anti p enos abcam uk 1 1000  (Danaher Inc)


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    Danaher Inc anti p enos abcam uk 1 1000
    Anti P Enos Abcam Uk 1 1000, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti enos abcam uk 1 1000  (Danaher Inc)


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    Danaher Inc anti enos abcam uk 1 1000
    Anti Enos Abcam Uk 1 1000, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti eno1  (Danaher Inc)


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    Danaher Inc anti eno1
    <t>ENO1</t> shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant
    Anti Eno1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression"

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    Journal: Cell & Bioscience

    doi: 10.1186/s13578-024-01249-x

    ENO1 shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant
    Figure Legend Snippet: ENO1 shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot, Comparison

    ENO1 localisation is altered across MCF10 TNBC cell lines. (A) Typical CLSM images of the indicated MCF10 tumour progression cell lines, fixed and stained using an anti-ENO1 antibody (green) and DAPI to indicate nuclei (blue). (B) Digital images such as those shown in (A) were analysed to determine the nuclear to cytoplasmic fluorescence ratio (Fn/c) (where a ratio below 1 indicates cytoplasmic localisation and above 1 indicates nuclear localisation). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Typical CLSM images of the indicated cell lines, transfected to express GFP-ENO1 and imaged live 18–24 h post-transfection. (D) Digital images such as those shown in (C) were analyses to determine the Fn/c as per (B). Results represent mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments. * p < 0.05, ** p < 0.01, *** p < 0.001 relative to MCF10A, ns – non-significant
    Figure Legend Snippet: ENO1 localisation is altered across MCF10 TNBC cell lines. (A) Typical CLSM images of the indicated MCF10 tumour progression cell lines, fixed and stained using an anti-ENO1 antibody (green) and DAPI to indicate nuclei (blue). (B) Digital images such as those shown in (A) were analysed to determine the nuclear to cytoplasmic fluorescence ratio (Fn/c) (where a ratio below 1 indicates cytoplasmic localisation and above 1 indicates nuclear localisation). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Typical CLSM images of the indicated cell lines, transfected to express GFP-ENO1 and imaged live 18–24 h post-transfection. (D) Digital images such as those shown in (C) were analyses to determine the Fn/c as per (B). Results represent mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments. * p < 0.05, ** p < 0.01, *** p < 0.001 relative to MCF10A, ns – non-significant

    Techniques Used: Staining, Fluorescence, Transfection

    ENO1 is phosphorylated at S419 in breast cancer patient samples (A) Data used in this figure was publicly available data generated as stated by the Clinical Proteomic Tumor Analysis Consortium (NCI/NIH). Quantitative mass-spectrometry based phosphoproteomic analyses were performed on breast tumours (125 participants). Data were generated with TMT10plex quantification, and each 10-plex experiment contained a common reference sample composed of a pooled mixture of 40 tumour samples. Data was separated into receptor positive breast cancer (ER, PR, HER2 +) and TNBC manually for the current study, based on reported therapeutic receptor expression. When ER, PR or HER2 status was not stated, samples were assigned to a non-TNBC category. The graph indicates log transformed fold change ENO1 phosphopeptide abundance relative to a pooled breast cancer control sample. (B) Western blot of GFP-ENO1 expression in MCF10A and MCF10Ca1h TNBC cell lines. GFP-trap immunoprecipitations of the indicated MCF10 cell lines were subjected to western blot and probed with anti-phospho-serine antibody. Result representative of a single typical experiment from a series of 3 independent experiments
    Figure Legend Snippet: ENO1 is phosphorylated at S419 in breast cancer patient samples (A) Data used in this figure was publicly available data generated as stated by the Clinical Proteomic Tumor Analysis Consortium (NCI/NIH). Quantitative mass-spectrometry based phosphoproteomic analyses were performed on breast tumours (125 participants). Data were generated with TMT10plex quantification, and each 10-plex experiment contained a common reference sample composed of a pooled mixture of 40 tumour samples. Data was separated into receptor positive breast cancer (ER, PR, HER2 +) and TNBC manually for the current study, based on reported therapeutic receptor expression. When ER, PR or HER2 status was not stated, samples were assigned to a non-TNBC category. The graph indicates log transformed fold change ENO1 phosphopeptide abundance relative to a pooled breast cancer control sample. (B) Western blot of GFP-ENO1 expression in MCF10A and MCF10Ca1h TNBC cell lines. GFP-trap immunoprecipitations of the indicated MCF10 cell lines were subjected to western blot and probed with anti-phospho-serine antibody. Result representative of a single typical experiment from a series of 3 independent experiments

    Techniques Used: Generated, Mass Spectrometry, Expressing, Transformation Assay, Western Blot

    Phosphomimetic point mutants of ENO1-S419 show altered nuclear transport only in MCF10Ca1h tumour cells. (A) MCF10A non-tumour and MCF10Ca1h tumour cells were transfected to express GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), then analysed by CLSM 18 h later. (B) Images such as those in (A) were analysed to determine the Fn/c ratio as per the legend to Fig. . Results represent mean Fn/c ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. ** p < 0.01 relative to GFP-ENO1, ns – non-significant. Data was not corrected for multiple comparisons
    Figure Legend Snippet: Phosphomimetic point mutants of ENO1-S419 show altered nuclear transport only in MCF10Ca1h tumour cells. (A) MCF10A non-tumour and MCF10Ca1h tumour cells were transfected to express GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), then analysed by CLSM 18 h later. (B) Images such as those in (A) were analysed to determine the Fn/c ratio as per the legend to Fig. . Results represent mean Fn/c ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. ** p < 0.01 relative to GFP-ENO1, ns – non-significant. Data was not corrected for multiple comparisons

    Techniques Used: Transfection

    Casein kinase 1 inhibition with D4476 increases ENO1 nuclear accumulation in MCF10Ca1h tumour cells only. (A) MCF10 TNBC cell lines that were treated with 125 µM casein kinase 1 inhibitor D4476 or DMSO for 3 h, then fixed and stained with anti-ENO1 antibodies and imaged by CLSM. White star indicates complete nuclear accumulation of ENO1 observed in 10% of D4476 treated MCF10Ca1h cells. Images represent single typical cells from a series of 4 independent biological replicate experiments. (B) Images such as those in (A) were analysed to determine Fn/c ratio as previous. Results represent mean ± SEM ( n > 50) of a single typical experiment from a series of 4 independent biological replicate experiments. **** p < 0.0001 compared to DMSO treated cell line, all other comparisons were nonsignificant. Data was not corrected for multiple comparisons
    Figure Legend Snippet: Casein kinase 1 inhibition with D4476 increases ENO1 nuclear accumulation in MCF10Ca1h tumour cells only. (A) MCF10 TNBC cell lines that were treated with 125 µM casein kinase 1 inhibitor D4476 or DMSO for 3 h, then fixed and stained with anti-ENO1 antibodies and imaged by CLSM. White star indicates complete nuclear accumulation of ENO1 observed in 10% of D4476 treated MCF10Ca1h cells. Images represent single typical cells from a series of 4 independent biological replicate experiments. (B) Images such as those in (A) were analysed to determine Fn/c ratio as previous. Results represent mean ± SEM ( n > 50) of a single typical experiment from a series of 4 independent biological replicate experiments. **** p < 0.0001 compared to DMSO treated cell line, all other comparisons were nonsignificant. Data was not corrected for multiple comparisons

    Techniques Used: Inhibition, Staining

    Inhibition of CRM-1 mediated nuclear export using Leptomycin B (LMB) demonstrates enhanced tumour specific nuclear export of ENO1. MCF10A non-tumour and MCF10Ca1h tumour cells were transfected with GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), treated with LMB or untreated (UT), then fixed and stained with DAPI to define nuclei (blue), and imaged by CLSM. (A) Representative CLSM images of GFP-ENO1 and S419 point mutant transfected MCF10A (left) and MCF10Ca1h (right). (B) Images such as those in (A) were analysed to determine nuclear-cytoplasmic fluorescence ratios (Fn/c). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 4 independent biological replicate experiments. * p < 0.05, ** p < 0.01, ns – non-significant
    Figure Legend Snippet: Inhibition of CRM-1 mediated nuclear export using Leptomycin B (LMB) demonstrates enhanced tumour specific nuclear export of ENO1. MCF10A non-tumour and MCF10Ca1h tumour cells were transfected with GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), treated with LMB or untreated (UT), then fixed and stained with DAPI to define nuclei (blue), and imaged by CLSM. (A) Representative CLSM images of GFP-ENO1 and S419 point mutant transfected MCF10A (left) and MCF10Ca1h (right). (B) Images such as those in (A) were analysed to determine nuclear-cytoplasmic fluorescence ratios (Fn/c). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 4 independent biological replicate experiments. * p < 0.05, ** p < 0.01, ns – non-significant

    Techniques Used: Inhibition, Transfection, Staining, Mutagenesis, Fluorescence

    Relative glycolytic activity of ENO1 is not altered by charge at residue 419, or by tumour progression in MCF10 cell lines. (A) Recombinant proteins of wild type (WT) full length ENO1 or ENO1-S419A mutant, and equal amounts of cell lysate from MCF10 TNBC cells, were incubated in ENO1 antibody coated 96-well plates, then washed and activity solution containing pyruvate kinase and lactate dehydrogenase added. ENO1 activity was measured by NADH consumption over 60 min. Data is presented relative to the activity of an active ENO1 standard (Abcam, ab89248). (B) Activity of endogenous ENO1 immunopurified from whole cell lysates of the indicated MCF10 TNBC cell lines. Results represent mean ± SEM of a single experiment with 3 biological replicates. ns – non-significant
    Figure Legend Snippet: Relative glycolytic activity of ENO1 is not altered by charge at residue 419, or by tumour progression in MCF10 cell lines. (A) Recombinant proteins of wild type (WT) full length ENO1 or ENO1-S419A mutant, and equal amounts of cell lysate from MCF10 TNBC cells, were incubated in ENO1 antibody coated 96-well plates, then washed and activity solution containing pyruvate kinase and lactate dehydrogenase added. ENO1 activity was measured by NADH consumption over 60 min. Data is presented relative to the activity of an active ENO1 standard (Abcam, ab89248). (B) Activity of endogenous ENO1 immunopurified from whole cell lysates of the indicated MCF10 TNBC cell lines. Results represent mean ± SEM of a single experiment with 3 biological replicates. ns – non-significant

    Techniques Used: Activity Assay, Residue, Recombinant, Mutagenesis, Incubation

    Inhibited phosphorylation of miniTurbo-ENO1 with CK1 inhibitor D4476 reduces ENO1 interaction with cytoskeletal proteins and increases interaction with DNA-metabolism proteins. MCF10Ca1h tumour cells were transfected with V5-miniTurbo or V5-miniTurbo-ENO1, then biotinylated by addition of exogenous biotin for 20 min to induce proximity labelling of ENO1 interacting proteins. (A) CLSM images of MCF10Ca1h cells transfected with V5-miniTurbo (left) or V5-miniTurbo-ENO1 (right), then left untreated (UT) or treated with 50 µM biotin, cells were then fixed and stained with anti-V5 antibodies (red), or FITC-streptavidin (green) and nuclei were counterstained with DAPI (blue). Images represent single typical cells from a series of 3 independent biological replicate experiments. (B) Western blot of MCF10Ca1h cell lysates expressing miniTurbo-ENO1 (mT-ENO1) that were either untreated (UT) or treated with 50 µM biotin to induce proximity labelling of other proteins interacting with mT-ENO1. (C) Volcano plot of proteins that showed differences in label free quantitation (LFQ) of expression between MCF10Ca1h cells expressing MiniTurbo-ENO1 that were D4476 treated or DMSO treated, identified by LC-MS. Results represent difference in mean LFQ intensity (D4476 treated – DMSO treated) from 3 replicates, plotted against -log transformed p-values. Red stars indicate statistically significant differences in LFQ intensity between samples with gene name listed. (D) Graphical representation of protein classes present in significantly reduced miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 10 genes. Highest percentage group was coloured red. (E) Graphical representation of protein classes present in significantly enriched miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 9 genes. Highest percentage group was coloured red. Protein classes were assigned using Panther Gene Ontology (GO) analysis online tool. LFQ intensity differences and p-values are reported for all differing proteins in Supplementary Table 1
    Figure Legend Snippet: Inhibited phosphorylation of miniTurbo-ENO1 with CK1 inhibitor D4476 reduces ENO1 interaction with cytoskeletal proteins and increases interaction with DNA-metabolism proteins. MCF10Ca1h tumour cells were transfected with V5-miniTurbo or V5-miniTurbo-ENO1, then biotinylated by addition of exogenous biotin for 20 min to induce proximity labelling of ENO1 interacting proteins. (A) CLSM images of MCF10Ca1h cells transfected with V5-miniTurbo (left) or V5-miniTurbo-ENO1 (right), then left untreated (UT) or treated with 50 µM biotin, cells were then fixed and stained with anti-V5 antibodies (red), or FITC-streptavidin (green) and nuclei were counterstained with DAPI (blue). Images represent single typical cells from a series of 3 independent biological replicate experiments. (B) Western blot of MCF10Ca1h cell lysates expressing miniTurbo-ENO1 (mT-ENO1) that were either untreated (UT) or treated with 50 µM biotin to induce proximity labelling of other proteins interacting with mT-ENO1. (C) Volcano plot of proteins that showed differences in label free quantitation (LFQ) of expression between MCF10Ca1h cells expressing MiniTurbo-ENO1 that were D4476 treated or DMSO treated, identified by LC-MS. Results represent difference in mean LFQ intensity (D4476 treated – DMSO treated) from 3 replicates, plotted against -log transformed p-values. Red stars indicate statistically significant differences in LFQ intensity between samples with gene name listed. (D) Graphical representation of protein classes present in significantly reduced miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 10 genes. Highest percentage group was coloured red. (E) Graphical representation of protein classes present in significantly enriched miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 9 genes. Highest percentage group was coloured red. Protein classes were assigned using Panther Gene Ontology (GO) analysis online tool. LFQ intensity differences and p-values are reported for all differing proteins in Supplementary Table 1

    Techniques Used: Transfection, Staining, Western Blot, Expressing, Quantitation Assay, Liquid Chromatography with Mass Spectroscopy, Transformation Assay

    Proposed model of phosphorylated ENO1’s nucleocytoplasmic transport and associated roles in non-tumour MCF10A and tumorigenic MCF10Ca1h cells. (A) Diagram of proposed model of ENO1-S419 phosphorylation-mediated regulation of tumour-specific nucleocytoplasmic transport. Upon ENO1-S419 phosphorylation we suggest that ENO1 is unable to enter the nucleus, whereas a lack of S419 phosphorylation renders ENO1 unable to be exported to the cytoplasm (left side). Our results may also suggest that phosphorylated ENO1-S419 specifically exhibits enhanced nuclear export in comparison to that observed in non-tumour cells (right side). (B) In non-tumour cells non-phosphorylated ENO1-S419 shows increased localisation in the nucleus, possibly supporting functions such as DNA-repair or transcriptional regulation. (C) In tumour cells phosphorylated ENO1-S419 is mostly excluded from the nucleus and localised in the cytoplasm, possibly supporting functions such as cytoskeletal organisation or molecular chaperoning of proteins to the cell membrane when phosphorylated. Figure created on Biorender.com
    Figure Legend Snippet: Proposed model of phosphorylated ENO1’s nucleocytoplasmic transport and associated roles in non-tumour MCF10A and tumorigenic MCF10Ca1h cells. (A) Diagram of proposed model of ENO1-S419 phosphorylation-mediated regulation of tumour-specific nucleocytoplasmic transport. Upon ENO1-S419 phosphorylation we suggest that ENO1 is unable to enter the nucleus, whereas a lack of S419 phosphorylation renders ENO1 unable to be exported to the cytoplasm (left side). Our results may also suggest that phosphorylated ENO1-S419 specifically exhibits enhanced nuclear export in comparison to that observed in non-tumour cells (right side). (B) In non-tumour cells non-phosphorylated ENO1-S419 shows increased localisation in the nucleus, possibly supporting functions such as DNA-repair or transcriptional regulation. (C) In tumour cells phosphorylated ENO1-S419 is mostly excluded from the nucleus and localised in the cytoplasm, possibly supporting functions such as cytoskeletal organisation or molecular chaperoning of proteins to the cell membrane when phosphorylated. Figure created on Biorender.com

    Techniques Used: Comparison, Membrane

    rabbit anti human eno1 igg antibody  (Danaher Inc)


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    Danaher Inc rabbit anti human eno1 igg antibody
    Reagents and tools table
    Rabbit Anti Human Eno1 Igg Antibody, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Single-cell and spatial transcriptomics reveal a high glycolysis B cell and tumor-associated macrophages cluster correlated with poor prognosis and exhausted immune microenvironment in diffuse large B-cell lymphoma"

    Article Title: Single-cell and spatial transcriptomics reveal a high glycolysis B cell and tumor-associated macrophages cluster correlated with poor prognosis and exhausted immune microenvironment in diffuse large B-cell lymphoma

    Journal: Biomarker Research

    doi: 10.1186/s40364-024-00605-w

    Reagents and tools table
    Figure Legend Snippet: Reagents and tools table

    Techniques Used: RNA Sequencing Assay, Sequencing, Expressing, Formalin-fixed Paraffin-Embedded, Immunohistochemistry, Microscopy, Immunofluorescence, Software

    Identifcation of glycolysis / gluconeogenesis maker genes in high malignant B cells. A Volcano plot of differential genes among the benign B cells, low malignant B cells, and high malignant B cells. B. Functional analysis of highly expressed genes in high malignant B cells by Metascape. C. Identification of eight commonly genes overlapped across three groups and glycolysis hallmark genes. D. Module trait correlation showed the relationships between modules, CNV score, and Glycolysis score. E. Network visualization of 10 modules of high maligant B cells.( The modules highlighted in red and underlined are modules associated with CNV score and Glycolysis score. ) F. The first 25 eigengenes of each module. G. Trajectory of different malignant B subclusters predicted by monocle. H. Genes expression level in single spot ordered along the pseudotime for MKI67 and seven glycolysis / gluconeogenesis gene markers ( STMN1, ENO1, LDHA, TPI1, CDK1, PKM , and PPIA ). ( Abbreviation : HMB: high malignant B cells; CNV: copy number variation; UMAP: uniform manifold approximation and projection. *** p < 0.001.)
    Figure Legend Snippet: Identifcation of glycolysis / gluconeogenesis maker genes in high malignant B cells. A Volcano plot of differential genes among the benign B cells, low malignant B cells, and high malignant B cells. B. Functional analysis of highly expressed genes in high malignant B cells by Metascape. C. Identification of eight commonly genes overlapped across three groups and glycolysis hallmark genes. D. Module trait correlation showed the relationships between modules, CNV score, and Glycolysis score. E. Network visualization of 10 modules of high maligant B cells.( The modules highlighted in red and underlined are modules associated with CNV score and Glycolysis score. ) F. The first 25 eigengenes of each module. G. Trajectory of different malignant B subclusters predicted by monocle. H. Genes expression level in single spot ordered along the pseudotime for MKI67 and seven glycolysis / gluconeogenesis gene markers ( STMN1, ENO1, LDHA, TPI1, CDK1, PKM , and PPIA ). ( Abbreviation : HMB: high malignant B cells; CNV: copy number variation; UMAP: uniform manifold approximation and projection. *** p < 0.001.)

    Techniques Used: Functional Assay, Expressing

    Prognostic value of four glycolysis / gluconeogenesis (STMN1, ENO1, CDK1, PKM, and PPIA) proteins in IHC cohort ( n = 34, 100X) and IFN_TAMs (CD68 + CXCL10 + PD-L1 + ) in mIF cohort ( n = 20, 10X). A-B. Kaplan–Meier curves of OS and PFS according to STMN1, CDK1, ENO1 and PKM proteins expression. C. Representative IHC staining of STMN1, CDK1, ENO1 and PKM in patient 1 (PFS = 7 months, OS = 9 months) and patient 2 (PFS = 135 months, OS = 135 months). D. Kaplan-Meier analysis for PFS based on IFN_TAMs intensity. E. Comparison of IFN_TAMs intensity in relapse and non_relapse groups. F. Correlation of IFN_TAMs’ intensity, CD8 + T cells’ intensity, and TGFβ1 intensity. G. Representative mIF staining of IFN_TAMs and CD8 + T cells in patient #1 (PFS = 2.7 months) and patient #2 (PFS = 90 months). ( Abbreviation : IHC: immunohistochemistry; IFN_TAMs: interferon-primed tumor-associated macrophages; mIF: multiple immunofluorescence; OS: overall survival; PFS: progression -free survival, Relapse: relapsed patients, patients without EFS24; Non_Relapse: non-relapsed patients, patients with EFS24. Mann-Whitney test was performed between groups.)
    Figure Legend Snippet: Prognostic value of four glycolysis / gluconeogenesis (STMN1, ENO1, CDK1, PKM, and PPIA) proteins in IHC cohort ( n = 34, 100X) and IFN_TAMs (CD68 + CXCL10 + PD-L1 + ) in mIF cohort ( n = 20, 10X). A-B. Kaplan–Meier curves of OS and PFS according to STMN1, CDK1, ENO1 and PKM proteins expression. C. Representative IHC staining of STMN1, CDK1, ENO1 and PKM in patient 1 (PFS = 7 months, OS = 9 months) and patient 2 (PFS = 135 months, OS = 135 months). D. Kaplan-Meier analysis for PFS based on IFN_TAMs intensity. E. Comparison of IFN_TAMs intensity in relapse and non_relapse groups. F. Correlation of IFN_TAMs’ intensity, CD8 + T cells’ intensity, and TGFβ1 intensity. G. Representative mIF staining of IFN_TAMs and CD8 + T cells in patient #1 (PFS = 2.7 months) and patient #2 (PFS = 90 months). ( Abbreviation : IHC: immunohistochemistry; IFN_TAMs: interferon-primed tumor-associated macrophages; mIF: multiple immunofluorescence; OS: overall survival; PFS: progression -free survival, Relapse: relapsed patients, patients without EFS24; Non_Relapse: non-relapsed patients, patients with EFS24. Mann-Whitney test was performed between groups.)

    Techniques Used: Expressing, Immunohistochemistry, Comparison, Staining, Immunofluorescence, MANN-WHITNEY

    rabbit anti eno1  (Danaher Inc)


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    Danaher Inc rabbit anti eno1
    HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and <t>ENO1,</t> and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Rabbit Anti Eno1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti eno1/product/Danaher Inc
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    1) Product Images from "Plant-Derived Exosomes as Novel Nanotherapeutics Contrive Glycolysis Reprogramming-Mediated Angiogenesis for Diabetic Ulcer Healing"

    Article Title: Plant-Derived Exosomes as Novel Nanotherapeutics Contrive Glycolysis Reprogramming-Mediated Angiogenesis for Diabetic Ulcer Healing

    Journal: Biomaterials Research

    doi: 10.34133/bmr.0035

    HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and ENO1, and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Figure Legend Snippet: HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and ENO1, and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Techniques Used: Expressing

    GExos promote angiogenesis in diabetic ulcers in mice by reprogramming glycolysis. Microvascular imaging (A 1 ) and semi-quantification of the microvascular density (A 2 ) in diabetic healed skins. 8D, 8 days; 16D, 16 days. Immunofluorescence staining (B 1 ) of CD31 (red) and semi-quantification of the area percentage of CD31 (B 2 ) in diabetic healed skins. H&E staining (C) and eNOS staining (D) in diabetic healed skins. Expression levels (E) and quantitative analysis (F 1 to F 3 ) of PFKM, PGK1, and ENO1 on day 8 in diabetic healed skin. Expression levels (G) and quantitative analysis (H 1 to H 3 ) of PFKM, PGK1, and ENO1 on day 16 in diabetic healed skin. Quantitative analysis of G6P (I 1 and I 2 ), FDP (J 1 and J 2 ), and Acetyl-CoA (K 1 and K 2 ) in diabetic healed skins on day 8 and day 16. (L) Schematic diagram of the therapeutic mechanism of GExos promoting angiogenesis in diabetic ulcers. P values are shown: * P < 0.05, ** P < 0.01, **** P < 0.0001.
    Figure Legend Snippet: GExos promote angiogenesis in diabetic ulcers in mice by reprogramming glycolysis. Microvascular imaging (A 1 ) and semi-quantification of the microvascular density (A 2 ) in diabetic healed skins. 8D, 8 days; 16D, 16 days. Immunofluorescence staining (B 1 ) of CD31 (red) and semi-quantification of the area percentage of CD31 (B 2 ) in diabetic healed skins. H&E staining (C) and eNOS staining (D) in diabetic healed skins. Expression levels (E) and quantitative analysis (F 1 to F 3 ) of PFKM, PGK1, and ENO1 on day 8 in diabetic healed skin. Expression levels (G) and quantitative analysis (H 1 to H 3 ) of PFKM, PGK1, and ENO1 on day 16 in diabetic healed skin. Quantitative analysis of G6P (I 1 and I 2 ), FDP (J 1 and J 2 ), and Acetyl-CoA (K 1 and K 2 ) in diabetic healed skins on day 8 and day 16. (L) Schematic diagram of the therapeutic mechanism of GExos promoting angiogenesis in diabetic ulcers. P values are shown: * P < 0.05, ** P < 0.01, **** P < 0.0001.

    Techniques Used: Imaging, Immunofluorescence, Staining, Expressing

    anti eno1  (Danaher Inc)


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    Danaher Inc anti eno1
    PGC interacts with IQGAP1 and interferes with IQGAP1 protein stability in GC cells. For the Co-IP assays, AGS cells were transfected with FLAG-PGC, and the FLAG fusion magnetic beads were used for pulldown analysis. ( A – C ) FLAG-PGC interacts with IQGAP1 ( A ), but not ARHGEF2 ( B ), CDC42BP2, or <t>ENO1</t> ( C ). ( D ) HA-IQGAP1 interacts with FLAG-PGC in GC cells, indicating that PGC and IQGAP1 can interact with each other. The AGS cells were cotransfected with HA-IQGAP1 and FLAG-PGC. HA fusion magnetic beads were used for pull-down analysis, and anti-HA antibodies as well as anti-FLAG antibodies were used for WB. The red arrow points to the band of interest. ( E ) PGC and IQGAP1 are co-localized in the cytoplasm, as demonstrated by immunofluorescence staining analysis. The red arrows indicate the representative overlap of green fluorescence with red fluorescence. ( F – H ) qRT-PCR and WB were used to determine the expression level changes of IQGAP1 in HGC-27, AGS, and MKN-45 cells transfected with LV-PGC and LV-Ctrl. The results showed that PGC decreased the expression of the IQGAP1 protein rather than the mRNA, which suggested that the effect of PGC on IQGAP1 may be at the post-transcriptional level. ( I ) AGS cells treated with CHX (100 µM/mL) revealed that PGC overexpression accelerated the degradation of IQGAP1. ( J ) AGS cells treated with MG132 for 6 h showed that the downregulation of IQGAP1 protein induced by PGC was rescued by the proteasome inhibitor MG132. PGC may decrease the protein stability of IQGAP1 by affecting its ubiquitination level. Data are shown as means ± SEM; * p < 0.05, ns: no significance. The uncropped bolts are shown in .
    Anti Eno1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Pepsinogen C Interacts with IQGAP1 to Inhibit the Metastasis of Gastric Cancer Cells by Suppressing Rho-GTPase Pathway"

    Article Title: Pepsinogen C Interacts with IQGAP1 to Inhibit the Metastasis of Gastric Cancer Cells by Suppressing Rho-GTPase Pathway

    Journal: Cancers

    doi: 10.3390/cancers16101796

    PGC interacts with IQGAP1 and interferes with IQGAP1 protein stability in GC cells. For the Co-IP assays, AGS cells were transfected with FLAG-PGC, and the FLAG fusion magnetic beads were used for pulldown analysis. ( A – C ) FLAG-PGC interacts with IQGAP1 ( A ), but not ARHGEF2 ( B ), CDC42BP2, or ENO1 ( C ). ( D ) HA-IQGAP1 interacts with FLAG-PGC in GC cells, indicating that PGC and IQGAP1 can interact with each other. The AGS cells were cotransfected with HA-IQGAP1 and FLAG-PGC. HA fusion magnetic beads were used for pull-down analysis, and anti-HA antibodies as well as anti-FLAG antibodies were used for WB. The red arrow points to the band of interest. ( E ) PGC and IQGAP1 are co-localized in the cytoplasm, as demonstrated by immunofluorescence staining analysis. The red arrows indicate the representative overlap of green fluorescence with red fluorescence. ( F – H ) qRT-PCR and WB were used to determine the expression level changes of IQGAP1 in HGC-27, AGS, and MKN-45 cells transfected with LV-PGC and LV-Ctrl. The results showed that PGC decreased the expression of the IQGAP1 protein rather than the mRNA, which suggested that the effect of PGC on IQGAP1 may be at the post-transcriptional level. ( I ) AGS cells treated with CHX (100 µM/mL) revealed that PGC overexpression accelerated the degradation of IQGAP1. ( J ) AGS cells treated with MG132 for 6 h showed that the downregulation of IQGAP1 protein induced by PGC was rescued by the proteasome inhibitor MG132. PGC may decrease the protein stability of IQGAP1 by affecting its ubiquitination level. Data are shown as means ± SEM; * p < 0.05, ns: no significance. The uncropped bolts are shown in .
    Figure Legend Snippet: PGC interacts with IQGAP1 and interferes with IQGAP1 protein stability in GC cells. For the Co-IP assays, AGS cells were transfected with FLAG-PGC, and the FLAG fusion magnetic beads were used for pulldown analysis. ( A – C ) FLAG-PGC interacts with IQGAP1 ( A ), but not ARHGEF2 ( B ), CDC42BP2, or ENO1 ( C ). ( D ) HA-IQGAP1 interacts with FLAG-PGC in GC cells, indicating that PGC and IQGAP1 can interact with each other. The AGS cells were cotransfected with HA-IQGAP1 and FLAG-PGC. HA fusion magnetic beads were used for pull-down analysis, and anti-HA antibodies as well as anti-FLAG antibodies were used for WB. The red arrow points to the band of interest. ( E ) PGC and IQGAP1 are co-localized in the cytoplasm, as demonstrated by immunofluorescence staining analysis. The red arrows indicate the representative overlap of green fluorescence with red fluorescence. ( F – H ) qRT-PCR and WB were used to determine the expression level changes of IQGAP1 in HGC-27, AGS, and MKN-45 cells transfected with LV-PGC and LV-Ctrl. The results showed that PGC decreased the expression of the IQGAP1 protein rather than the mRNA, which suggested that the effect of PGC on IQGAP1 may be at the post-transcriptional level. ( I ) AGS cells treated with CHX (100 µM/mL) revealed that PGC overexpression accelerated the degradation of IQGAP1. ( J ) AGS cells treated with MG132 for 6 h showed that the downregulation of IQGAP1 protein induced by PGC was rescued by the proteasome inhibitor MG132. PGC may decrease the protein stability of IQGAP1 by affecting its ubiquitination level. Data are shown as means ± SEM; * p < 0.05, ns: no significance. The uncropped bolts are shown in .

    Techniques Used: Co-Immunoprecipitation Assay, Transfection, Magnetic Beads, Immunofluorescence, Staining, Fluorescence, Quantitative RT-PCR, Expressing, Over Expression

    anti eno1  (Danaher Inc)


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    Danaher Inc anti eno1
    Prognostic value of the senescence-metabolism-related risk model (SeMRM) in two independent renal cell carcinoma (ccRCC) cohorts. ( A ) Kaplan‒Meier analysis of the overall survival (OS) curve of patients with low or high senescence-metabolism-related risk score (SeMRM) subgroups from two independent validation cohorts (International Cancer Genome Consortium (ICGC) KIRC and GSE29609). ( B ) Receiver operating characteristic (ROC) curve for predicting 1-year, 3-year and 5-year OS in the ICGC KIRC and GSE29609 cohorts. ( C ) ROC analysis showed that in the ICGC KIRC and GSE29609 cohorts, the predictive accuracy of SeMRM in OS was better than that of other clinical features. Univariate and multivariate Cox regression analysis of SeMRM and clinical features in the ( D, E ) ICGC KIRC and GSE29609 cohorts. ( F, G ) Immunohistochemistry (IHC) staining was used to detect the expression of key metabolism-related differentially expressed genes (mDEGs) (NME2, CD44, COL1A1, ENO2, <t>ENO1,</t> FGF1, and PTGER4) in ccRCC tissue arrays from 61 normal tissues and 153 tumor tissues. A representative image is shown. Statistical analysis of the IHC staining immunoreactivity score (IRS). * p < 0. 05; ** p < 0. 01; *** p < 0. 001
    Anti Eno1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Cellular senescence and metabolic reprogramming model based on bulk/single-cell RNA sequencing reveals PTGER4 as a therapeutic target for ccRCC"

    Article Title: Cellular senescence and metabolic reprogramming model based on bulk/single-cell RNA sequencing reveals PTGER4 as a therapeutic target for ccRCC

    Journal: BMC Cancer

    doi: 10.1186/s12885-024-12234-5

    Prognostic value of the senescence-metabolism-related risk model (SeMRM) in two independent renal cell carcinoma (ccRCC) cohorts. ( A ) Kaplan‒Meier analysis of the overall survival (OS) curve of patients with low or high senescence-metabolism-related risk score (SeMRM) subgroups from two independent validation cohorts (International Cancer Genome Consortium (ICGC) KIRC and GSE29609). ( B ) Receiver operating characteristic (ROC) curve for predicting 1-year, 3-year and 5-year OS in the ICGC KIRC and GSE29609 cohorts. ( C ) ROC analysis showed that in the ICGC KIRC and GSE29609 cohorts, the predictive accuracy of SeMRM in OS was better than that of other clinical features. Univariate and multivariate Cox regression analysis of SeMRM and clinical features in the ( D, E ) ICGC KIRC and GSE29609 cohorts. ( F, G ) Immunohistochemistry (IHC) staining was used to detect the expression of key metabolism-related differentially expressed genes (mDEGs) (NME2, CD44, COL1A1, ENO2, ENO1, FGF1, and PTGER4) in ccRCC tissue arrays from 61 normal tissues and 153 tumor tissues. A representative image is shown. Statistical analysis of the IHC staining immunoreactivity score (IRS). * p < 0. 05; ** p < 0. 01; *** p < 0. 001
    Figure Legend Snippet: Prognostic value of the senescence-metabolism-related risk model (SeMRM) in two independent renal cell carcinoma (ccRCC) cohorts. ( A ) Kaplan‒Meier analysis of the overall survival (OS) curve of patients with low or high senescence-metabolism-related risk score (SeMRM) subgroups from two independent validation cohorts (International Cancer Genome Consortium (ICGC) KIRC and GSE29609). ( B ) Receiver operating characteristic (ROC) curve for predicting 1-year, 3-year and 5-year OS in the ICGC KIRC and GSE29609 cohorts. ( C ) ROC analysis showed that in the ICGC KIRC and GSE29609 cohorts, the predictive accuracy of SeMRM in OS was better than that of other clinical features. Univariate and multivariate Cox regression analysis of SeMRM and clinical features in the ( D, E ) ICGC KIRC and GSE29609 cohorts. ( F, G ) Immunohistochemistry (IHC) staining was used to detect the expression of key metabolism-related differentially expressed genes (mDEGs) (NME2, CD44, COL1A1, ENO2, ENO1, FGF1, and PTGER4) in ccRCC tissue arrays from 61 normal tissues and 153 tumor tissues. A representative image is shown. Statistical analysis of the IHC staining immunoreactivity score (IRS). * p < 0. 05; ** p < 0. 01; *** p < 0. 001

    Techniques Used: Immunohistochemistry, Expressing

    Prognostic value of the senescence-metabolism-related risk model (SeMRM) in single-cell data of renal cell carcinoma (ccRCC) and real-world studies. ( A-B ) UMAP maps of all single cells. ( A ) Each color encodes 12 sample sources. ( B ) Each color encodes 6 major cell types. ( C ) The proportion of cells derived from 5 nonmalignant and 7 tumor samples according to the SeMRM classification. ( D ) The expression of seven key mDEGs in the whole umap. ( E ) Expression and distribution of seven key mDEGs in the differentiation trajectory of ccRCC epithelial cells. ( F ) The differentiation trajectory of ccRCC epithelial cells with SeMRM as the classification standard. ( G ) Immunohistochemical (IHC) staining was performed using ccRCC tissue arrays from 61 normal tissues and 153 tumor tissues to detect the expression of key metabolism-related differentially expressed genes (mDEG) (NME2, CD44, COL1A1, ENO2, ENO1, FGF1, and PTGER4). A representative image is shown. Statistical analysis of the IHC staining immunoreactivity score (IRS). ( H )According to the survival data of chip patients, a survival analysis diagram of high and low SeMRM patients was drawn. * p < 0. 05; ** p < 0. 01; *** p < 0. 001
    Figure Legend Snippet: Prognostic value of the senescence-metabolism-related risk model (SeMRM) in single-cell data of renal cell carcinoma (ccRCC) and real-world studies. ( A-B ) UMAP maps of all single cells. ( A ) Each color encodes 12 sample sources. ( B ) Each color encodes 6 major cell types. ( C ) The proportion of cells derived from 5 nonmalignant and 7 tumor samples according to the SeMRM classification. ( D ) The expression of seven key mDEGs in the whole umap. ( E ) Expression and distribution of seven key mDEGs in the differentiation trajectory of ccRCC epithelial cells. ( F ) The differentiation trajectory of ccRCC epithelial cells with SeMRM as the classification standard. ( G ) Immunohistochemical (IHC) staining was performed using ccRCC tissue arrays from 61 normal tissues and 153 tumor tissues to detect the expression of key metabolism-related differentially expressed genes (mDEG) (NME2, CD44, COL1A1, ENO2, ENO1, FGF1, and PTGER4). A representative image is shown. Statistical analysis of the IHC staining immunoreactivity score (IRS). ( H )According to the survival data of chip patients, a survival analysis diagram of high and low SeMRM patients was drawn. * p < 0. 05; ** p < 0. 01; *** p < 0. 001

    Techniques Used: Derivative Assay, Expressing, Immunohistochemical staining, Immunohistochemistry

    anti eno1 2 3  (Danaher Inc)


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    Danaher Inc anti eno1 2 3
    Anti Eno1 2 3, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    mouse anti eno1 antibody  (Danaher Inc)


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    Danaher Inc mouse anti eno1 antibody
    Relative mRNA ( a ) and protein ( b ) level of key host cell proteins <t>(ENO1,</t> ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays
    Mouse Anti Eno1 Antibody, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40"

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    Journal: Parasites & Vectors

    doi: 10.1186/s13071-024-06233-5

    Relative mRNA ( a ) and protein ( b ) level of key host cell proteins (ENO1, ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays
    Figure Legend Snippet: Relative mRNA ( a ) and protein ( b ) level of key host cell proteins (ENO1, ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays

    Techniques Used: Cell Culture

    Confirmation of the interactions between Cpgp40 and host protein ENO1. a Verification of recombinant protein expression in HEK293T cells. b Interactions between ENO1 and Cpgp40 in vivo as determined by coimmunoprecipitation. c Bimolecular fluorescence complementation (BiFC) assessing the interactions between ENO1 and Cpgp40 in live mammalian cells. A: positive control: pbJun-VN155 + pbFos-vc155. B: pBiFC-VC155-GP40 + pBiFC-VN155-ENO1. C: negative control: pbJun-VN155 + pbFos-vc155(delta ZIP). D: blank. (scale bar: 100 μm). The red arrow points to the fluorescent signal
    Figure Legend Snippet: Confirmation of the interactions between Cpgp40 and host protein ENO1. a Verification of recombinant protein expression in HEK293T cells. b Interactions between ENO1 and Cpgp40 in vivo as determined by coimmunoprecipitation. c Bimolecular fluorescence complementation (BiFC) assessing the interactions between ENO1 and Cpgp40 in live mammalian cells. A: positive control: pbJun-VN155 + pbFos-vc155. B: pBiFC-VC155-GP40 + pBiFC-VN155-ENO1. C: negative control: pbJun-VN155 + pbFos-vc155(delta ZIP). D: blank. (scale bar: 100 μm). The red arrow points to the fluorescent signal

    Techniques Used: Recombinant, Expressing, In Vivo, Fluorescence, Positive Control, Negative Control

    The silent efficiency detection of siRNA and inhibition of Cryptosporidium parvum invasion of HCT-8 cells by monoclonal ENO1 antibodies, siRNA, and overexpression of ENO1. a The silent efficiency detection of siRNA. GAPDH was used as an internal reference protein. b – d Inhibition of C. parvum invasion of HCT-8 cells. Human SSU rRNA gene was used as an internal control. Values are mean ± SEM. control: b PBS; c si-NC; d pcDNA3.1 blank vector
    Figure Legend Snippet: The silent efficiency detection of siRNA and inhibition of Cryptosporidium parvum invasion of HCT-8 cells by monoclonal ENO1 antibodies, siRNA, and overexpression of ENO1. a The silent efficiency detection of siRNA. GAPDH was used as an internal reference protein. b – d Inhibition of C. parvum invasion of HCT-8 cells. Human SSU rRNA gene was used as an internal control. Values are mean ± SEM. control: b PBS; c si-NC; d pcDNA3.1 blank vector

    Techniques Used: Inhibition, Over Expression, Plasmid Preparation

    Effects of Cryptosporidium parvum infection on the mRNA and protein levels of Occludin, Claudin 4, and E‐cadherin in HCT-8 cells in the presence of siENO1 ( a ) or pcDNA3.1-ENO1 ( b ) transfection
    Figure Legend Snippet: Effects of Cryptosporidium parvum infection on the mRNA and protein levels of Occludin, Claudin 4, and E‐cadherin in HCT-8 cells in the presence of siENO1 ( a ) or pcDNA3.1-ENO1 ( b ) transfection

    Techniques Used: Infection, Transfection

    Alignment of amino acid sequence and phylogenetic analysis of human ENO1 with other enolase sequences. a Alignment of amino acid sequence of human ENO1 and other species. The Mg2 + binding motifs are shown in a blue box, substrate-binding motifs are shown in a green box, plasminogen binding motifs are shown in a black box, and the enolase signature is shown in red box. The shade of the blue background represents the level of similarity. b Phylogenetic analysis of human ENO1 with other enolase sequences. The phylogenetic tree was constructed using the neighbor-joining method. The percentages of replicate trees in which the associated taxa clustered together in the bootstrap test (1000 replicates) are shown next to the branches
    Figure Legend Snippet: Alignment of amino acid sequence and phylogenetic analysis of human ENO1 with other enolase sequences. a Alignment of amino acid sequence of human ENO1 and other species. The Mg2 + binding motifs are shown in a blue box, substrate-binding motifs are shown in a green box, plasminogen binding motifs are shown in a black box, and the enolase signature is shown in red box. The shade of the blue background represents the level of similarity. b Phylogenetic analysis of human ENO1 with other enolase sequences. The phylogenetic tree was constructed using the neighbor-joining method. The percentages of replicate trees in which the associated taxa clustered together in the bootstrap test (1000 replicates) are shown next to the branches

    Techniques Used: Sequencing, Binding Assay, Construct

    Effect of truncated ENO1 protein on the load of C. parvum in HCT-8 cells. a 3 h postinvasion and b 18 h postinvasion
    Figure Legend Snippet: Effect of truncated ENO1 protein on the load of C. parvum in HCT-8 cells. a 3 h postinvasion and b 18 h postinvasion

    Techniques Used:

    anti eno1  (Danaher Inc)


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    Danaher Inc anti eno1
    B7-H3 directly interacted with <t>ENO1</t> in vitro and in vivo . (A) B7-H3 or ENO1 acts as a decoy protein to reverse its interaction with B7-H3. Western blot analysis of immunoprecipitation confirmed the presence of ENO1. Input represented the total protein of H446 cells and normal IgG was used as a control. (B) The interaction between B7-H3 and ENO1 was confirmed in vitro by GST-pulldown using recombinant chimeric protein GST-B7-H3. Western blotting was used to analyze the expression levels of related proteins. The results showed that a specific band was observed at about 47 kDa compared to negative controls, suggesting that there may be interaction between B7-H3 and ENO1 in H446. The data were representative of three independent experiments. IB, immunoblotting; IP, immunoprecipitation; IgG, immunoglobulin G; GST, glutathione S-transferase.
    Anti Eno1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti eno1/product/Danaher Inc
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    1) Product Images from "B7-H3 promotes proliferation and migration of lung cancer cells by modulating PI3K/AKT pathway via ENO1 activity"

    Article Title: B7-H3 promotes proliferation and migration of lung cancer cells by modulating PI3K/AKT pathway via ENO1 activity

    Journal: Translational Cancer Research

    doi: 10.21037/tcr-23-1537

    B7-H3 directly interacted with ENO1 in vitro and in vivo . (A) B7-H3 or ENO1 acts as a decoy protein to reverse its interaction with B7-H3. Western blot analysis of immunoprecipitation confirmed the presence of ENO1. Input represented the total protein of H446 cells and normal IgG was used as a control. (B) The interaction between B7-H3 and ENO1 was confirmed in vitro by GST-pulldown using recombinant chimeric protein GST-B7-H3. Western blotting was used to analyze the expression levels of related proteins. The results showed that a specific band was observed at about 47 kDa compared to negative controls, suggesting that there may be interaction between B7-H3 and ENO1 in H446. The data were representative of three independent experiments. IB, immunoblotting; IP, immunoprecipitation; IgG, immunoglobulin G; GST, glutathione S-transferase.
    Figure Legend Snippet: B7-H3 directly interacted with ENO1 in vitro and in vivo . (A) B7-H3 or ENO1 acts as a decoy protein to reverse its interaction with B7-H3. Western blot analysis of immunoprecipitation confirmed the presence of ENO1. Input represented the total protein of H446 cells and normal IgG was used as a control. (B) The interaction between B7-H3 and ENO1 was confirmed in vitro by GST-pulldown using recombinant chimeric protein GST-B7-H3. Western blotting was used to analyze the expression levels of related proteins. The results showed that a specific band was observed at about 47 kDa compared to negative controls, suggesting that there may be interaction between B7-H3 and ENO1 in H446. The data were representative of three independent experiments. IB, immunoblotting; IP, immunoprecipitation; IgG, immunoglobulin G; GST, glutathione S-transferase.

    Techniques Used: In Vitro, In Vivo, Western Blot, Immunoprecipitation, Recombinant, Expressing

    Silencing of B7-H3 or ENO1 can attenuate cell growth and migration in lung carcinoma cell, affecting the PI3K/AKT signaling pathway. (A,B) qRT-PCR analysis showed that B7-H3 or ENO1 expression was markedly decreased in H446 cells transfected with siB7-H3 or siENO1 compared with siNC, respectively. The knockdown efficiency of B7-H3 and ENO1 also were confirmed by western blot analysis. (C) Silencing of B7-H3 or ENO1 significantly attenuated cell proliferation in H446 by CCK-8 assays. (D) Conversely, wound healing assays showed that B7-H3 or ENO1 knockdown can attenuated the migration ability of H446 cells compared with control group cells. Magnification: 10×. (E) Xenograft mouse models indicated that down-regulation of B7-H3 or ENO1 expression could significantly inhibit tumor growth in lung cancer. (F) The phosphorylation levels of PI3K and AKT were assessed by Western blot. As a result, the phosphorylate levels of PI3K-p85α, and AKT were significantly decreased in B7-H3 down-regulated or ENO1 down-regulated cells, whereas PI3K-p85α and AKT total protein levels were not altered. The data are mean ± SD of three independent experiments. *, P<0.05; **, P<0.01; ***, P<0.001. mRNA, messenger RNA; siNC, specific small interfering RNAs targeting negative control; siB7-H3, specific small interfering RNAs targeting human B7-H3; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; siENO1, specific small interfering RNAs targeting ENO1; OD, optical density; WT, wild type; shNC, specific short hairpin RNAs targeting negative control; shB7-H3, specific short hairpin RNAs targeting human B7-H3; qRT-PCR, quantitative real-time polymerase chain reaction; CCK-8, cell counting kit-8; SD, standard deviation.
    Figure Legend Snippet: Silencing of B7-H3 or ENO1 can attenuate cell growth and migration in lung carcinoma cell, affecting the PI3K/AKT signaling pathway. (A,B) qRT-PCR analysis showed that B7-H3 or ENO1 expression was markedly decreased in H446 cells transfected with siB7-H3 or siENO1 compared with siNC, respectively. The knockdown efficiency of B7-H3 and ENO1 also were confirmed by western blot analysis. (C) Silencing of B7-H3 or ENO1 significantly attenuated cell proliferation in H446 by CCK-8 assays. (D) Conversely, wound healing assays showed that B7-H3 or ENO1 knockdown can attenuated the migration ability of H446 cells compared with control group cells. Magnification: 10×. (E) Xenograft mouse models indicated that down-regulation of B7-H3 or ENO1 expression could significantly inhibit tumor growth in lung cancer. (F) The phosphorylation levels of PI3K and AKT were assessed by Western blot. As a result, the phosphorylate levels of PI3K-p85α, and AKT were significantly decreased in B7-H3 down-regulated or ENO1 down-regulated cells, whereas PI3K-p85α and AKT total protein levels were not altered. The data are mean ± SD of three independent experiments. *, P<0.05; **, P<0.01; ***, P<0.001. mRNA, messenger RNA; siNC, specific small interfering RNAs targeting negative control; siB7-H3, specific small interfering RNAs targeting human B7-H3; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; siENO1, specific small interfering RNAs targeting ENO1; OD, optical density; WT, wild type; shNC, specific short hairpin RNAs targeting negative control; shB7-H3, specific short hairpin RNAs targeting human B7-H3; qRT-PCR, quantitative real-time polymerase chain reaction; CCK-8, cell counting kit-8; SD, standard deviation.

    Techniques Used: Migration, Quantitative RT-PCR, Expressing, Transfection, Western Blot, CCK-8 Assay, Negative Control, Real-time Polymerase Chain Reaction, Cell Counting, Standard Deviation

    Overexpression or silencing of B7-H3 affects the enzymatic activity of ENO1 in lung cancer cells. The activity of ENO1 was measured in different group cells, assessed by its corresponding detection kits. Results were determined by monitoring NADH consumption, with the rate of change in absorbance at 340 nm representing the enzymatic activity of ENO1. (A) Overexpression of B7-H3 enhanced the activity of ENO1 compared with vehicle group in SBC5. (B) Then, we found that inhibition of B7-H3 expression reduced the enzymatic activity of ENO1 compared with siNC group in H446. (C) Western blot analysis of the total protein and phosphorylation levels of PI3K and AKT in B7-H3 up-regulated or ENO1-inhibited lung cancer cells. Moreover, the phosphorylation levels of PI3K-p85α and AKT was expedited in SBC5-B7-H3 cells, while inhibition of ENO1 activity by AP-III-a4 reversed the above results. (D,E) The effects of B7-H3 overexpression on lung cancer cells could be attenuated through blocking ENO1 activity. Changes in the proliferation and relative mobility rate in SBC5-B7-H3 cells treated with ENO1 active inhibitor. Magnification: 4×. Our results indicated that the proliferation and wound-healing ability were markedly decreased by blocking of ENO1 activity in SBC5-B7-H3 cells. The data were representative of three independent experiments. *, P<0.05; ***, P<0.001. WT, wild type; siNC, specific small interfering RNAs targeting negative control; siB7-H3, specific small interfering RNAs targeting human B7-H3; OD, optical density.
    Figure Legend Snippet: Overexpression or silencing of B7-H3 affects the enzymatic activity of ENO1 in lung cancer cells. The activity of ENO1 was measured in different group cells, assessed by its corresponding detection kits. Results were determined by monitoring NADH consumption, with the rate of change in absorbance at 340 nm representing the enzymatic activity of ENO1. (A) Overexpression of B7-H3 enhanced the activity of ENO1 compared with vehicle group in SBC5. (B) Then, we found that inhibition of B7-H3 expression reduced the enzymatic activity of ENO1 compared with siNC group in H446. (C) Western blot analysis of the total protein and phosphorylation levels of PI3K and AKT in B7-H3 up-regulated or ENO1-inhibited lung cancer cells. Moreover, the phosphorylation levels of PI3K-p85α and AKT was expedited in SBC5-B7-H3 cells, while inhibition of ENO1 activity by AP-III-a4 reversed the above results. (D,E) The effects of B7-H3 overexpression on lung cancer cells could be attenuated through blocking ENO1 activity. Changes in the proliferation and relative mobility rate in SBC5-B7-H3 cells treated with ENO1 active inhibitor. Magnification: 4×. Our results indicated that the proliferation and wound-healing ability were markedly decreased by blocking of ENO1 activity in SBC5-B7-H3 cells. The data were representative of three independent experiments. *, P<0.05; ***, P<0.001. WT, wild type; siNC, specific small interfering RNAs targeting negative control; siB7-H3, specific small interfering RNAs targeting human B7-H3; OD, optical density.

    Techniques Used: Over Expression, Activity Assay, Inhibition, Expressing, Western Blot, Blocking Assay, Negative Control

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    <t>ENO1</t> shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant
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    HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and <t>ENO1,</t> and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
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    HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and <t>ENO1,</t> and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
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    Relative mRNA ( a ) and protein ( b ) level of key host cell proteins <t>(ENO1,</t> ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays
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    Image Search Results


    ENO1 shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: ENO1 shows increased expression, correlated with the level of tumorigenicity, in MCF10 TNBC cell lines. (A) Levels of ENO1 mRNA in the MCF10 TNBC tumour progression series of cells as detected by real-time qRT-PCR. ENO1 expression levels in the TNBC tumour progression series of cells, analysed using the -∆∆Ct method. Results represent the mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments, presented as fold change relative to the MCF10A normal cells. (B) Western blot of ENO1 expression in MCF10 TNBC cell lines. Cell lysates from MCF10 cell lines were subjected to western blot and probed with the indicated antibodies. ENO1 is shown to expressed in all cell lines with expression increasing in MCF10AT, MCF10Ca1h and MCF10Ca1a in comparison to MCF10A. Actin was used as a loading control. Result representative of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Densitometric analysis of 3 biological replicates of the western blot in panel B, ENO1 expression is normalised to the actin loading controls and represent the fold change increase in density of ENO1 protein in comparison to MCF10A. ** p < 0.01, *** p < 0.001, **** p < 0.0001 relative to MCF10A, ns – non-significant

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, Comparison

    ENO1 localisation is altered across MCF10 TNBC cell lines. (A) Typical CLSM images of the indicated MCF10 tumour progression cell lines, fixed and stained using an anti-ENO1 antibody (green) and DAPI to indicate nuclei (blue). (B) Digital images such as those shown in (A) were analysed to determine the nuclear to cytoplasmic fluorescence ratio (Fn/c) (where a ratio below 1 indicates cytoplasmic localisation and above 1 indicates nuclear localisation). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Typical CLSM images of the indicated cell lines, transfected to express GFP-ENO1 and imaged live 18–24 h post-transfection. (D) Digital images such as those shown in (C) were analyses to determine the Fn/c as per (B). Results represent mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments. * p < 0.05, ** p < 0.01, *** p < 0.001 relative to MCF10A, ns – non-significant

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: ENO1 localisation is altered across MCF10 TNBC cell lines. (A) Typical CLSM images of the indicated MCF10 tumour progression cell lines, fixed and stained using an anti-ENO1 antibody (green) and DAPI to indicate nuclei (blue). (B) Digital images such as those shown in (A) were analysed to determine the nuclear to cytoplasmic fluorescence ratio (Fn/c) (where a ratio below 1 indicates cytoplasmic localisation and above 1 indicates nuclear localisation). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. (C) Typical CLSM images of the indicated cell lines, transfected to express GFP-ENO1 and imaged live 18–24 h post-transfection. (D) Digital images such as those shown in (C) were analyses to determine the Fn/c as per (B). Results represent mean ± SEM of a single typical experiment from a series of 3 independent biological replicate experiments. * p < 0.05, ** p < 0.01, *** p < 0.001 relative to MCF10A, ns – non-significant

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Staining, Fluorescence, Transfection

    ENO1 is phosphorylated at S419 in breast cancer patient samples (A) Data used in this figure was publicly available data generated as stated by the Clinical Proteomic Tumor Analysis Consortium (NCI/NIH). Quantitative mass-spectrometry based phosphoproteomic analyses were performed on breast tumours (125 participants). Data were generated with TMT10plex quantification, and each 10-plex experiment contained a common reference sample composed of a pooled mixture of 40 tumour samples. Data was separated into receptor positive breast cancer (ER, PR, HER2 +) and TNBC manually for the current study, based on reported therapeutic receptor expression. When ER, PR or HER2 status was not stated, samples were assigned to a non-TNBC category. The graph indicates log transformed fold change ENO1 phosphopeptide abundance relative to a pooled breast cancer control sample. (B) Western blot of GFP-ENO1 expression in MCF10A and MCF10Ca1h TNBC cell lines. GFP-trap immunoprecipitations of the indicated MCF10 cell lines were subjected to western blot and probed with anti-phospho-serine antibody. Result representative of a single typical experiment from a series of 3 independent experiments

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: ENO1 is phosphorylated at S419 in breast cancer patient samples (A) Data used in this figure was publicly available data generated as stated by the Clinical Proteomic Tumor Analysis Consortium (NCI/NIH). Quantitative mass-spectrometry based phosphoproteomic analyses were performed on breast tumours (125 participants). Data were generated with TMT10plex quantification, and each 10-plex experiment contained a common reference sample composed of a pooled mixture of 40 tumour samples. Data was separated into receptor positive breast cancer (ER, PR, HER2 +) and TNBC manually for the current study, based on reported therapeutic receptor expression. When ER, PR or HER2 status was not stated, samples were assigned to a non-TNBC category. The graph indicates log transformed fold change ENO1 phosphopeptide abundance relative to a pooled breast cancer control sample. (B) Western blot of GFP-ENO1 expression in MCF10A and MCF10Ca1h TNBC cell lines. GFP-trap immunoprecipitations of the indicated MCF10 cell lines were subjected to western blot and probed with anti-phospho-serine antibody. Result representative of a single typical experiment from a series of 3 independent experiments

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Generated, Mass Spectrometry, Expressing, Transformation Assay, Western Blot

    Phosphomimetic point mutants of ENO1-S419 show altered nuclear transport only in MCF10Ca1h tumour cells. (A) MCF10A non-tumour and MCF10Ca1h tumour cells were transfected to express GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), then analysed by CLSM 18 h later. (B) Images such as those in (A) were analysed to determine the Fn/c ratio as per the legend to Fig. . Results represent mean Fn/c ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. ** p < 0.01 relative to GFP-ENO1, ns – non-significant. Data was not corrected for multiple comparisons

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Phosphomimetic point mutants of ENO1-S419 show altered nuclear transport only in MCF10Ca1h tumour cells. (A) MCF10A non-tumour and MCF10Ca1h tumour cells were transfected to express GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), then analysed by CLSM 18 h later. (B) Images such as those in (A) were analysed to determine the Fn/c ratio as per the legend to Fig. . Results represent mean Fn/c ± SEM ( n > 30) of a single typical experiment from a series of 3 independent biological replicate experiments. ** p < 0.01 relative to GFP-ENO1, ns – non-significant. Data was not corrected for multiple comparisons

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Transfection

    Casein kinase 1 inhibition with D4476 increases ENO1 nuclear accumulation in MCF10Ca1h tumour cells only. (A) MCF10 TNBC cell lines that were treated with 125 µM casein kinase 1 inhibitor D4476 or DMSO for 3 h, then fixed and stained with anti-ENO1 antibodies and imaged by CLSM. White star indicates complete nuclear accumulation of ENO1 observed in 10% of D4476 treated MCF10Ca1h cells. Images represent single typical cells from a series of 4 independent biological replicate experiments. (B) Images such as those in (A) were analysed to determine Fn/c ratio as previous. Results represent mean ± SEM ( n > 50) of a single typical experiment from a series of 4 independent biological replicate experiments. **** p < 0.0001 compared to DMSO treated cell line, all other comparisons were nonsignificant. Data was not corrected for multiple comparisons

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Casein kinase 1 inhibition with D4476 increases ENO1 nuclear accumulation in MCF10Ca1h tumour cells only. (A) MCF10 TNBC cell lines that were treated with 125 µM casein kinase 1 inhibitor D4476 or DMSO for 3 h, then fixed and stained with anti-ENO1 antibodies and imaged by CLSM. White star indicates complete nuclear accumulation of ENO1 observed in 10% of D4476 treated MCF10Ca1h cells. Images represent single typical cells from a series of 4 independent biological replicate experiments. (B) Images such as those in (A) were analysed to determine Fn/c ratio as previous. Results represent mean ± SEM ( n > 50) of a single typical experiment from a series of 4 independent biological replicate experiments. **** p < 0.0001 compared to DMSO treated cell line, all other comparisons were nonsignificant. Data was not corrected for multiple comparisons

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Inhibition, Staining

    Inhibition of CRM-1 mediated nuclear export using Leptomycin B (LMB) demonstrates enhanced tumour specific nuclear export of ENO1. MCF10A non-tumour and MCF10Ca1h tumour cells were transfected with GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), treated with LMB or untreated (UT), then fixed and stained with DAPI to define nuclei (blue), and imaged by CLSM. (A) Representative CLSM images of GFP-ENO1 and S419 point mutant transfected MCF10A (left) and MCF10Ca1h (right). (B) Images such as those in (A) were analysed to determine nuclear-cytoplasmic fluorescence ratios (Fn/c). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 4 independent biological replicate experiments. * p < 0.05, ** p < 0.01, ns – non-significant

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Inhibition of CRM-1 mediated nuclear export using Leptomycin B (LMB) demonstrates enhanced tumour specific nuclear export of ENO1. MCF10A non-tumour and MCF10Ca1h tumour cells were transfected with GFP-ENO1 and S419 point mutants (S419A phospho-null and S419D phosphomimetic), treated with LMB or untreated (UT), then fixed and stained with DAPI to define nuclei (blue), and imaged by CLSM. (A) Representative CLSM images of GFP-ENO1 and S419 point mutant transfected MCF10A (left) and MCF10Ca1h (right). (B) Images such as those in (A) were analysed to determine nuclear-cytoplasmic fluorescence ratios (Fn/c). Results represent mean ± SEM ( n > 30) of a single typical experiment from a series of 4 independent biological replicate experiments. * p < 0.05, ** p < 0.01, ns – non-significant

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Inhibition, Transfection, Staining, Mutagenesis, Fluorescence

    Relative glycolytic activity of ENO1 is not altered by charge at residue 419, or by tumour progression in MCF10 cell lines. (A) Recombinant proteins of wild type (WT) full length ENO1 or ENO1-S419A mutant, and equal amounts of cell lysate from MCF10 TNBC cells, were incubated in ENO1 antibody coated 96-well plates, then washed and activity solution containing pyruvate kinase and lactate dehydrogenase added. ENO1 activity was measured by NADH consumption over 60 min. Data is presented relative to the activity of an active ENO1 standard (Abcam, ab89248). (B) Activity of endogenous ENO1 immunopurified from whole cell lysates of the indicated MCF10 TNBC cell lines. Results represent mean ± SEM of a single experiment with 3 biological replicates. ns – non-significant

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Relative glycolytic activity of ENO1 is not altered by charge at residue 419, or by tumour progression in MCF10 cell lines. (A) Recombinant proteins of wild type (WT) full length ENO1 or ENO1-S419A mutant, and equal amounts of cell lysate from MCF10 TNBC cells, were incubated in ENO1 antibody coated 96-well plates, then washed and activity solution containing pyruvate kinase and lactate dehydrogenase added. ENO1 activity was measured by NADH consumption over 60 min. Data is presented relative to the activity of an active ENO1 standard (Abcam, ab89248). (B) Activity of endogenous ENO1 immunopurified from whole cell lysates of the indicated MCF10 TNBC cell lines. Results represent mean ± SEM of a single experiment with 3 biological replicates. ns – non-significant

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Activity Assay, Residue, Recombinant, Mutagenesis, Incubation

    Inhibited phosphorylation of miniTurbo-ENO1 with CK1 inhibitor D4476 reduces ENO1 interaction with cytoskeletal proteins and increases interaction with DNA-metabolism proteins. MCF10Ca1h tumour cells were transfected with V5-miniTurbo or V5-miniTurbo-ENO1, then biotinylated by addition of exogenous biotin for 20 min to induce proximity labelling of ENO1 interacting proteins. (A) CLSM images of MCF10Ca1h cells transfected with V5-miniTurbo (left) or V5-miniTurbo-ENO1 (right), then left untreated (UT) or treated with 50 µM biotin, cells were then fixed and stained with anti-V5 antibodies (red), or FITC-streptavidin (green) and nuclei were counterstained with DAPI (blue). Images represent single typical cells from a series of 3 independent biological replicate experiments. (B) Western blot of MCF10Ca1h cell lysates expressing miniTurbo-ENO1 (mT-ENO1) that were either untreated (UT) or treated with 50 µM biotin to induce proximity labelling of other proteins interacting with mT-ENO1. (C) Volcano plot of proteins that showed differences in label free quantitation (LFQ) of expression between MCF10Ca1h cells expressing MiniTurbo-ENO1 that were D4476 treated or DMSO treated, identified by LC-MS. Results represent difference in mean LFQ intensity (D4476 treated – DMSO treated) from 3 replicates, plotted against -log transformed p-values. Red stars indicate statistically significant differences in LFQ intensity between samples with gene name listed. (D) Graphical representation of protein classes present in significantly reduced miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 10 genes. Highest percentage group was coloured red. (E) Graphical representation of protein classes present in significantly enriched miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 9 genes. Highest percentage group was coloured red. Protein classes were assigned using Panther Gene Ontology (GO) analysis online tool. LFQ intensity differences and p-values are reported for all differing proteins in Supplementary Table 1

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Inhibited phosphorylation of miniTurbo-ENO1 with CK1 inhibitor D4476 reduces ENO1 interaction with cytoskeletal proteins and increases interaction with DNA-metabolism proteins. MCF10Ca1h tumour cells were transfected with V5-miniTurbo or V5-miniTurbo-ENO1, then biotinylated by addition of exogenous biotin for 20 min to induce proximity labelling of ENO1 interacting proteins. (A) CLSM images of MCF10Ca1h cells transfected with V5-miniTurbo (left) or V5-miniTurbo-ENO1 (right), then left untreated (UT) or treated with 50 µM biotin, cells were then fixed and stained with anti-V5 antibodies (red), or FITC-streptavidin (green) and nuclei were counterstained with DAPI (blue). Images represent single typical cells from a series of 3 independent biological replicate experiments. (B) Western blot of MCF10Ca1h cell lysates expressing miniTurbo-ENO1 (mT-ENO1) that were either untreated (UT) or treated with 50 µM biotin to induce proximity labelling of other proteins interacting with mT-ENO1. (C) Volcano plot of proteins that showed differences in label free quantitation (LFQ) of expression between MCF10Ca1h cells expressing MiniTurbo-ENO1 that were D4476 treated or DMSO treated, identified by LC-MS. Results represent difference in mean LFQ intensity (D4476 treated – DMSO treated) from 3 replicates, plotted against -log transformed p-values. Red stars indicate statistically significant differences in LFQ intensity between samples with gene name listed. (D) Graphical representation of protein classes present in significantly reduced miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 10 genes. Highest percentage group was coloured red. (E) Graphical representation of protein classes present in significantly enriched miniTurbo-ENO1 with D4476 treatment interactor list. Results represent percentage of genes mapped to each protein class listed from n = 9 genes. Highest percentage group was coloured red. Protein classes were assigned using Panther Gene Ontology (GO) analysis online tool. LFQ intensity differences and p-values are reported for all differing proteins in Supplementary Table 1

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Transfection, Staining, Western Blot, Expressing, Quantitation Assay, Liquid Chromatography with Mass Spectroscopy, Transformation Assay

    Proposed model of phosphorylated ENO1’s nucleocytoplasmic transport and associated roles in non-tumour MCF10A and tumorigenic MCF10Ca1h cells. (A) Diagram of proposed model of ENO1-S419 phosphorylation-mediated regulation of tumour-specific nucleocytoplasmic transport. Upon ENO1-S419 phosphorylation we suggest that ENO1 is unable to enter the nucleus, whereas a lack of S419 phosphorylation renders ENO1 unable to be exported to the cytoplasm (left side). Our results may also suggest that phosphorylated ENO1-S419 specifically exhibits enhanced nuclear export in comparison to that observed in non-tumour cells (right side). (B) In non-tumour cells non-phosphorylated ENO1-S419 shows increased localisation in the nucleus, possibly supporting functions such as DNA-repair or transcriptional regulation. (C) In tumour cells phosphorylated ENO1-S419 is mostly excluded from the nucleus and localised in the cytoplasm, possibly supporting functions such as cytoskeletal organisation or molecular chaperoning of proteins to the cell membrane when phosphorylated. Figure created on Biorender.com

    Journal: Cell & Bioscience

    Article Title: Tumour-specific phosphorylation of serine 419 drives alpha-enolase (ENO1) nuclear export in triple negative breast cancer progression

    doi: 10.1186/s13578-024-01249-x

    Figure Lengend Snippet: Proposed model of phosphorylated ENO1’s nucleocytoplasmic transport and associated roles in non-tumour MCF10A and tumorigenic MCF10Ca1h cells. (A) Diagram of proposed model of ENO1-S419 phosphorylation-mediated regulation of tumour-specific nucleocytoplasmic transport. Upon ENO1-S419 phosphorylation we suggest that ENO1 is unable to enter the nucleus, whereas a lack of S419 phosphorylation renders ENO1 unable to be exported to the cytoplasm (left side). Our results may also suggest that phosphorylated ENO1-S419 specifically exhibits enhanced nuclear export in comparison to that observed in non-tumour cells (right side). (B) In non-tumour cells non-phosphorylated ENO1-S419 shows increased localisation in the nucleus, possibly supporting functions such as DNA-repair or transcriptional regulation. (C) In tumour cells phosphorylated ENO1-S419 is mostly excluded from the nucleus and localised in the cytoplasm, possibly supporting functions such as cytoskeletal organisation or molecular chaperoning of proteins to the cell membrane when phosphorylated. Figure created on Biorender.com

    Article Snippet: Anti-ENO1 (ab155102) and pan-phospho-serine (ab9332) antibodies were purchased from Abcam.

    Techniques: Comparison, Membrane

    Reagents and tools table

    Journal: Biomarker Research

    Article Title: Single-cell and spatial transcriptomics reveal a high glycolysis B cell and tumor-associated macrophages cluster correlated with poor prognosis and exhausted immune microenvironment in diffuse large B-cell lymphoma

    doi: 10.1186/s40364-024-00605-w

    Figure Lengend Snippet: Reagents and tools table

    Article Snippet: Rabbit anti-human ENO1 IgG antibody , ab227978 , Abcam.

    Techniques: RNA Sequencing Assay, Sequencing, Expressing, Formalin-fixed Paraffin-Embedded, Immunohistochemistry, Microscopy, Immunofluorescence, Software

    Identifcation of glycolysis / gluconeogenesis maker genes in high malignant B cells. A Volcano plot of differential genes among the benign B cells, low malignant B cells, and high malignant B cells. B. Functional analysis of highly expressed genes in high malignant B cells by Metascape. C. Identification of eight commonly genes overlapped across three groups and glycolysis hallmark genes. D. Module trait correlation showed the relationships between modules, CNV score, and Glycolysis score. E. Network visualization of 10 modules of high maligant B cells.( The modules highlighted in red and underlined are modules associated with CNV score and Glycolysis score. ) F. The first 25 eigengenes of each module. G. Trajectory of different malignant B subclusters predicted by monocle. H. Genes expression level in single spot ordered along the pseudotime for MKI67 and seven glycolysis / gluconeogenesis gene markers ( STMN1, ENO1, LDHA, TPI1, CDK1, PKM , and PPIA ). ( Abbreviation : HMB: high malignant B cells; CNV: copy number variation; UMAP: uniform manifold approximation and projection. *** p < 0.001.)

    Journal: Biomarker Research

    Article Title: Single-cell and spatial transcriptomics reveal a high glycolysis B cell and tumor-associated macrophages cluster correlated with poor prognosis and exhausted immune microenvironment in diffuse large B-cell lymphoma

    doi: 10.1186/s40364-024-00605-w

    Figure Lengend Snippet: Identifcation of glycolysis / gluconeogenesis maker genes in high malignant B cells. A Volcano plot of differential genes among the benign B cells, low malignant B cells, and high malignant B cells. B. Functional analysis of highly expressed genes in high malignant B cells by Metascape. C. Identification of eight commonly genes overlapped across three groups and glycolysis hallmark genes. D. Module trait correlation showed the relationships between modules, CNV score, and Glycolysis score. E. Network visualization of 10 modules of high maligant B cells.( The modules highlighted in red and underlined are modules associated with CNV score and Glycolysis score. ) F. The first 25 eigengenes of each module. G. Trajectory of different malignant B subclusters predicted by monocle. H. Genes expression level in single spot ordered along the pseudotime for MKI67 and seven glycolysis / gluconeogenesis gene markers ( STMN1, ENO1, LDHA, TPI1, CDK1, PKM , and PPIA ). ( Abbreviation : HMB: high malignant B cells; CNV: copy number variation; UMAP: uniform manifold approximation and projection. *** p < 0.001.)

    Article Snippet: Rabbit anti-human ENO1 IgG antibody , ab227978 , Abcam.

    Techniques: Functional Assay, Expressing

    Prognostic value of four glycolysis / gluconeogenesis (STMN1, ENO1, CDK1, PKM, and PPIA) proteins in IHC cohort ( n = 34, 100X) and IFN_TAMs (CD68 + CXCL10 + PD-L1 + ) in mIF cohort ( n = 20, 10X). A-B. Kaplan–Meier curves of OS and PFS according to STMN1, CDK1, ENO1 and PKM proteins expression. C. Representative IHC staining of STMN1, CDK1, ENO1 and PKM in patient 1 (PFS = 7 months, OS = 9 months) and patient 2 (PFS = 135 months, OS = 135 months). D. Kaplan-Meier analysis for PFS based on IFN_TAMs intensity. E. Comparison of IFN_TAMs intensity in relapse and non_relapse groups. F. Correlation of IFN_TAMs’ intensity, CD8 + T cells’ intensity, and TGFβ1 intensity. G. Representative mIF staining of IFN_TAMs and CD8 + T cells in patient #1 (PFS = 2.7 months) and patient #2 (PFS = 90 months). ( Abbreviation : IHC: immunohistochemistry; IFN_TAMs: interferon-primed tumor-associated macrophages; mIF: multiple immunofluorescence; OS: overall survival; PFS: progression -free survival, Relapse: relapsed patients, patients without EFS24; Non_Relapse: non-relapsed patients, patients with EFS24. Mann-Whitney test was performed between groups.)

    Journal: Biomarker Research

    Article Title: Single-cell and spatial transcriptomics reveal a high glycolysis B cell and tumor-associated macrophages cluster correlated with poor prognosis and exhausted immune microenvironment in diffuse large B-cell lymphoma

    doi: 10.1186/s40364-024-00605-w

    Figure Lengend Snippet: Prognostic value of four glycolysis / gluconeogenesis (STMN1, ENO1, CDK1, PKM, and PPIA) proteins in IHC cohort ( n = 34, 100X) and IFN_TAMs (CD68 + CXCL10 + PD-L1 + ) in mIF cohort ( n = 20, 10X). A-B. Kaplan–Meier curves of OS and PFS according to STMN1, CDK1, ENO1 and PKM proteins expression. C. Representative IHC staining of STMN1, CDK1, ENO1 and PKM in patient 1 (PFS = 7 months, OS = 9 months) and patient 2 (PFS = 135 months, OS = 135 months). D. Kaplan-Meier analysis for PFS based on IFN_TAMs intensity. E. Comparison of IFN_TAMs intensity in relapse and non_relapse groups. F. Correlation of IFN_TAMs’ intensity, CD8 + T cells’ intensity, and TGFβ1 intensity. G. Representative mIF staining of IFN_TAMs and CD8 + T cells in patient #1 (PFS = 2.7 months) and patient #2 (PFS = 90 months). ( Abbreviation : IHC: immunohistochemistry; IFN_TAMs: interferon-primed tumor-associated macrophages; mIF: multiple immunofluorescence; OS: overall survival; PFS: progression -free survival, Relapse: relapsed patients, patients without EFS24; Non_Relapse: non-relapsed patients, patients with EFS24. Mann-Whitney test was performed between groups.)

    Article Snippet: Rabbit anti-human ENO1 IgG antibody , ab227978 , Abcam.

    Techniques: Expressing, Immunohistochemistry, Comparison, Staining, Immunofluorescence, MANN-WHITNEY

    HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and ENO1, and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Journal: Biomaterials Research

    Article Title: Plant-Derived Exosomes as Novel Nanotherapeutics Contrive Glycolysis Reprogramming-Mediated Angiogenesis for Diabetic Ulcer Healing

    doi: 10.34133/bmr.0035

    Figure Lengend Snippet: HUVECs’ genetic and metabolic alterations to GExos treatment in HG culture. (A1 to A2) Enrichment plots from GSEAs of gene sets for the “Positive regulation of glycolysis signaling”. Expression levels and quantitative analysis of (B1 to B4) PFKM, PGK1, and ENO1, and (C1 to C4) PGLS, ACACA, and PDHA1. (D) Schematic illustration of the major genes and metabolic signaling pathways relevant to angiogenesis, regulated by GExos. (E) Volcano plots of differentially expressed metabolites identified at q < 0.05. (F) KEGG pathway enrichment analyses of the differentially expressed metabolites. (G) Sankey diagram of the differentially expressed metabolites and corresponding enrichment pathways. (H) Mechanism diagram of gene–metabolite interaction. Expression levels (I 1 to I 3 ) and quantitative analysis (J 1 to J 3 ) of G6P, FDP, and Acetyl-CoA. P values are shown: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Article Snippet: After blocking with 5% non-fat milk in Tris-buffered saline containing 0.1% Tween-20, the membranes were then incubated at 4 °C overnight with the following antibodies: rabbit anti-PFKM (Abcam, ab154804, 1:1,000), rabbit anti-PGK1 (Abcam, ab199438, 1:2,000), rabbit anti-ENO1 (Abcam, ab227978, 1:1,000), rabbit anti-PGLS (Abcam, ab229980, 1:2,000), rabbit anti-ACACA (Abcam, ab45174, 1:2,000), rabbit anti-PDHA1 (Abcam, ab168379, 1:2,000), rabbit anti-β-actin (Abcam, ab68477, 1:10,000, internal control), rabbit anti-Cyclin D1 (Abcam, ab134175, 1:10,000), mouse anti-Cyclin D3 (Abcam, ab289546, 1:1,000), and mouse anti-β-actin (Abcam, ab8226, 1:1,000, internal control).

    Techniques: Expressing

    GExos promote angiogenesis in diabetic ulcers in mice by reprogramming glycolysis. Microvascular imaging (A 1 ) and semi-quantification of the microvascular density (A 2 ) in diabetic healed skins. 8D, 8 days; 16D, 16 days. Immunofluorescence staining (B 1 ) of CD31 (red) and semi-quantification of the area percentage of CD31 (B 2 ) in diabetic healed skins. H&E staining (C) and eNOS staining (D) in diabetic healed skins. Expression levels (E) and quantitative analysis (F 1 to F 3 ) of PFKM, PGK1, and ENO1 on day 8 in diabetic healed skin. Expression levels (G) and quantitative analysis (H 1 to H 3 ) of PFKM, PGK1, and ENO1 on day 16 in diabetic healed skin. Quantitative analysis of G6P (I 1 and I 2 ), FDP (J 1 and J 2 ), and Acetyl-CoA (K 1 and K 2 ) in diabetic healed skins on day 8 and day 16. (L) Schematic diagram of the therapeutic mechanism of GExos promoting angiogenesis in diabetic ulcers. P values are shown: * P < 0.05, ** P < 0.01, **** P < 0.0001.

    Journal: Biomaterials Research

    Article Title: Plant-Derived Exosomes as Novel Nanotherapeutics Contrive Glycolysis Reprogramming-Mediated Angiogenesis for Diabetic Ulcer Healing

    doi: 10.34133/bmr.0035

    Figure Lengend Snippet: GExos promote angiogenesis in diabetic ulcers in mice by reprogramming glycolysis. Microvascular imaging (A 1 ) and semi-quantification of the microvascular density (A 2 ) in diabetic healed skins. 8D, 8 days; 16D, 16 days. Immunofluorescence staining (B 1 ) of CD31 (red) and semi-quantification of the area percentage of CD31 (B 2 ) in diabetic healed skins. H&E staining (C) and eNOS staining (D) in diabetic healed skins. Expression levels (E) and quantitative analysis (F 1 to F 3 ) of PFKM, PGK1, and ENO1 on day 8 in diabetic healed skin. Expression levels (G) and quantitative analysis (H 1 to H 3 ) of PFKM, PGK1, and ENO1 on day 16 in diabetic healed skin. Quantitative analysis of G6P (I 1 and I 2 ), FDP (J 1 and J 2 ), and Acetyl-CoA (K 1 and K 2 ) in diabetic healed skins on day 8 and day 16. (L) Schematic diagram of the therapeutic mechanism of GExos promoting angiogenesis in diabetic ulcers. P values are shown: * P < 0.05, ** P < 0.01, **** P < 0.0001.

    Article Snippet: After blocking with 5% non-fat milk in Tris-buffered saline containing 0.1% Tween-20, the membranes were then incubated at 4 °C overnight with the following antibodies: rabbit anti-PFKM (Abcam, ab154804, 1:1,000), rabbit anti-PGK1 (Abcam, ab199438, 1:2,000), rabbit anti-ENO1 (Abcam, ab227978, 1:1,000), rabbit anti-PGLS (Abcam, ab229980, 1:2,000), rabbit anti-ACACA (Abcam, ab45174, 1:2,000), rabbit anti-PDHA1 (Abcam, ab168379, 1:2,000), rabbit anti-β-actin (Abcam, ab68477, 1:10,000, internal control), rabbit anti-Cyclin D1 (Abcam, ab134175, 1:10,000), mouse anti-Cyclin D3 (Abcam, ab289546, 1:1,000), and mouse anti-β-actin (Abcam, ab8226, 1:1,000, internal control).

    Techniques: Imaging, Immunofluorescence, Staining, Expressing

    Relative mRNA ( a ) and protein ( b ) level of key host cell proteins (ENO1, ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: Relative mRNA ( a ) and protein ( b ) level of key host cell proteins (ENO1, ACTG1, TUBB, and TUBA3D) in HCT-8 cell culture. The qPCR result is displayed after normalizing the Ct values with data from the GAPDH gene of HCT-8 cells. Data shown are mean ± SD from three replicate assays

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: Cell Culture

    Confirmation of the interactions between Cpgp40 and host protein ENO1. a Verification of recombinant protein expression in HEK293T cells. b Interactions between ENO1 and Cpgp40 in vivo as determined by coimmunoprecipitation. c Bimolecular fluorescence complementation (BiFC) assessing the interactions between ENO1 and Cpgp40 in live mammalian cells. A: positive control: pbJun-VN155 + pbFos-vc155. B: pBiFC-VC155-GP40 + pBiFC-VN155-ENO1. C: negative control: pbJun-VN155 + pbFos-vc155(delta ZIP). D: blank. (scale bar: 100 μm). The red arrow points to the fluorescent signal

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: Confirmation of the interactions between Cpgp40 and host protein ENO1. a Verification of recombinant protein expression in HEK293T cells. b Interactions between ENO1 and Cpgp40 in vivo as determined by coimmunoprecipitation. c Bimolecular fluorescence complementation (BiFC) assessing the interactions between ENO1 and Cpgp40 in live mammalian cells. A: positive control: pbJun-VN155 + pbFos-vc155. B: pBiFC-VC155-GP40 + pBiFC-VN155-ENO1. C: negative control: pbJun-VN155 + pbFos-vc155(delta ZIP). D: blank. (scale bar: 100 μm). The red arrow points to the fluorescent signal

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: Recombinant, Expressing, In Vivo, Fluorescence, Positive Control, Negative Control

    The silent efficiency detection of siRNA and inhibition of Cryptosporidium parvum invasion of HCT-8 cells by monoclonal ENO1 antibodies, siRNA, and overexpression of ENO1. a The silent efficiency detection of siRNA. GAPDH was used as an internal reference protein. b – d Inhibition of C. parvum invasion of HCT-8 cells. Human SSU rRNA gene was used as an internal control. Values are mean ± SEM. control: b PBS; c si-NC; d pcDNA3.1 blank vector

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: The silent efficiency detection of siRNA and inhibition of Cryptosporidium parvum invasion of HCT-8 cells by monoclonal ENO1 antibodies, siRNA, and overexpression of ENO1. a The silent efficiency detection of siRNA. GAPDH was used as an internal reference protein. b – d Inhibition of C. parvum invasion of HCT-8 cells. Human SSU rRNA gene was used as an internal control. Values are mean ± SEM. control: b PBS; c si-NC; d pcDNA3.1 blank vector

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: Inhibition, Over Expression, Plasmid Preparation

    Effects of Cryptosporidium parvum infection on the mRNA and protein levels of Occludin, Claudin 4, and E‐cadherin in HCT-8 cells in the presence of siENO1 ( a ) or pcDNA3.1-ENO1 ( b ) transfection

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: Effects of Cryptosporidium parvum infection on the mRNA and protein levels of Occludin, Claudin 4, and E‐cadherin in HCT-8 cells in the presence of siENO1 ( a ) or pcDNA3.1-ENO1 ( b ) transfection

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: Infection, Transfection

    Alignment of amino acid sequence and phylogenetic analysis of human ENO1 with other enolase sequences. a Alignment of amino acid sequence of human ENO1 and other species. The Mg2 + binding motifs are shown in a blue box, substrate-binding motifs are shown in a green box, plasminogen binding motifs are shown in a black box, and the enolase signature is shown in red box. The shade of the blue background represents the level of similarity. b Phylogenetic analysis of human ENO1 with other enolase sequences. The phylogenetic tree was constructed using the neighbor-joining method. The percentages of replicate trees in which the associated taxa clustered together in the bootstrap test (1000 replicates) are shown next to the branches

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: Alignment of amino acid sequence and phylogenetic analysis of human ENO1 with other enolase sequences. a Alignment of amino acid sequence of human ENO1 and other species. The Mg2 + binding motifs are shown in a blue box, substrate-binding motifs are shown in a green box, plasminogen binding motifs are shown in a black box, and the enolase signature is shown in red box. The shade of the blue background represents the level of similarity. b Phylogenetic analysis of human ENO1 with other enolase sequences. The phylogenetic tree was constructed using the neighbor-joining method. The percentages of replicate trees in which the associated taxa clustered together in the bootstrap test (1000 replicates) are shown next to the branches

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: Sequencing, Binding Assay, Construct

    Effect of truncated ENO1 protein on the load of C. parvum in HCT-8 cells. a 3 h postinvasion and b 18 h postinvasion

    Journal: Parasites & Vectors

    Article Title: Identification of host protein ENO1 (alpha-enolase) interacting with Cryptosporidium parvum sporozoite surface protein, Cpgp40

    doi: 10.1186/s13071-024-06233-5

    Figure Lengend Snippet: Effect of truncated ENO1 protein on the load of C. parvum in HCT-8 cells. a 3 h postinvasion and b 18 h postinvasion

    Article Snippet: The cell lysates were incubated with mouse anti-ENO1 antibody or anti-HA antibody (Abcam, UK) at 4 °C overnight, followed by antibody capture by Protein G agarose beads (Santa Cruz Biotechnology, CA) at 4 °C for 3 h. The agarose beads were then extensively washed with weak RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail and PBS containing 1 mM phenylmethylsulfonyl fluoride and protease inhibitor cocktail.

    Techniques: