Bioz Stars, 2022-11
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    A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated

    Journal: Journal of Proteins and Proteomics

    Article Title: Mass spectrometric analysis of chondroitin sulfate-linked peptides

    doi: 10.1007/s42485-022-00092-3

    Figure Lengend Snippet: A schematic showing the workflow for enrichment and analysis of intact GAG-linked glycopeptides. The schematic depicts stepwise processing of indicated samples by trypsin digestion, intact glycopeptide enrichment, chondroitinase ABC digestion and LC–MS/MS analysis. Two different enrichment strategies were employed for plasma and urine samples as shown—ultrafiltration (10 kDa MWCO) and strong anion exchange (SAX) for enriching intact chondroitin sulfate (CS) chains attached to tryptic peptides. For fibroblast samples, SAX was employed for enriching the CS-linked peptides. The CS chains obtained from all sample types were digested by chondroitinase ABC enzyme mixture to yield glycopeptides with linker oligosaccharide attached to peptide backbones as indicated

    Article Snippet: Chondroitinase ABC (EC 4.2.2.20) (C3667, Sigma Aldrich) was reconstituted with digestion buffer (100 mM Tris–HCl, 50 mM NaCl, 10 mM MgCl2 , 60 mM sodium acetate, pH 8.0).

    Techniques: Liquid Chromatography with Mass Spectroscopy