mcd diet  (Inotiv)

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Targeting lanosterol synthase alleviates MASLD by promoting fatty acid catabolism

doi: 10.1007/s00018-026-06091-7

Figure Lengend Snippet: Heterozygous knockout of LSS alleviated MCD induced MASLD. ( a ) Liver H&E and Oil Red O staining of ND and MCD-fed WT and LSS +/− mice, ( b ) Liver H&E and Oil Red O staining of ND and MCD-fed WT mice with or without RO 48–8071 injection, ( c ) Plasma ALT and ( d ) Plasma AST of ND and MCD-fed WT and LSS +/− mice, ( e ) Plasma ALT and ( f ) Plasma AST of ND and MCD-fed WT mice with or without RO 48–8071 injection, ( g ) NASH score of ND and MCD-fed WT and LSS +/− mice, ( h ) NASH score of ND and MCD-fed WT mice with or without RO 48–8071 injection, ( i ) Quantification of liver Oil Red O staining of ND and MCD-fed WT and LSS +/− mice, ( j ) Quantification of liver Oil Red O staining of ND and MCD-fed WT mice with or without RO 48–8071 injection, ( k ) Liver LSS protein levels of WT and LSS +/− mice fed ND and MCD. N = 10 mice for each group. * p < 0.05, & p < 0.01, # p < 0.001

Article Snippet: Male eight-week-old WT mice were fed with ND or MCD diet for two weeks, with or without intraperitoneal injection of LSS inhibitor, RO48-8071 (MedChemExpress, NJ), at 10 mg/kg/day to confirm the role of LSS loss of function in MCD-induced liver injury model, with PBS serving as control.

Techniques: Knock-Out, Staining, Injection, Clinical Proteomics

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Targeting lanosterol synthase alleviates MASLD by promoting fatty acid catabolism

doi: 10.1007/s00018-026-06091-7

Figure Lengend Snippet: Heterozygous knockout of LSS alter the overall composition of lipid classes in MCD mouse model. ( a ) Hepatic TG, ( b ) Tc, ( c ) HDLc and ( d ) LDLc of ND and MCD-fed WT and LSS +/− mice. ( e ) Hepatic TG, ( f ) Tc, ( g ) HDLc and ( h ) LDLc of of ND and MCD-fed WT mice with or without RO 48–8071 injection. ( i ) The relative contents of DGs, ( j ) PCs, ( k ) PIs, and ( l ) TGs in livers of ND and MCD -fed WT and LSS +/− mice. N = 10 mice for each group. * p < 0.05, & p < 0.01, # p < 0.001

Article Snippet: Male eight-week-old WT mice were fed with ND or MCD diet for two weeks, with or without intraperitoneal injection of LSS inhibitor, RO48-8071 (MedChemExpress, NJ), at 10 mg/kg/day to confirm the role of LSS loss of function in MCD-induced liver injury model, with PBS serving as control.

Techniques: Knock-Out, Injection

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Targeting lanosterol synthase alleviates MASLD by promoting fatty acid catabolism

doi: 10.1007/s00018-026-06091-7

Figure Lengend Snippet: Heterozygous knockout of LSS changed the expression of numerous genes in mice livers. ( a ) Volcano plot of RNAseq, ( b ) Pathway enrichment analysis of RNAseq, ( c ) Differentially expressed genes involved in ketone bodies metabolism and associated pathways between ND-fed WT and LSS +/− mice, and ( d ) between MCD-fed WT and LSS +/− mice. ( e ) Differentially expressed genes involved in fatty acid degradation and associated pathways between ND-fed WT and LSS +/− mice, and ( f ) between MCD-fed WT and LSS +/− mice. ( g ) Location of differentially expressed genes between ND-fed WT and LSS +/− mice, and ( h ) between MCD-fed WT and LSS +/− mice in the metabolic process of ketone bodies synthesis and degradation. ( i ) Location of differentially expressed genes between ND-fed WT and LSS +/− mice, and ( i ) between MCD-fed WT and LSS +/− mice in the metabolic process of fatty acid degradation. N = 3 mice for each group. CONW: ND-fed WT mice, CONK: ND-fed WT and LSS +/− mice, MW: MCD-fed WT mice, MK: M CD-fed LSS +/− mice

Article Snippet: Male eight-week-old WT mice were fed with ND or MCD diet for two weeks, with or without intraperitoneal injection of LSS inhibitor, RO48-8071 (MedChemExpress, NJ), at 10 mg/kg/day to confirm the role of LSS loss of function in MCD-induced liver injury model, with PBS serving as control.

Techniques: Knock-Out, Expressing, RNA sequencing

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Targeting lanosterol synthase alleviates MASLD by promoting fatty acid catabolism

doi: 10.1007/s00018-026-06091-7

Figure Lengend Snippet: Heterozygous knockout of LSS activated β-oxidation and ketonebodies synthesis in MASLD mice models. ( a ) Liver mRNA levels of interested genes involved in ketogenesis and fatty acid catabolism of ND and MCD-fed WT and LSS +/− mice. ( b ) Expression level of fatty acid β-oxidation and ketogenesis key enzymes and activities of AKT signaling pathway in liver lysates of ND and MCD-fed WT and LSS +/− mice, ( c ) Serum ketone bodies levels of ND and MCD-fed WT mice with or without RO48-8071 injection, ( d ) Serum ketone bodies levels of ND and MCD-fed WT and LSS +/− mice, ( e ) Liver mitochondrial ultrastructures of ND and MCD-fed WT and LSS +/− mice (The arrows point to pathologic structural features), ( f ) Serum ketone bodies levels of MASLD patients and control. N = 10 mice for each group. * p < 0.05, & p < 0.01, # p < 0.001

Article Snippet: Male eight-week-old WT mice were fed with ND or MCD diet for two weeks, with or without intraperitoneal injection of LSS inhibitor, RO48-8071 (MedChemExpress, NJ), at 10 mg/kg/day to confirm the role of LSS loss of function in MCD-induced liver injury model, with PBS serving as control.

Techniques: Knock-Out, Expressing, Injection, Control

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Targeting lanosterol synthase alleviates MASLD by promoting fatty acid catabolism

doi: 10.1007/s00018-026-06091-7

Figure Lengend Snippet: LSS loss of function alleviated MCDE induced cellular steatosis by activating β-oxidation and ketonebodies synthesis. ( a ) LSS shRNA transfection efficiency detected using GFP reporter, ( b ) LSS knockdown efficiency detected using Western blot analysis, ( c ) H&E and Oil Red O staining of primary hepatocytes isolated from ND and MCD-fed WT and LSS +/− mice, ( d ) H&E and Oil Red O staining of DMEM and MCDE cultured HepG2 cells transfected with LSS shRNA or sramble shRNA, ( e ) mRNA levels of interested genes involved in ketogenesis and fatty acid catabolism in DMEM and MCDE cultured HepG2 cells transfected with LSS shRNA or sramble shRNA, ( f ) Quantification of Oil Red O staining of primary hepatocytes isolated from ND and MCD-fed WT and LSS +/− mice, ( g ) Quantification of Oil Red O staining of DMEM and MCDE cultured HepG2 cells transfected with LSS shRNA or sramble shRNA, ( h ) Ketone bodies levels in DMEM and MCDE cultured HepG2 cells transfected with LSS shRNA or sramble shRNA, ( i ) Protein levels of fatty acid β-oxidation and ketogenesis key enzymes in DMEM and MCDE cultured HepG2 cells transfected with LSS shRNA or sramble shRNA. * p < 0.05, & p < 0.01, # p < 0.001

Article Snippet: Male eight-week-old WT mice were fed with ND or MCD diet for two weeks, with or without intraperitoneal injection of LSS inhibitor, RO48-8071 (MedChemExpress, NJ), at 10 mg/kg/day to confirm the role of LSS loss of function in MCD-induced liver injury model, with PBS serving as control.

Techniques: shRNA, Transfection, Knockdown, Western Blot, Staining, Isolation, Cell Culture

Journal: International Journal of Biological Sciences

Article Title: TM4SF5-mediated KEAP1 Regulation in Hepatocytes Irrelevant to NRF2 Expression and Activity Promotes Oxidative Stress and Inflammation to Develop Metabolic Dysfunction-Associated Steatotic Liver Disease

doi: 10.7150/ijbs.126251

Figure Lengend Snippet: Keap1 downregulation reverses TM4SF5-driven, MASH-associated fibrosis upon MCD diet. (A-D) WT, Alb -TG Tm4sf5-Flag , and Tm4sf5 -/- KO C57BL/6 male mice (n=4~5, 8-week-old) were maintained on an MCD diet for 3.5 weeks (A) and received intravenous injections of either PBS or siKeap1 (0.02 mg/kg, twice a week) prior to sacrifice for subsequent hepatic analyses, including body and liver weight measurements (B), and evaluation through H&E, Masson's trichrome (M-T), Oil Red O (ORO), or dihydroethidium (DHE) staining, immunohistochemistry (C), or immunoblotting (D) for specified proteins. Scale bar: 100 μm. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ***, P < 0.0001; ns, non-significant, one-way ANOVA. All data are expressed as mean ± SEM.

Article Snippet: For positive control groups in the MASH model, mice were fed an MCD diet (TD90262, Teklad) for 4 weeks or a MASH diet (A06071302, CDAHFD, Research Diet Inc., New Brunswick, NJ, USA) with L-amino acid rodent formulation containing 60 kcal% fat, 0.1% methionine, and without choline for 12 weeks.

Techniques: Staining, Immunohistochemistry, Western Blot

Journal: The Journal of Biological Chemistry

Article Title: HuR-driven reversible mitochondrial shuttling buffers cytosolic miRNA levels in hepatic cells

doi: 10.1016/j.jbc.2026.111255

Figure Lengend Snippet: The starvation-induced enrichment of mito-miRs in hepatic cell mitochondria. A , fold change in cellular miRNA content after 16 h of amino acid starvation of Huh7 cells. Relative levels of various miRNAs were quantified using qRT–PCR. Data were normalized to U6 snRNA (n = 3). B , miRNA-specific Ct values are plotted to show the changes in their relative abundance in purified mitochondria after amino acid starvation of Huh7 cells. The analysis indicates a significant decrease in Ct values for miRNAs let-7b, let-7g, and miR-181a in starved cell mitochondria, reflecting their enrichment in the mitochondrial fraction on starvation. A bar diagram displays the fold enrichment of let-7b and let-7g mito-miRs in purified mitochondria compared with let-7a (n = 3). C , Western blot analysis done with fed and starved Huh7 extracts exhibited increased levels of expression of the stress marker protein phosphorylated–eukaryotic initiation factor 2 alpha and cleaved PARP, accompanied by decreased 4EBP1 (eukaryotic initiation factor 4E–binding protein 1) phosphorylation. β-actin served as the loading control for all samples. Relative levels, quantified from band intensity, are plotted at the bottom of Western blot panels against the beta-actin normalized value of Fed Huh7 cells as a unit. D , cellular miRNA levels change in the liver of mice under a normal diet (fed) and after 12h of starvation, as estimated by qRT–PCR and normalization against U6 snRNA levels (n = 3). E , the fold changes of let-7b and let-7g in the isolated pure mitochondrial fraction obtained from the liver of mice having a normal diet (fed) or starved for 12 h. Levels of each miRNA in the fed condition are considered as units (n = 3). F and G , the relative enrichment of mito-miRs with the outer membrane and intermembrane space (OM + IMS) ( F ) and inner membrane and mitochondrial matrix (IM + matrix) ( G ) of mitochondria isolated from control (fed) and 16 h amino acid–starved Huh7 cells (starved). Ct values are plotted (n = 6). H , fold change in mitochondrial miR-122 and let-7g levels in control and methionine/choline-deficient (MCD) diet–exposed animal’s liver mitochondria (n = 4). I , Western blot analysis ( left panel ) and relative quantification ( right panel ) of different proteins present in the mitochondrial fractions isolated from the control and MCD diet–exposed animal liver (n = 3). J , effect of thapsigargin (TG) on the expression of stress-responsive proteins in Huh7 cells determined by Western blot analysis. β-actin was used as a loading control. K – L , effect of TG treatment (2.5 micromolar;16 h) on cellular ( K ) and mitochondrial ( L ) miRNA content. Relative levels of miRNAs were measured and plotted. For cellular and mitochondrial samples, U6 and let-7a levels were used for normalization. Relative change in let-7a in mitochondrial fraction was determined from Ct values and plotted in L . Values at the control set were used as a unit (n = 3). M , cellular miR-122 levels increased, whereas its mitochondrial levels remained unchanged when cells were treated (10 micromolar, 24 h) with a pharmacological blocker of extracellular vesicle production, GW4869, a powerful, selective, noncompetitive inhibitor of neutral sphingomyelinase (N-SMase), an enzyme crucial for generating ceramide, which drives the formation and release of exosomes (extracellular vesicles) from cells . Normalization was done with U6 snRNA and let-7a for cellular and mitochondrial miR-122, respectively (n = 3). Statistically analyzed data are indicated as mean ± SD of three experiments, with statistical significance marked as ns (nonsignificant), ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001, calculated using two-tailed Student’s t test. PARP, poly(ADP-ribose) polymerase; qRT–PCR, quantitative RT–PCR.

Article Snippet: They were randomly assigned to two groups and fed either a standard chow or an MCD diet (MP Biomedicals; catalog no.: 0296043910) for 4 weeks.

Techniques: Quantitative RT-PCR, Purification, Western Blot, Expressing, Marker, Binding Assay, Phospho-proteomics, Control, Isolation, Membrane, Quantitative Proteomics, Two Tailed Test

Journal: bioRxiv

Article Title: Flexibility of systemic one-carbon metabolism partially buffers dietary methyl donor deficiency

doi: 10.64898/2026.02.05.703880

Figure Lengend Snippet: (a) Schematic showing intravenous infusion of [trimethyl- H 9 ]choline and [methyl- C 1 ]methionine in mice fed a methionine and choline deficient diet or fed a paired control diet. (b) Rate of appearance of choline calculated from m+9 serum enrichments from 8 h intravenous infusion of [trimethyl- H 9 ]choline. (c) Rate of appearance of methionine calculated from m+1 serum enrichments from 8 h intravenous infusion of [methyl- C 1 ]methionine. (d) Normalized labeling of tissue SAM from 8 hour intravenous infusion of [methyl- C 1 ]methionine. (e) Normalized labeling of tissue SAM from 8 hour intravenous infusion of [trimethyl- H 9 ]choline. The red line represents the fraction of serum methionine that is labeled in control conditions and the green line represents the fraction of serum methionine that is labeled in MCD diet. Labeling below these lines indicates that labeling is potentially sourced from serum methionine pools rather than tissue autonomous production. (f) Normalized labeling of pooled PCs in the liver from 8 hour intravenous infusion of [trimethyl- H 9 ]choline. (g) Ratio of ion counts of pooled PC species to pooled PE species. Bars represent mean ± S.D. Each data point represents data from an independent mouse. P-values were calculated with two-way ANOVA with Šídák correction for multiple comparisons. All experiments were performed in male ad lib fed C57Bl/6N mice during the light cycle. PC, phosphatidylcholine; PE, phosphatidylethanoline; PEMT, phosphatidylethanolamine methyltransferase

Article Snippet: Methyl deficiency was induced by transitioning mice from standard chow to a methionine and choline-deficient (MCD) diet (MP Biomedicals, MP296043910), while age-matched controls received a matched methionine and choline replete control diet (MP Biomedicals, MP296044110).

Techniques: Control, Labeling

Journal: bioRxiv

Article Title: Flexibility of systemic one-carbon metabolism partially buffers dietary methyl donor deficiency

doi: 10.64898/2026.02.05.703880

Figure Lengend Snippet: (a) Normalized labeling of serum and tissue serine from 8 hour intravenous infusion of [trimethyl- H 9 ]choline.The red line represents the fraction of serum serine that is labeled in control conditions and the green line represents the fraction of serum serine that is labeled in MCD diet. Labeling below these lines indicates that labeling is potentially sourced from serum serine pools rather than tissue autonomous production. (b) Relative ion counts for glycine across tissues in MCD diet and control diet fed mice. Bars represent mean ± S.D. Each data point represents data from an independent mouse. P-values were calculated with two-way ANOVA with Šídák correction for multiple comparisons (a) or Mixed-effects analysis with Šídák correction for multiple comparisons (b). All experiments were performed in male ad lib fed C57Bl/6N mice during the light cycle. MCD, methionine and choline deficient

Article Snippet: Methyl deficiency was induced by transitioning mice from standard chow to a methionine and choline-deficient (MCD) diet (MP Biomedicals, MP296043910), while age-matched controls received a matched methionine and choline replete control diet (MP Biomedicals, MP296044110).

Techniques: Labeling, Control

Journal: bioRxiv

Article Title: Flexibility of systemic one-carbon metabolism partially buffers dietary methyl donor deficiency

doi: 10.64898/2026.02.05.703880

Figure Lengend Snippet: (a) Schematic of the folate cycle highlighting reactions that support production of 5,10-methylene-THF and SAM. (b) Schematic showing intravenous infusion of [2,3,3- H 3 ]serine and [U- C ]glycine in mice fed a methionine and choline deficient diet or fed a paired control diet. (c) Rate of appearance of serine calculated from m+3 serum enrichments from 8 h intravenous infusion of [2,3,3- H 3 ]serine. (d) Rate of appearance of glycine calculated from m+2 serum enrichments from 8 h intravenous infusion of [U- C 2 ]glycine. (e) Schematic of use of [2,3,3- H 3 ]serine tracing to measure the contribution of the folate cycle to SAM synthesis. (f) Normalized labeling of tissue SAM from 8 hour intravenous infusion of [2,3,3- H 3 ]serine. The red line represents the fraction of serum methionine that is labeled in control conditions and the green line represents the fraction of serum methionine that is labeled in MCD diet. Labeling below these lines indicates that labeling is potentially sourced from serum methionine pools rather than tissue autonomous production. Bars represent mean ± S.D. Each data point represents data from an independent mouse. P-values were calculated with two tailed T-test (c,d) or two-way ANOVA with Šídák correction for multiple comparisons (f). All experiments were performed in male ad lib fed C57Bl/6N mice during the light cycle. MCD, methionine and choline deficient; SHMT, serine hydroxymethyltransferase, MTR, 5-methyltetrahyrofolate homocysteine methyltransferase; SAM, s-adenosylmethionine

Article Snippet: Methyl deficiency was induced by transitioning mice from standard chow to a methionine and choline-deficient (MCD) diet (MP Biomedicals, MP296043910), while age-matched controls received a matched methionine and choline replete control diet (MP Biomedicals, MP296044110).

Techniques: Control, Labeling, Two Tailed Test

Journal: bioRxiv

Article Title: Flexibility of systemic one-carbon metabolism partially buffers dietary methyl donor deficiency

doi: 10.64898/2026.02.05.703880

Figure Lengend Snippet: (a) Schematic showing potential sources of circulating serine. (b) Normalized labeled fraction of serum serine from infusion of [U- C 2 ]glycine. (c) Normalized labeled fraction of serum serine from infusion of [U- C 6 ]glucose. (d) Rate of appearance of essential amino acid phenylalanine from intravenous infusion of [ N]phenylalanine. (e) Serine production fluxes from different sources measured using the serine rate of appearance and infusions of U- C 2 ]glycine, U- C 6 ]glucose, and [ N]phenylalanine. (f) Relative ion counts for serine across tissues in MCD diet and control diet fed mice. (g) Schematic of proposed mechanism. When methionine and choline are deficient in the diet, there is increased release of serine from the kidney that supports maintained methionine, PC, and choline synthesis in the liver. Thus, methionine and choline fluxes are maintained by one-carbon metabolism buffering. Bars represent mean ± S.D. Each data point represents data from an independent mouse. P-values were calculated with two tailed T-test (b), two-way ANOVA with Šídák correction for multiple comparisons (e), or mixed-effects analysis with Šídák correction for multiple comparisons (f). All experiments were performed in male ad lib fed C57Bl/6N mice during the light cycle. SAM, s-adenosylmethionine; MCD, methionine and choline deficient

Article Snippet: Methyl deficiency was induced by transitioning mice from standard chow to a methionine and choline-deficient (MCD) diet (MP Biomedicals, MP296043910), while age-matched controls received a matched methionine and choline replete control diet (MP Biomedicals, MP296044110).

Techniques: Labeling, Control, Two Tailed Test

Journal: Journal of Clinical and Translational Hepatology

Article Title: Investigation of HO-1 Regulation of Liver Fibrosis Related to Nonalcoholic Fatty Liver Disease Through the SIRT1/TGF-ß/Smad3 Pathway

doi: 10.14218/JCTH.2024.00481

Figure Lengend Snippet: (A) liver /body weight. (B) Body weight. Serum (C) ALT and (D) AST in each group. (E) Images of H&E (×200 magnification) staining of representative liver sections and (F) the NAFLD activity score. (G) Images of Masson (×200 magnification) staining of representative liver sections and (H) the Metavir score. (I) Images of Sirius (×200 magnification) red staining of representative liver sections and (J) Relative collagen content (%). Values are the mean ± SD (n = 6 per group). * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. MCD, methionine-and-choline-deficient diet; NAFLD, nonalcoholic fatty liver disease; H&E, hematoxylin-eosin. ALT, alanine aminotransferase; AST, aspartate transaminase; Znpp, zincprotoporphyria.

Article Snippet: The mice were randomly divided into four groups (n = 6) and received group-specific diets for eight weeks: (1) Control group: Mice were fed a normal diet; (2) Methionine- and choline-deficient (MCD) group: Mice were fed an MCD diet (Research Diets, Inc., NJ, New Brunswick, USA); (3) Hemin group: Mice were fed an MCD diet and treated with the HO-1 chemical inducer Hemin three times per week; (4) Zinc protoporphyrin (Znpp) group: Mice were fed an MCD diet and treated with the HO-1 inhibitor Znpp three times per week.

Techniques: Staining, Activity Assay

Journal: Journal of Clinical and Translational Hepatology

Article Title: Investigation of HO-1 Regulation of Liver Fibrosis Related to Nonalcoholic Fatty Liver Disease Through the SIRT1/TGF-ß/Smad3 Pathway

doi: 10.14218/JCTH.2024.00481

Figure Lengend Snippet: (A–F) The expression levels of HO-1, SIRT1, TGF-β, Smad3, Collagen1 and α-SMA were measured by RT-qPCR. (G) Immunofluorescence (×200 magnification) double staining between of HO-1 and SIRT1 in liver tissue. (H–K) Immunofluorescence double staining semi-quantitative analysis. GAPDH served as the loading control. Data are presented as representative results of three independent experiments. Values are the mean ± SD (n = 6 per group). *** p < 0.001, **** p < 0.0001. MCD, methionine-and-choline-deficient diet; HO-1, heme oxygenase 1; SIRT1, Sirtuin 1; TGF-β, transforming growth factor beta; α-SMA, alpha-smooth muscle actin; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Znpp, zincprotoporphyria.

Article Snippet: The mice were randomly divided into four groups (n = 6) and received group-specific diets for eight weeks: (1) Control group: Mice were fed a normal diet; (2) Methionine- and choline-deficient (MCD) group: Mice were fed an MCD diet (Research Diets, Inc., NJ, New Brunswick, USA); (3) Hemin group: Mice were fed an MCD diet and treated with the HO-1 chemical inducer Hemin three times per week; (4) Zinc protoporphyrin (Znpp) group: Mice were fed an MCD diet and treated with the HO-1 inhibitor Znpp three times per week.

Techniques: Expressing, Quantitative RT-PCR, Immunofluorescence, Double Staining, Control

Journal: Journal of Clinical and Translational Hepatology

Article Title: Investigation of HO-1 Regulation of Liver Fibrosis Related to Nonalcoholic Fatty Liver Disease Through the SIRT1/TGF-ß/Smad3 Pathway

doi: 10.14218/JCTH.2024.00481

Figure Lengend Snippet: (A, C–G) Western blot analysis of HO-1, SIRT1, TGF-β, P-Smad2/3, and Smad2/3 in liver tissue. (B, H, I) Western blot analysis of α-SMA and Collagen1 in liver tissue. Values are the mean ± SD (n = 6 per group). ** p < 0.01, *** p < 0.001, **** p < 0.0001. MCD, methionine-and-choline-deficient diet; HO-1, heme oxygenase 1; SIRT1, Sirtuin 1; TGF-β, transforming growth factor beta; α-SMA, alpha-smooth muscle actin; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Znpp, zincprotoporphyria.

Article Snippet: The mice were randomly divided into four groups (n = 6) and received group-specific diets for eight weeks: (1) Control group: Mice were fed a normal diet; (2) Methionine- and choline-deficient (MCD) group: Mice were fed an MCD diet (Research Diets, Inc., NJ, New Brunswick, USA); (3) Hemin group: Mice were fed an MCD diet and treated with the HO-1 chemical inducer Hemin three times per week; (4) Zinc protoporphyrin (Znpp) group: Mice were fed an MCD diet and treated with the HO-1 inhibitor Znpp three times per week.

Techniques: Western Blot

Journal: Journal of Clinical and Translational Hepatology

Article Title: Investigation of HO-1 Regulation of Liver Fibrosis Related to Nonalcoholic Fatty Liver Disease Through the SIRT1/TGF-ß/Smad3 Pathway

doi: 10.14218/JCTH.2024.00481

Figure Lengend Snippet: (A, B) Western blot analysis of HO-1 overexpression and silencing in LX2 cells. (C, D) Western blot analysis of LX2 cells treated with SIRT1 activators and inhibitors. (E–I) Western blot analysis of SIRT1, TGF-β, P-Smad2/3, Smad2/3 in LX2 cells. (J–L) Western blot analysis of α-SMA and Collagen I in LX2 cells. Values are the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. MCD, methionine-and-choline-deficient diet; HO-1, heme oxygenase 1; SIRT1, Sirtuin 1; TGF-β, transforming growth factor beta; α-SMA, alpha-smooth muscle actin; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; OE HO-1, overexpressing HO-1; SiHO-1, small interfering RNA silencing of HO-1.

Article Snippet: The mice were randomly divided into four groups (n = 6) and received group-specific diets for eight weeks: (1) Control group: Mice were fed a normal diet; (2) Methionine- and choline-deficient (MCD) group: Mice were fed an MCD diet (Research Diets, Inc., NJ, New Brunswick, USA); (3) Hemin group: Mice were fed an MCD diet and treated with the HO-1 chemical inducer Hemin three times per week; (4) Zinc protoporphyrin (Znpp) group: Mice were fed an MCD diet and treated with the HO-1 inhibitor Znpp three times per week.

Techniques: Western Blot, Over Expression, Small Interfering RNA