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ATCC iec
Iec, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1281 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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iec - by Bioz Stars, 2026-03

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A, B The overexpression A and knockdown B efficiency of TIGAR in IEC-6 cells were assessed by western blot analysis. C, D IEC-6 cells with TIGAR overexpression C or knockdown D were cultured in the absence or presence of LPS (100 μg/mL) for 0-72 h, the cell viability at different time points was assessed by CCK8 assay ( n = 4 biological replicates). E–H IEC-6 cells with TIGAR overexpression E, G or knockdown F, H were cultured in the presence or absence of LPS for 5 days. Colony formation assays were subsequently performed to analyze cell growth. I-L IEC-6 cells with TIGAR overexpression I, K or knockdown J, L were cultured in the presence or absence of LPS for 24 h. The cell proliferation was detected using EdU assays. Scale bars: 100 μm. M Protocol for creating intestinal-specific TIGAR knockout mice ( TIGAR f/f Vil1-Cre ). N TIGAR deletion in intestinal tissues was validated using western blot from TIGAR f/f Vil1-Cre and TIGAR f/f mice. O Intestinal organoids derived from TIGAR f/f or TIGAR f/f Vil1-Cre mice were cultured in the presence or absence of LPS (100 μg/mL) for 0-5 days. The variations in organoid growth were monitored and comparatively analyzed across distinct experimental groups. Scale bars: 100 μm. P–R Intestinal organoids derived from TIGAR f/f or TIGAR f/f Vil1-Cre mice were cultured in the presence or absence of LPS (100 μg/mL) for 48 h. The number of Ki67 + P , Brdu + Q and LGR5 + cells R were verified by immunofluorescence assay. Scale bars: 100 μm. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-way ANOVA C, D and One-way ANOVA G, H, K, L and P–R were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A, B The overexpression A and knockdown B efficiency of TIGAR in IEC-6 cells were assessed by western blot analysis. C, D IEC-6 cells with TIGAR overexpression C or knockdown D were cultured in the absence or presence of LPS (100 μg/mL) for 0-72 h, the cell viability at different time points was assessed by CCK8 assay ( n = 4 biological replicates). E–H IEC-6 cells with TIGAR overexpression E, G or knockdown F, H were cultured in the presence or absence of LPS for 5 days. Colony formation assays were subsequently performed to analyze cell growth. I-L IEC-6 cells with TIGAR overexpression I, K or knockdown J, L were cultured in the presence or absence of LPS for 24 h. The cell proliferation was detected using EdU assays. Scale bars: 100 μm. M Protocol for creating intestinal-specific TIGAR knockout mice ( TIGAR f/f Vil1-Cre ). N TIGAR deletion in intestinal tissues was validated using western blot from TIGAR f/f Vil1-Cre and TIGAR f/f mice. O Intestinal organoids derived from TIGAR f/f or TIGAR f/f Vil1-Cre mice were cultured in the presence or absence of LPS (100 μg/mL) for 0-5 days. The variations in organoid growth were monitored and comparatively analyzed across distinct experimental groups. Scale bars: 100 μm. P–R Intestinal organoids derived from TIGAR f/f or TIGAR f/f Vil1-Cre mice were cultured in the presence or absence of LPS (100 μg/mL) for 48 h. The number of Ki67 + P , Brdu + Q and LGR5 + cells R were verified by immunofluorescence assay. Scale bars: 100 μm. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-way ANOVA C, D and One-way ANOVA G, H, K, L and P–R were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: Over Expression, Knockdown, Western Blot, Cell Culture, CCK-8 Assay, Knock-Out, Derivative Assay, Immunofluorescence

$A Western blot analysis was performed to detect changes in β-catenin protein levels in the intestinal crypts of mice with burn sepsis on day 7. B The alterations in the nuclear and cytoplasmic distribution of β-catenin in intestinal crypt cells of mice with burn sepsis on day 7 were assessed using nucleocytoplasmic fractionation and western blot analysis. Fibrillarin (FBL) was used as the nuclear internal control and GAPDH served as the cytoplasmic internal control. C The expression levels of β-catenin were evaluated by western blot analysis in IEC-6 cells cultured with or without LPS (100 μg/mL) for 24 h. D, E After overexpression D and knockdown E of TIGAR in IEC-6 cells, the protein levels of β-catenin were verified by western blot. F After the overexpression of TIGAR in IEC-6 cells, nuclear-cytoplasmic fractionation was conducted, followed by western blot analysis to assess alterations in the subcellular distribution of β-catenin. G Immunofluorescence was employed to assess the nuclear translocation of β-catenin following TIGAR overexpression in IEC-6 cells. H, I Nuclear-cytoplasmic fractionation H and immunofluorescence I were performed to assess the nuclear translocation of β-catenin in vector and TIGAR-overexpressing IEC-6 cells cultured in the presence or absence of LPS (100 μg/mL) for 24 h. J, K Nuclear-cytoplasmic fractionation J and immunofluorescence K were performed to assess the nuclear translocation of β-catenin in shNC and TIGAR knockdown IEC-6 cells. L Immunoprecipitation analysis of the interaction of β-catenin with TCF4 by the corresponding antibodies in TIGAR overexpression (left) or knockdown (right) IEC-6 cells. M The specific inhibitor of β-catenin β-catenin-IN-7 (50 μM) and LPS (100 μg/mL) were co-administered to small intestinal organoids for 48 h, and the morphological and growth changes of the organoids were quantitatively assessed under an optical microscope. Scale bars: 100 μm. N, O β-catenin-IN-7 and LPS were co-administered to small intestinal organoids for 48 h, the number of Ki67 + N and LGR5 + O cells were acquired through confocal microscopy. Scale bars: 100 μm. P IEC-6 cells overexpressing TIGAR were treated with LPS (100 μg/mL) and β-catenin-IN-7 (50 μM) for 24 h, followed by assessment of cell proliferation using the EdU assay. Scale bars: 100 μm. Q IEC-6 cells overexpressing TIGAR were treated with LPS and β-catenin-IN-7 for 5 days, the cell growth was detected by colony formation assay. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-sided paired Student’s t-test B, F, J and One-way ANOVA H, N–Q were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.$

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A Western blot analysis was performed to detect changes in β-catenin protein levels in the intestinal crypts of mice with burn sepsis on day 7. B The alterations in the nuclear and cytoplasmic distribution of β-catenin in intestinal crypt cells of mice with burn sepsis on day 7 were assessed using nucleocytoplasmic fractionation and western blot analysis. Fibrillarin (FBL) was used as the nuclear internal control and GAPDH served as the cytoplasmic internal control. C The expression levels of β-catenin were evaluated by western blot analysis in IEC-6 cells cultured with or without LPS (100 μg/mL) for 24 h. D, E After overexpression D and knockdown E of TIGAR in IEC-6 cells, the protein levels of β-catenin were verified by western blot. F After the overexpression of TIGAR in IEC-6 cells, nuclear-cytoplasmic fractionation was conducted, followed by western blot analysis to assess alterations in the subcellular distribution of β-catenin. G Immunofluorescence was employed to assess the nuclear translocation of β-catenin following TIGAR overexpression in IEC-6 cells. H, I Nuclear-cytoplasmic fractionation H and immunofluorescence I were performed to assess the nuclear translocation of β-catenin in vector and TIGAR-overexpressing IEC-6 cells cultured in the presence or absence of LPS (100 μg/mL) for 24 h. J, K Nuclear-cytoplasmic fractionation J and immunofluorescence K were performed to assess the nuclear translocation of β-catenin in shNC and TIGAR knockdown IEC-6 cells. L Immunoprecipitation analysis of the interaction of β-catenin with TCF4 by the corresponding antibodies in TIGAR overexpression (left) or knockdown (right) IEC-6 cells. M The specific inhibitor of β-catenin β-catenin-IN-7 (50 μM) and LPS (100 μg/mL) were co-administered to small intestinal organoids for 48 h, and the morphological and growth changes of the organoids were quantitatively assessed under an optical microscope. Scale bars: 100 μm. N, O β-catenin-IN-7 and LPS were co-administered to small intestinal organoids for 48 h, the number of Ki67 + N and LGR5 + O cells were acquired through confocal microscopy. Scale bars: 100 μm. P IEC-6 cells overexpressing TIGAR were treated with LPS (100 μg/mL) and β-catenin-IN-7 (50 μM) for 24 h, followed by assessment of cell proliferation using the EdU assay. Scale bars: 100 μm. Q IEC-6 cells overexpressing TIGAR were treated with LPS and β-catenin-IN-7 for 5 days, the cell growth was detected by colony formation assay. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-sided paired Student’s t-test B, F, J and One-way ANOVA H, N–Q were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: Western Blot, Fractionation, Control, Expressing, Cell Culture, Over Expression, Knockdown, Immunofluorescence, Translocation Assay, Plasmid Preparation, Immunoprecipitation, Microscopy, Confocal Microscopy, EdU Assay, Colony Assay

$A, B Volcano plot displaying metabolites differentially expressed in mice with burn sepsis on day1 A and day7 B . C–E Untargeted metabolomics revealed relative amounts of BHB from different samples: the intestinal tissues of Sham group and burn sepsis on day1, 3, 5 and 7 group mice C ( n = 6 mice); the TIGAR knockdown HIEC-6 D ( n = 4 biological replicates) and IEC-6 E ( n = 5 biological replicates) cells. F The Kbhb levels of total protein in intestinal crypt of normal and burn sepsis mice were validated using western blot assay. G After overexpression (left) and knockdown (right) of TIGAR in IEC-6 cells, the levels of Kbhb in total cellular protein were assessed by western blot. H IEC-6 cells were treated with different concentrations of BHB for 24 h, and the Kbhb levels of total protein were detected by western blot. I, J The Kbhb modification level of β-catenin was evaluated by immunoprecipitation followed by western blot analysis in IEC-6 cells treated with 20 mM BHB for 24 h, with TIGAR expression modulated through either knockdown I or overexpression J . K After the transfection of wild-type and six β-catenin mutants into HEK293T cells and treatment with 20 mM BHB for 24 h, the β-hydroxybutyrylation levels of β-catenin were assessed by immunoprecipitation followed by western blot analysis. L The wild-type and K335R mutant forms of β-catenin were transfected into HEK293T cells, followed by treatment with BHB for 24 h. Subcellular fractionation and western blot analyses were subsequently conducted to assess alterations in the nuclear and cytoplasmic distribution of β-catenin. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-sided paired Student’s t-test D, E and One-way ANOVA C were performed to assess statistical significance. ** p < 0.01, *** p < 0.001.$

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A, B Volcano plot displaying metabolites differentially expressed in mice with burn sepsis on day1 A and day7 B . C–E Untargeted metabolomics revealed relative amounts of BHB from different samples: the intestinal tissues of Sham group and burn sepsis on day1, 3, 5 and 7 group mice C ( n = 6 mice); the TIGAR knockdown HIEC-6 D ( n = 4 biological replicates) and IEC-6 E ( n = 5 biological replicates) cells. F The Kbhb levels of total protein in intestinal crypt of normal and burn sepsis mice were validated using western blot assay. G After overexpression (left) and knockdown (right) of TIGAR in IEC-6 cells, the levels of Kbhb in total cellular protein were assessed by western blot. H IEC-6 cells were treated with different concentrations of BHB for 24 h, and the Kbhb levels of total protein were detected by western blot. I, J The Kbhb modification level of β-catenin was evaluated by immunoprecipitation followed by western blot analysis in IEC-6 cells treated with 20 mM BHB for 24 h, with TIGAR expression modulated through either knockdown I or overexpression J . K After the transfection of wild-type and six β-catenin mutants into HEK293T cells and treatment with 20 mM BHB for 24 h, the β-hydroxybutyrylation levels of β-catenin were assessed by immunoprecipitation followed by western blot analysis. L The wild-type and K335R mutant forms of β-catenin were transfected into HEK293T cells, followed by treatment with BHB for 24 h. Subcellular fractionation and western blot analyses were subsequently conducted to assess alterations in the nuclear and cytoplasmic distribution of β-catenin. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-sided paired Student’s t-test D, E and One-way ANOVA C were performed to assess statistical significance. ** p < 0.01, *** p < 0.001.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: Knockdown, Western Blot, Over Expression, Modification, Immunoprecipitation, Expressing, Transfection, Mutagenesis, Fractionation

A–C The proliferation of IEC-6 cells following treatment with LPS (100 μg/mL) and BHB (20 mM) for 24 h was detected by CCK-8 A ( n = 4 biological replicates) and EdU B, C assay. Scale bars: 100 μm. D, E The proliferation of IEC-6 cells was evaluated using clone formation assays after treatment with LPS and BHB over a 5-day period. F, G The nuclear translocation of β-catenin was analyzed by nuclear-cytoplasmic separation and western blot in IEC-6 cells cultured with LPS and BHB for 24 h. H LPS and BHB were co-administered to IEC-6 cells for 24 h, immunofluorescence analysis was conducted to examine the nuclear and cytoplasmic distribution of β-catenin in cells. Scale bars: 25 μm. I, J The interaction of β-catenin and TCF4 in IEC-6 cells administered with LPS and BHB for 24 h was validated by immunoprecipitation and western blot. K LPS and BHB were co-administered to intestinal organoids for 48 h, and the growth and morphological changes of organoids were monitored. Scale bars: 100 μm. L–O LPS and BHB were co-administered to intestinal organoids for 48 h, the number of Ki67 + L, M and LGR5 + N, O cells was verified by immunofluorescence. Scale bars: 100 μm. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-way ANOVA A , One-way ANOVA C, E, G, J and Two-sided paried Student’s t-test M, O were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A–C The proliferation of IEC-6 cells following treatment with LPS (100 μg/mL) and BHB (20 mM) for 24 h was detected by CCK-8 A ( n = 4 biological replicates) and EdU B, C assay. Scale bars: 100 μm. D, E The proliferation of IEC-6 cells was evaluated using clone formation assays after treatment with LPS and BHB over a 5-day period. F, G The nuclear translocation of β-catenin was analyzed by nuclear-cytoplasmic separation and western blot in IEC-6 cells cultured with LPS and BHB for 24 h. H LPS and BHB were co-administered to IEC-6 cells for 24 h, immunofluorescence analysis was conducted to examine the nuclear and cytoplasmic distribution of β-catenin in cells. Scale bars: 25 μm. I, J The interaction of β-catenin and TCF4 in IEC-6 cells administered with LPS and BHB for 24 h was validated by immunoprecipitation and western blot. K LPS and BHB were co-administered to intestinal organoids for 48 h, and the growth and morphological changes of organoids were monitored. Scale bars: 100 μm. L–O LPS and BHB were co-administered to intestinal organoids for 48 h, the number of Ki67 + L, M and LGR5 + N, O cells was verified by immunofluorescence. Scale bars: 100 μm. Data presented are representative of three independent experiments. The data are presented as mean ± SD. Two-way ANOVA A , One-way ANOVA C, E, G, J and Two-sided paried Student’s t-test M, O were performed to assess statistical significance. * p < 0.05, ** p < 0.01 , *** p < 0.001.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: CCK-8 Assay, Translocation Assay, Western Blot, Cell Culture, Immunofluorescence, Immunoprecipitation

A, B The protein levels of ketogenic enzymes in HIEC-6 A and IEC-6 B cells overexpressing and knockdown of TIGAR were detected by western blot. C The western blot assay was performed to validate the expression of HMGCL in TIGAR f/f and TIGAR f/f Vil1-Cre mice. D IEC-6 cells were administered with 100 μg/mL LPS for 24 h, the protein level of HMGCL was verified by western blot. E The expression of HMGCL in intestinal crypts of burn sepsis on different time points ( n = 3). F Immunofluorescence was used to detect the cellular distribution and expression of HMGCL in the small intestinal tissues of mice with burn sepsis. Scale bars: 50 μm. G, H The expression of HMGCL mRNA in intestinal crypts of burn sepsis on day7 G and overexpression and knockdown TIGAR IEC-6 cells H was assessed by qRT-PCR ( n = 3 biological replicates). I, J CHX (100 μg/mL) was added to the IEC-6 cells with TIGAR knockdown and overexpression I as well as LPS (100 μg/mL) treatment J , and the cells were collected at 0, 2, 4, and 8 h respectively. The protein level of HMGCL was detected by western blot. K The Biogrid database predicts proteins that may interact with TIGAR. L Co-immunoprecipitation was used to detect the interaction between endogenous TIGAR and HMGCL in IEC-6 cells. M Using Flag-TIGAR and His-HMGCL co-transfected into HEK293T cells, the interaction between TIGAR and HMGCL was assessed by co-immunoprecipitation and western blot assays. N The schematic diagram of TIGAR and HMGCL protein truncation mutant, red: PFK domain, green: mitochondrial location reported in the literature. O Co-transfected the full-length HMGCL and the truncated TIGAR into HEK293T cells. Immunoprecipitation analysis of the interaction of TIGAR with HMGCL by anti-His. P Co-transfected the full-length TIGAR and the truncated HMGCL into HEK293T cells. Immunoprecipitation analysis of the interaction of TIGAR with HMGCL by anti-Flag. Q TIGAR overexpression plasmid and HMGCL shRNA plasmid were co-transfected into IEC-6 cells, the cell proliferation was verified by EdU assay. Scale bars: 100 μm. Data presented are representative of three independent experiments. Two-sided paired Student’s t-test A–C, G , One-way ANOVA H, Q were performed to assess statistical significance. ns no significant, * p < 0.05, ** p < 0.01 , *** p < 0.001.

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A, B The protein levels of ketogenic enzymes in HIEC-6 A and IEC-6 B cells overexpressing and knockdown of TIGAR were detected by western blot. C The western blot assay was performed to validate the expression of HMGCL in TIGAR f/f and TIGAR f/f Vil1-Cre mice. D IEC-6 cells were administered with 100 μg/mL LPS for 24 h, the protein level of HMGCL was verified by western blot. E The expression of HMGCL in intestinal crypts of burn sepsis on different time points ( n = 3). F Immunofluorescence was used to detect the cellular distribution and expression of HMGCL in the small intestinal tissues of mice with burn sepsis. Scale bars: 50 μm. G, H The expression of HMGCL mRNA in intestinal crypts of burn sepsis on day7 G and overexpression and knockdown TIGAR IEC-6 cells H was assessed by qRT-PCR ( n = 3 biological replicates). I, J CHX (100 μg/mL) was added to the IEC-6 cells with TIGAR knockdown and overexpression I as well as LPS (100 μg/mL) treatment J , and the cells were collected at 0, 2, 4, and 8 h respectively. The protein level of HMGCL was detected by western blot. K The Biogrid database predicts proteins that may interact with TIGAR. L Co-immunoprecipitation was used to detect the interaction between endogenous TIGAR and HMGCL in IEC-6 cells. M Using Flag-TIGAR and His-HMGCL co-transfected into HEK293T cells, the interaction between TIGAR and HMGCL was assessed by co-immunoprecipitation and western blot assays. N The schematic diagram of TIGAR and HMGCL protein truncation mutant, red: PFK domain, green: mitochondrial location reported in the literature. O Co-transfected the full-length HMGCL and the truncated TIGAR into HEK293T cells. Immunoprecipitation analysis of the interaction of TIGAR with HMGCL by anti-His. P Co-transfected the full-length TIGAR and the truncated HMGCL into HEK293T cells. Immunoprecipitation analysis of the interaction of TIGAR with HMGCL by anti-Flag. Q TIGAR overexpression plasmid and HMGCL shRNA plasmid were co-transfected into IEC-6 cells, the cell proliferation was verified by EdU assay. Scale bars: 100 μm. Data presented are representative of three independent experiments. Two-sided paired Student’s t-test A–C, G , One-way ANOVA H, Q were performed to assess statistical significance. ns no significant, * p < 0.05, ** p < 0.01 , *** p < 0.001.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: Knockdown, Western Blot, Expressing, Immunofluorescence, Over Expression, Quantitative RT-PCR, Immunoprecipitation, Transfection, Mutagenesis, Plasmid Preparation, shRNA, EdU Assay

A Rapamycin (50 μM) was administered to IEC-6 cells for 6 h to induce autophagy, and the protein expression level of HMGCL was assessed via western blot analysis. B Stable TIGAR knockdown IEC-6 cells were treated with MG132 (20 μM) for 6 h and then HMGCL protein levels were analyzed by western blot analysis. C Using Flag-TIGAR, HA-Ub and His-HMGCL co-transfected into HEK293T cells, immunoprecipitation assay was performed to validate the ubiquitination of HMGCL. D HEK293T cells were transfected with the indicated plasmids. Ubiquitination assay was used to detect the ubiquitination level of His-HMGCL. E Predicting possible E3 ubiquitin ligases of HMGCL using the ubibrowse 2.0 database. F The expression of HMGCL was detected in Park2 overexpressing IEC-6 and HIEC-6 cells via western blot. G Co-transfected the Flag-Park2, His-HMGCL, HA-Ub wilt-type and mutants into HEK293T cells, immunoprecipitation assay was used to assess the ubiquitination level of His-HMGCL. H HEK293T cells were transfected with the Flag-Park2, His-HMGCL, TIGAR and HA-Ub K48 only plasmids. Immunoprecipitation assay was used to assess the ubiquitination level of His-HMGCL. I HEK293T cells were transfected with the Flag-Park2, His-HMGCL wild type and truncated plasmids. The interaction between Park2 and HMGCL was validated by co-immunoprecipitation assay. J HEK293T cells were co-transfected with Flag-Park2, His-HMGCL, and TIGAR plasmids. The interaction between Park2 and HMGCL was confirmed through co-immunoprecipitation assay. Data presented are representative of three independent experiments.

Journal: Cell Death & Disease

Article Title: TIGAR maintains intestinal epithelial regeneration by stabilizing HMGCL and promoting β-catenin β-hydroxybutyrylation in burn-induced sepsis

doi: 10.1038/s41419-026-08486-7

Figure Lengend Snippet: A Rapamycin (50 μM) was administered to IEC-6 cells for 6 h to induce autophagy, and the protein expression level of HMGCL was assessed via western blot analysis. B Stable TIGAR knockdown IEC-6 cells were treated with MG132 (20 μM) for 6 h and then HMGCL protein levels were analyzed by western blot analysis. C Using Flag-TIGAR, HA-Ub and His-HMGCL co-transfected into HEK293T cells, immunoprecipitation assay was performed to validate the ubiquitination of HMGCL. D HEK293T cells were transfected with the indicated plasmids. Ubiquitination assay was used to detect the ubiquitination level of His-HMGCL. E Predicting possible E3 ubiquitin ligases of HMGCL using the ubibrowse 2.0 database. F The expression of HMGCL was detected in Park2 overexpressing IEC-6 and HIEC-6 cells via western blot. G Co-transfected the Flag-Park2, His-HMGCL, HA-Ub wilt-type and mutants into HEK293T cells, immunoprecipitation assay was used to assess the ubiquitination level of His-HMGCL. H HEK293T cells were transfected with the Flag-Park2, His-HMGCL, TIGAR and HA-Ub K48 only plasmids. Immunoprecipitation assay was used to assess the ubiquitination level of His-HMGCL. I HEK293T cells were transfected with the Flag-Park2, His-HMGCL wild type and truncated plasmids. The interaction between Park2 and HMGCL was validated by co-immunoprecipitation assay. J HEK293T cells were co-transfected with Flag-Park2, His-HMGCL, and TIGAR plasmids. The interaction between Park2 and HMGCL was confirmed through co-immunoprecipitation assay. Data presented are representative of three independent experiments.

Article Snippet: The intestinal epithelial cell line HIEC-6 and IEC-6, and HEK293T cells were obtained from the American Type Culture Collection (ATCC) (Manassas, USA).

Techniques: Expressing, Western Blot, Knockdown, Transfection, Immunoprecipitation, Ubiquitin Proteomics, Co-Immunoprecipitation Assay

(A-E) Multi-step growth curves and EMCV cytopathology in intestinal cells. Cells were infected at an MOI = 0.001 and harvested daily for 7 days. Cells shown are (A) HIEC-6 (human small intestinal enterocytes), (B) CMT-93 (House mouse large intestinal/rectal carcinoma cells), and (C) IEC-18 (Norway rat small intestinal [ileum] epithelial cells). Note EMCV infection in rat intestinal cells is non-cytolytic, in contrast to human and mouse cells. Scale bar = 100µm; (D) An overlay between the three cell lines highlights the reduced replication kinetics observed in rat intestinal cells over time; (E) Growth curves in IEC-18 cells infected with an MOI = 0.001 or 0.1 of EMCV over a 30-day period. Similar to the 7-day growth curve, EMCV infection in IEC-18 cells shows no cytopathology over the course of 30 days and infection is ultimately cleared from cells; (F) Multi-step growth curves in kidney cells from various hosts. Cell lines shown are BHK (Syrian golden hamster), OK (Virginia opossum), Vero E6 (African green monkey), MDCK (domestic dog), and Efk3B (big brown bat). Both BHK and Vero E6 cells, which are defective in interferon production [ , ], are routinely used in viral diagnostics for EMCV. Note a host restriction for EMCV in dog kidney and big brown bat kidney cells. An overlay of growth curves is shown to highlight the differences of titers in various kidney cell lines. Image was created, in part, using BioRender (Allison, A. [2026] https://BioRender.com/umgiypr ).

Journal: PLOS Pathogens

Article Title: Zoological transmission of encephalomyocarditis virus in the United States: Virus evolution, host ecology, and capsid antigenicity derived from an outbreak

doi: 10.1371/journal.ppat.1013861

Figure Lengend Snippet: (A-E) Multi-step growth curves and EMCV cytopathology in intestinal cells. Cells were infected at an MOI = 0.001 and harvested daily for 7 days. Cells shown are (A) HIEC-6 (human small intestinal enterocytes), (B) CMT-93 (House mouse large intestinal/rectal carcinoma cells), and (C) IEC-18 (Norway rat small intestinal [ileum] epithelial cells). Note EMCV infection in rat intestinal cells is non-cytolytic, in contrast to human and mouse cells. Scale bar = 100µm; (D) An overlay between the three cell lines highlights the reduced replication kinetics observed in rat intestinal cells over time; (E) Growth curves in IEC-18 cells infected with an MOI = 0.001 or 0.1 of EMCV over a 30-day period. Similar to the 7-day growth curve, EMCV infection in IEC-18 cells shows no cytopathology over the course of 30 days and infection is ultimately cleared from cells; (F) Multi-step growth curves in kidney cells from various hosts. Cell lines shown are BHK (Syrian golden hamster), OK (Virginia opossum), Vero E6 (African green monkey), MDCK (domestic dog), and Efk3B (big brown bat). Both BHK and Vero E6 cells, which are defective in interferon production [ , ], are routinely used in viral diagnostics for EMCV. Note a host restriction for EMCV in dog kidney and big brown bat kidney cells. An overlay of growth curves is shown to highlight the differences of titers in various kidney cell lines. Image was created, in part, using BioRender (Allison, A. [2026] https://BioRender.com/umgiypr ).

Article Snippet: During the 2019 outbreak and up to post-outbreak Oct 2020, a subset of 40 qRT-PCR-positive samples were subsequently shipped to the University of Florida and tested for virus isolation in cell culture using the protocols listed above, with the addition of IEC-18 (Norway rat [ Rattus norvegicus ] ileum) cells (ATCC).

Techniques: Infection

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