Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: FGF21 is regulated by the nutritional status in fed, fasted and diet-induced obesity (DIO). Fasting reduced FGF21 mRNA in whole pancreas (A). β-klotho, the co-receptor of FGF21, is expressed in the pancreas and is inversely regulated by fasting (B). FGF21 protein was only detected in pancreas compared to liver and inguinal white adipose tissue (IWAT) (C). Pancreas FGF21 protein level was reduced by fasting in both chow fed and high fat diet fed conditions (D, E). Separation of pancreatic fractions to evaluate the individual contribution of islets and acinar tissue on FGF21 expression show that acinar pancreas contributes to the majority of FGF21 levels while islet cells have very low FGF21 levels and are not nutritionally regulated (F). Acinar expression of FGF21 is regulated with fasting (F, G). n = 6 per group. Each western blot lane represents an individual animal.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques: Expressing, Western Blot

Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: Acute FGF21 exposure induces ERK1/2 signaling events therefore phosphorylation of ERK1/2 (pERK1/2) has been chosen as a marker of FGF21 signaling. Up to 50% of acinar cells show strong nuclear pERK1/2 staining (brown) after FGF21 administration (A i, iii). Islets represent a very unique pattern with pERK1/2 only on the peripheral cells (A ii, iv). Percentage of pERK1/2-labeled acinar cells with saline and FGF21 administration (B). Western blot of pERK1/2 and total ERK1/2 from the same pancreas samples (C). Epididymal white adipose tissue (EWAT) is a positive control for FGF21 signaling (C). S = saline and F = FGF21. Confocal photomicrographs show FGF21-induced pERK1/2 immunoreactivity in islets (D). Absence of pERK1/2 staining (green) after saline treatment (Di; Inset , islet outline is indicated by insulin-immunoreactivity shown in red). FGF21 did not elicit pERK1/2 in insulin (red)-producing β-cells (D ii). Merged images show pERK1/2 co-localization in glucagon-positive α cells (D iii) and somatostatin-positive δ cell (D iv). Split panels show glucagon (iii a ) and pERK (iii b ) labeling or somatostatin (iv a ) and pERK (iv b ) labeling in single cells. A robust and specific pERK1/2 staining was observed in almost 10% of total islet nuclei mostly at the periphery. Outlined region (dashed line) in the inset indicates the region represented in each panel. Representative pERK1/2 labelled cells are indicated by white arrows. n = 4 per group. Scale: 200 μm, A; 20 μm, D.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques: Phospho-proteomics, Marker, Staining, Labeling, Saline, Western Blot, Positive Control

Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: Chronic FGF21 treatment for 3 days by mini osmotic pumps led to the reduction in FGF21 expression in pancreas (A). FGF21 infusion down-regulated insulin but glucagon, somatostatin or amylase expression. While FGF21 infusion did not alter serum glucose levels (B), it reduced the serum levels of pancreatic hormones, insulin (C) and glucagon (D) without affecting the amylase activity (E). n = 10 per group.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques: Expressing, Activity Assay

Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: WT and FGF21 KO mice on chow diet have similar body weight (A), glucose tolerance (B) and insulin secretion in response to glucose (C), despite notable differences in their pancreatic morphology (D i, iii). After consuming high fat diet for 16 weeks, FGF21 KO mice (D iv) had increased islet hyperplasia compared with WT mice (D ii). Islet cell surface area was measured and represented (E). Islet cell proliferation markers were substantially over expressed in obese FGF21 KO animals (F). Islet hyperplasia leads to increased serum insulin (G) in FGF21 KO animals with a slight reduction in blood glucose (H) (n = 7 per group). Scale: 1 mm.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques:

Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: HFD consumption caused severe pancreatic inflammation in FGF21 KO mice (A). H&E staining showing, that compared to WT animals (i), FGF21 KO mice developed severe pancreatic periductal inflammation (outlined area in ii-iii) when consuming a HFD diet for 16 weeks. Lymphocytic nature of inflammatory cells is shown in a higher magnification image (iii). (B) Immunohistochemical analysis for the lymphocytic marker CD3 on the pancreas of WT (i) and FGF21 KO animals (ii-iii) is represented. FGF21 KO showed higher number of CD3, T cell receptor antigen. n = 7 per group. Scale: 1 mm, Ai-ii; 2 mm, Bi-ii; 200 μm, iii.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques: Staining, Immunohistochemical staining, Marker

Journal: PLoS ONE

Article Title: Fibroblast Growth Factor 21 (FGF21) Protects against High Fat Diet Induced Inflammation and Islet Hyperplasia in Pancreas

doi: 10.1371/journal.pone.0148252

Figure Lengend Snippet: (A) Representative cytofluorometric dot plots of isolated lymphocytes from WT and FGF21 KO animals consuming high fat diet for 16 weeks. FGF21 KO mice show elevated CD45+ (i), TCRb+ and Thy1+ T lymphocytes (ii) and Foxp3+ Treg cells. CD19+ B lymphocytes were not significantly altered (iii). Corresponding summary data is shown in the right panel. The experiment was repeated twice (n = 4 per group). (B) Gene expression analysis of cytokines is presented. n = 7 per group.

Article Snippet: Antibodies were purchased from commercial vendors: FGF21 (AF3057; R&D systems, Minneapolis, MN); Insulin (ab7842; Abcam, Cambridge, MA); β-actin (ab8226; Abcam); α -tubulin (ab7291; Abcam); pERK1/2 (4370; Cell Signaling Technology, Denver, MA); ERK1/2 (9107; Cell Signaling Technology); glucagon (2654; Sigma Aldrich, St. Louis, MO); somatostatin (sc7819; Santa Cruz, Dallas, TX); CD3 (MA1-90582; Thermo Scientific, Waltham, MA).

Techniques: Isolation, Gene Expression

Journal: Cell Metabolism

Article Title: GDF15 Provides an Endocrine Signal of Nutritional Stress in Mice and Humans

doi: 10.1016/j.cmet.2018.12.016

Figure Lengend Snippet: GDF15 Expression Is Regulated by the Cellular ISR Pathway (A and C) GDF15 mRNA expression (A) and immunoblot analysis (C) of ISR components in wild-type (WT) mouse embryonic fibroblasts (MEFs) treated with vehicle control (Con), cobalt chloride (CoCl2, 625 μM), thapsigargin (Tg, 1 μM), tunicamycin (Tn 5 μg/mL), or L-Histidinol (His, 1 mM) for 6 h. (B) GDF15 mRNA expression in human cell lines (HeLA, HuH7, and A549) treated with Tn (5 μg/mL) for 6 h. (D) GDF15 mRNA expression in WT MEFs pre-treated for 1 h either with the PERK inhibitor GSK2606414 (GSK, 200 nM) or eIF2α inhibitor ISRIB (ISR, 100 nM), then co-treated with Tn (5 μg/mL) for a further 6 h. (E–G) GDF15 mRNA expression (E) in EIF2α Ser51 (SS) or phospho mutant (AA) MEFs or (F) in ATF4 wild-type (WT) or ATF4 knockout (KO) MEFs and (G) in control siRNA and CHOP siRNA transfected WT MEFs treated with Tn (5 μg/mL) for 6 h. (H) Diagram outlining pathway by which GDF15 and FGF21 expression is regulated by TN. mRNA expression is presented as fold expression relative to its respective control treatment for each cell type (set at 1) or TN-treated samples (set as 100) with normalization to HPRT gene expression in MEFs and GAPDH in human cells. Data are expressed as mean ± SD from at least three independent experiments. ∗∗∗ p < 0.001 versus control (con) for (A) and (B), and versus TN stimulated for (D)–(G) by two-tailed Student’s t test. Blots shown are representative of three independent experiments with Calnexin used as a loading control. See also Figures S3 and .

Article Snippet: Mouse FGF21 was analyzed by FGF21 Quantakine ELISA (R&D Systems) following the manufacturer’s instructions.

Techniques: Expressing, Western Blot, Control, Mutagenesis, Knock-Out, Transfection, Gene Expression, Two Tailed Test

Journal: Cell Metabolism

Article Title: GDF15 Provides an Endocrine Signal of Nutritional Stress in Mice and Humans

doi: 10.1016/j.cmet.2018.12.016

Figure Lengend Snippet:

Article Snippet: Mouse FGF21 was analyzed by FGF21 Quantakine ELISA (R&D Systems) following the manufacturer’s instructions.

Techniques: Recombinant, SYBR Green Assay, Protease Inhibitor, Reverse Transcription, Western Blot, Injection, Enzyme-linked Immunosorbent Assay, Control, TaqMan Assay, Software, Sterility, Electrophoresis, Real-time Polymerase Chain Reaction

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Construction, purification, and characterization of FGF21-164. ( A ) FGF21-164 sequence and FGF21 sequence. In the FGF21-164 sequence, red marked the mutated amino acid and blue represents the TR acid sequence from hCD164. In the FGF21 sequence, the red-labeled amino acid represents the amino acid sequence whose n-terminal is deleted in FGF21-164. ( B ) Subcloned cell culture supernatants expressing FGF21-164 and FGF21 were analyzed using Western blotting (Lane M: molecular weight marker. Lane 1~7: FGF21-164 clones 1, 2, 3, A4, B2, F3, and H4. Line 8: FGF21 clone2). ( C ) The purified FGF21-164 and FGF21 were assayed using SDS-PAGE and Western blotting (Lane M: molecular weight marker. Lane 1: purified FGF21-164. Line 2: purified FGF21). ( D ) Purity and hydrodynamic radius of FGF21-164 were analyzed using SEC-HPLC. ( E ) MALDI-TOF mass-spectrometry analysis of FGF21-164. ([M + H] + denotes the singly charged ionic forms, and [M + 2H] 2+ denotes doubly charged ionic forms). ( F ) Circular Dichroism (CD) spectra of FGF21-164 and FGF21.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques: Purification, Sequencing, Labeling, Cell Culture, Expressing, Western Blot, Molecular Weight, Marker, Clone Assay, SDS Page, Mass Spectrometry, Circular Dichroism

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Glycan forms analysis of the protein FGF21-164. ( A ) O-linked glycan forms of FGF21-164. ( B ) N-linked glycan forms of FGF21-164.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Effect of FGF21-164 in adipocytes induced by 3T3-L1. ( A ) The process of inducing 3T3-L1’s differentiation into adipocytes. ( B ) Reduction in glucose in medium stimulated by FGF21-164 in adipocytes induced by 3T3-L1. Data are means ± SEM (n = 6). * p < 0.05, *** p < 0.001, and **** p < 0.0001 compared to 0 μg/mL FGF21-164. ( C ) Phospho-Erk1/2-specific bands (Thr202/Tyr204; 44–42 kDa) were detected in 3T3-L1-derived adipocytes after FGF21-164 stimulation. ( D ) Evaluation of lipid droplet accumulation in adipocytes induced by 3T3-L1 with or without FGF21-164. The scale bar represents 50 μm.Data are the means ± SEM (n = 6). * p < 0.05, **** p < 0.0001.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques: Derivative Assay

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Pharmacokinetics of FGF21-164. FGF21-164 plasma levels in C57BL/6 mice as determined via targeted LC-MS after i.v. (tail vein) bolus injection of FGF21-164 protein.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques: Liquid Chromatography with Mass Spectroscopy, Injection

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: The results of an oral glucose tolerance test applied to ob / ob mice after a single FGF21-164 treatment. ( A ) Blood glucose levels were measured at 0, 2, 3, 4, 5, 6, 7, and 8 h after the administration of FGF21-164. Data are the means ± SEM (n = 4–5). * p < 0.05 and ** p < 0.01 compared with the model. ( B ) The decrease in blood glucose levels post-administration relative to the baseline measurement at 0 h. Data are the means ± SEM (n = 4–5). * p < 0.05 compared with the model.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Effect of a single administration of FGF21-164 on ob / ob mice. ( A , D , G ) Fasting glucose levels. Blood glucose levels were measured at 7, 21, and 28 days after a single dose of FGF21-164 was administered. Data are the means ± SEM (n = 4–5). ns: no significance. * p < 0.05, ** p < 0.01, and **** p < 0.0001. ( B , E , H ) The OGTT at 7, 21, and 28 days. After oral glucose administration, blood glucose levels were measured. Data are the means ± SEM (n = 4–5). * p < 0.05, *** p < 0.001, and **** p < 0.0001 at 6 mg·kg −1 vs. model. # p < 0.05, ## p < 0.01 and #### p < 0.0001 at 12 mg·kg −1 vs. model. ( C , F , I ) The glucose AUC during the OGTT process. Data are the means ± SEM (n = 4–5). ns: no significance. * p < 0.05, *** p < 0.001. ( J ) Body weight measured at 0, 7, 21, and 28 days. Data are the means ± SEM (n = 4–5). ns: no significance.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control

doi: 10.3390/ijms26062672

Figure Lengend Snippet: Effect of repeated administration of FGF21-164. ( A ) Body weight changes. The DIO mice were treated with PBS or FGF21-164 once every 2 days. Data are the means ± SEM (n = 5–7). **** p < 0.0001 vs. Ctrl. #### p < 0.0001 for FGF21-164 vs. the model. ( B ) The liver sections were stained with Oil-red-O. The scale bar represents 100 μm. DIO mice showed many red lipid droplets in hepatic tissue (indicated by the black arrow), while lipid droplet levels were lower after the FGF21-164 treatment.

Article Snippet: Here, we describe a novel human FGF21 analog, designated as FGF21-164, which was generated through fusion protein technology and co-encoded by a mutated FGF21 gene and the TR gene of hCD164.

Techniques: Staining

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: A Slco4c1 -/- mice were generated using Cas9/gRNA gene-editing techniques. Slco4c1 -/- mice were characterized by mouse tail genotyping ( B ), Western blot ( C ) and IF analyses ( D ). E The strategies for the establishment of Slco4c1 -/- and WT MASLD mice by feeding with GAN diet. F The percent of body weight (BW) changes in the GAN diet-fed Slco4c1 -/- mice ( n = 8 per time point) and WT mice ( n = 6 per time point). G The liver weights (LW) and the ratio of liver weights to body weights (LW/BW) in the GAN diet-fed Slco4c1 -/- mice ( n = 8) and WT mice ( n = 6). H WAT and BAT weights in the GAN diet-fed Slco4c1 -/- mice( n = 8) and WT mice ( n = 6). (I) serum ALT and AST levels in the GAN diet-fed Slco4c1 -/- mice( n = 8) and WT mice ( n = 6). J The levels of liver TG, FFA, and TC in the GAN diet-fed Slco4c1 -/- mice ( n = 8) and WT mice ( n = 6). K H&E (Scale bars:100 μm), Sirius red (Scale bars:100 μm), and Oil red O staining (Scale bars:50 μm) of liver sections from the GAN diet-fed WT ( n = 6) and Slco4c1 -/- ( n = 8) mice. L Liver histologic assessments of steatosis, lobular inflammation, hepatocyte ballooning, fibrosis and NAS score from the GAN diet-fed WT ( n = 6) and Slco4c1 -/- ( n = 8) mice. B: n = 3, biologically independent experiments, the results are similar. C , D An experiment was conducted on mice identified in Figure2B, yielding results consistent with those in Figure2B. F Plotted: mean ± SEM; Statistics: Multiple unpaired t test; *p < 0.05, ** p < 0.01, *** p < 0.001vs. the GAN diet-fed WT mice. G – J , L Each dot represents one mouse sample; Plotted: mean ± SD; Statistics: unpaired two-tailed Student’s t test; 95% confidence interval. *P < 0.05, ** p < 0.01, *** p < 0.001vs. the GAN diet-fed WT mice.

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Generated, Western Blot, Staining, Two Tailed Test

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: A Orthogonal Partial Least Squares Discriminant Analysis (OPLS-DA) of the lipidomic data from the livers of GAN diet-fed WT ( n = 6) and Slco4c1 -/- mice ( n = 6). B The lipid category ratios in mouse liver tissues. C The major components of liver lipid categories in the GAN diet-fed WT and Slco4c1 -/- mice. The relative levels of hepatic Fasn, Acc1, Scd1 mRNA transcripts ( D ) and protein expression ( E ) in the GAN diet-fed WT ( n = 6) and Slco4c1 -/- mice ( n = 8). F A diagram illustrates how SCLO4C1 inhibits lipid synthesis in the liver (Created with MedPeer (medpeer.cn). The relative levels of Fasn, Acc1, Scd1 mRNA transcripts ( G ) and protein expression ( H ) in primary mouse hepatocytes. The levels of TG ( I ) and TC ( J ) in primary mouse hepatocytes. K Oil red O staining in the BSA or PA-treated primary mouse hepatocytes from WT and Slco4c1 -/- mice. The relative levels of Fasn, Acc1, Scd1 mRNA transcripts ( L ) and protein expression ( M ) in different groups of HepG2 cells. The levels of TG ( N ) and TC ( O ) in different groups of HepG2 cells. P Oil red O staining of different groups of HepG2 cells. C The abscissa is the fold change after log2 conversion, and the ordinate is the lipid Sub Class. Each point in the figure represents a different lipid, the color of the point corresponds to different lipid Sub Class, and the size of the point is p after -log10 conversion. D , E Each dot represents one mouse sample; Plotted: mean ± SD; Statistics: unpaired two-tailed Student’s t test; 95% confidence interval. G n = 3 biologically independent experiments; Plotted: mean ± SD; Statistics: unpaired two-tailed Student’s t test; 95% confidence interval. H – P n = 3 biologically independent experiments; Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval. *p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. (PS Phosphatidylserine; PI Phosphatidylinositol; PG Phosphatidylglycerol; PE Phosphatidylethanolamine; PC Phosphatidylcholine; LPS Lyso-phosphatidylserine; LPG Lyso-phosphatidylglycerol; LPE Lyso-phosphatidylethanolamine; LPC Lyso-phosphatidylcholine; dMePE Dimethylphosphatidylethanolamine; SM Sphingomyelin; MGDG Monogalactosyldiacylglycerol; Cer Ceramides; DG Diglyceride).

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Expressing, Staining, Two Tailed Test

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: A Luminescence Diagram of the “Persistently Open” Fluorescent Probe Jat-cAMP: The fluorophore was chemically conjugated to cAMP to form the Jat-cAMP probe, which was used for visualizing the transport of cAMP by SLCO4C1 protein. B Chemical synthesis of the Jat-cAMP probe. C The 2D highlighted the key interaction sites. D The 3D depiction illustrated the spatial binding conformation. E The strategies for determining the importance of SLCO4C1 Gln463 in transporting cAMP. F The CCK-8 analysis of the impact of Jat-cAMP on the viability of HepG2 cells. ( n = 6 Biological replicates; Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval.) G , H Live cell imaging of Jat-cAMP treated HepG2 cells. I ELISA analyses of cAMP concentrations in different groups of primary mouse hepatocytes. J ELISA analyses of cAMP concentrations in liver tissues of the GAN diet-fed WT( n = 6) and Slco4c1 -/- mice( n = 8). K ELISA analyses of cAMP concentrations in serum samples of the GAN diet-fed WT( n = 6) and Slco4c1 -/- mice( n = 8). L Correlation between hepatic Slco4c1 mRNA transcripts and cAMP levels in the GAN-fed WT mice. (Person r, two-tailed, 95% confidence interval) ( M ) Relative levels of PKAc and p-Creb in different groups of primary mouse hepatocytes. N Relative Srebp1 mRNA transcripts in different groups of primary mouse hepatocytes. ( n = 6 Biological replicates; Plotted: mean ± SD; Statistics: unpaired two-tailed Student’s t test; 95% confidence interval.) O Relative Srebp1c protein levels in different groups of primary mouse hepatocytes. P Relative Epac1 protein levels in the different groups of primary mouse hepatocytes. H , I n = 5 Biological replicates; Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval. J-K: Each dot represents one mouse sample; Plotted: mean ± SD; Statistics: unpaired two-tailed Student’s t test; 95% confidence interval. *p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. M , O , P n = 3 per group, Biological replicates; Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval. * p < 0.05 vs. the BSA-treated cells from WT mice; # p < 0.05 vs. the PA-treated cells from WT mice. $ p < 0.05 vs. the BSA-treated cells from Slco4c1 -/- mice.

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Binding Assay, CCK-8 Assay, Live Cell Imaging, Enzyme-linked Immunosorbent Assay, Two Tailed Test

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: A Cytokines stimulated Slco4c1 mRNA transcription in primary mouse hepatocytes ( B ) FGF21 expression levels in different hepatic cell types. C Hepatic Fgf21 mRNA levels in GAN diet fed mice. D Correlation analysis between hepatic Fgf21 and Slco4c1 mRNA levels ( n = 6). E , F Treatment with FGF21 stimulated Slco4c1 mRNA and protein expression in primary mouse hepatocytes ( G ) Schematic illustration of the predicted transcription factors. H The predicted transcription factor mRNA transcripts in the FGF21-treated primary mouse hepatocytes. I , J Hepatic Egr1/2/3 mRNA transcripts and protein expression in the indicated groups of mice. (* p < 0.05, vs. Chow diet-WT) ( K ) Correlation between hepatic Slco4c1 and Egrs mRNA levels in the GAN diet-fed WT mice ( n = 6). L A diagram illustrating the potential EGRs binding sites in human SLCO4C1 proximal promoter and the reporter constructs. M Luciferase activities in 293 T cells co-transfected with truncated SLCO4C1 promoters with, or without, plasmids for EGRs overexpression. N A schematic diagram displayed the EGR1-binding site in the SLCO4C1 promoter and its mutant. O Luciferase activity in 293 T cells co-transfected with the mutant Slco4c1 promoter and the plasmid for EGR1 overexpression. Relative levels of Egr1 mRNA ( P ) and protein ( Q ) expression in primary mouse hepatocytes treated with, or without, an ERK/MAPK inhibitor, and after stimulated by FGF21 were examined. R ChIP assay revealed that FGF21 increased Egr1 binding to the Slco4c1 -59 promoters in primary mouse hepatocytes. Relative levels Slco4c1 mRNA (S) and protein (T) expression in primary mouse hepatocytes treated with, or without, an ERK/MAPK inhibitor, and after stimulated by FGF21 were examined. A n = 5 and M , O n = 3, Biological replicates; C , I , J Each dot represents one mouse sample; Statistics: unpaired two-tailed Student’s t test. R: n = 3 and E , F , H , P , Q , S , T n = 5, Biological replicates; Statistics: one-way ANOVA test, Multiple comparisons. *p < 0.05, * *p < 0.01, *** p < 0.001, **** p < 0.0001. F: * p < 0.05 vs. FGF21 0 μg/ml; # p < 0.05 vs. FGF21 0.1 μg/ml. Q, T: * p < 0.05 vs. FGF21 0 μg/ml; # p < 0.05 vs. FGF21 1 μg/ml. All data statistics are presented as mean ± SD and 95% confidence interval.

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Expressing, Binding Assay, Construct, Luciferase, Transfection, Over Expression, Mutagenesis, Activity Assay, Plasmid Preparation, Two Tailed Test

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: A Schematic illustrating of the experiment design of the GAN diet-induced MASL and MASH mouse models. B Bioluminescence images displayed the AAV8-mediated Slco4c1 expression in mice 12 weeks after inoculation. C The dynamic changes in body weights in the different groups of mice. (Plotted: mean ± SEM; Statistics: two-way ANOVA test, Multiple comparisons, 95% confidence interval.) D Liver weights and liver weight/body weight ratios (LW/BW) of MASL and MASH mice. E White and brown adipose tissue weights of MASL and MASH mice. H&E, Sirius red and Oil red O staining of liver tissue sections of MASL F and MASH ( G ) mice. Quantitative liver histologic assessment of the severity of MASL ( H ) and MASH ( I ) mice, including steatosis, lobular inflammation, hepatocyte ballooning, fibrosis and NAS score. The levels of serum ALT, AST ( J ) and TG, TC ( K ) in MASL and MASH mice. L Mice were injected with control virions or AAV8-TBG-Luciferase- Slco4c1 and their serum and hepatic cAMP levels were quantified using ELISA. M , N Western blot revealed that induction of Slco4c1 overexpression by injection with AAV8-TBG-Luciferase- Slco4c1 increased the relative levels of PKAc and p-Creb(S133) proteins ( M ), but decreased the relative levels of Srebp1 , Fasn , Acc1 , and Scd1 mRNA transcripts in the liver of mice, compared with that in the control mice ( N ). C – E , H – K n = 4 per group in MASL model. In MASH model, Chow diet group and GAN diet-AAV8-TBG-Luciferase-CTR group n = 5, AAV8-TBG-Luciferase- Slco4c1 group n = 6; D , E , H – K Each dot represents one mouse sample, Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval. *p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. L , N Chow diet group and GAN diet-AAV8-TBG-Luciferase-CTR group n = 9, AAV8-TBG-Luciferase- Slco4c1 group n = 10, each dot represents one mouse sample, Plotted: mean ± SD; Statistics: one-way ANOVA test, Multiple comparisons, 95% confidence interval. *p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. M: * P < 0.05 vs. the Chow diet group, # P < 0.05 vs. the GAN diet-AAV8-TBG-Luciferase-CTR group.

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Expressing, Staining, Injection, Control, Luciferase, Enzyme-linked Immunosorbent Assay, Western Blot, Over Expression

Journal: Nature Communications

Article Title: Hepatocyte SLCO4C1 is a cAMP uptake transporter for inhibiting lipogenesis and a therapeutic target for MASLD

doi: 10.1038/s41467-026-70729-0

Figure Lengend Snippet: During the pathogenic process, metabolic disorder stimulates FGF21 expression, which through its receptors, activates the ERK/MAPK signaling to induce EGR1 expression. The transcription factor of EGR1 binds to the SLCO4C1 promoter and up-regulates its expression in hepatocytes. The SLCO4C1 functions as a cAMP uptake transporter through the interaction of its Gln463 with cAMP, increasing intracellular cAMP levels that activate the PKA-CREB signaling to feedback down-regulate SREBP1 and downstream ACC1, FASN and SCD1 expression, inhibiting fatty acid synthesis. Accordingly, induction of SLCO4C1 overexpression by AAV8-mediated hepatic SLCO4C1 expression and/or increasing intracellular cAMP levels by the Forskolin treatment effectively prevent and mitigate the progression of MASLD. Therefore, SLCO4C1 is a therapeutic target for MASLD. Conceivably, our findings may aid in the design of therapeutic strategies for treating MASLD.

Article Snippet: Primary mouse hepatocytes were treated with FGF21 (1 μg/ml) or first treated with an inhibitor of the ERK/MAPK signaling (PD98059, 25 μM, MCE, New Jersey, USA, Cat: HY-12028) for 1 h and subsequently treated with FGF21.

Techniques: Expressing, Over Expression

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 2. Expression patterns of FGF21 and β‑klotho in skin following wounding. (A) Reverse‑transcription polymerase chain reaction analysis was used to analyze the expression of FGF21 and β‑klotho prior to and 3 h after wounding. Expression levels of (B) FGF21 and (C) β‑klotho were normalized against those of GAPDH. The experiments were repeated at least three times and values are expressed as the mean ± standard error of three replicates. ***P<0.001 vs. Con. Con, control.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Control

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 1. FGF21 expression patterns in a variety of mouse tissues. (A) Expression patterns of FGF21 were analyzed by reverse‑transcription polymerase chain reaction analysis. (B) FGF21 levels in A were normal ized against those of GAPDH. The experiments were repeated at least three times and values are expressed as the mean ± standard deviation of three replicates. **P<0.01; ***P<0.001 vs. heart FGF21 levels.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Standard Deviation

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 4. Polymerase chain reaction analysis confirmed that the FGF21 frag ment was successfully integrated into SMD1168 colonies. Lanes 1‑10 are colonies selected from a minimal dextrose plate. Yeast cells transfected with empty vector was used as a negative control. M, marker.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Polymerase Chain Reaction, Transfection, Plasmid Preparation, Negative Control, Marker

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 3. Gene synthesis of FGF21. PCR products of the gene FGF21. Lanes: M, 2000 DNA marker; 1, PCR reaction with primer pair P1/RP1; 2, PCR reaction with primer pair P2/RP2 using the PCR product from the previous cycle as a template; 3‑7, PCR reactions with primer pairs P3/RP3‑P7/RP7, respectively, using the PCR product from the previous round as a template. PCR, polymerase chain reaction.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Marker, Polymerase Chain Reaction

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 6. Effects of exogenous FGF21 treatment on the activation of cell migration and JNK phosphorylation levels. (A) Wound healing assay was performed to analyze the effects of FGF21 (100 ng/ml) in human fibroblasts under low‑glucose (5.5 mM) conditions. Scale bar, 0.05 µm. Magnification, 40x. (B) The cell migra tion distance was quantified from A. (C and D) Following 6 h culture, 100 ng/ml FGF21 was added to the culture medium and gently shaken. Phosphorylation levels of JNK were analyzed after 30 min of FGF21 stimulation. All experiments were performed after incubation with 5 µg/ml mitomycin‑C, an inhibitor of cell proliferation, for one day. Images were captured using an ImageQuant LAS 4000. Values are expressed as the mean ± standard error (n=10 for B and n=3 for D). *P<0.05 vs. control. p‑JNK, phosphorylated c‑Jun N‑terminal kinase; t‑JNK, total c‑Jun N‑terminal kinase; FGF, fibroblast growth factor; Con, control.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Activation Assay, Migration, Phospho-proteomics, Wound Healing Assay, Incubation, Control

Journal: Molecular medicine reports

Article Title: Expression and purification of FGF21 in Pichia pastoris and its effect on fibroblast-cell migration.

doi: 10.3892/mmr.2016.4942

Figure Lengend Snippet: Figure 5. Protein expression and purification of FGF21. (A) SDS‑PAGE analysis of supernatant of engineered P. pastoris cells and purified FGF21 protein. Lanes: 1, marker; 2, supernatant without transfection with the FGF21 overexpression vector; 3, supernatant after transfection; 4, purified protein. (B) Purified FGF21 protein was analyzed by western blotting using an Epson Perfection V700 photo scanner. Lanes: 1, protein in the supernatant after transfection; 2, purified protein. (C) The purity of recombinant FGF21 was analyzed by high‑performance liquid chromatography. FGF, fibroblast growth factor.

Article Snippet: Subsequently, cells were cultured for 72 h with addition of 0.8% methanol every 24 h. Proteins were separated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; Beyotime Institute of Biotechnology, Shanghai, China) and western blot analysis was performed using mouse anti-FGF21 monoclonal antibody (1:1,000; MAB25371; R&D Systems, Inc., Minneapolis, MN, USA) (18).

Techniques: Expressing, Purification, Marker, Transfection, Over Expression, Plasmid Preparation, Western Blot, Recombinant, High Performance Liquid Chromatography

Journal: Toxicology

Article Title: Alcoholic fatty liver is enhanced in CYP2A5 knockout mice: the role of the PPARα-FGF21 axis

doi: 10.1016/j.tox.2017.01.016

Figure Lengend Snippet: Chronic ethanol induces FGF21 in Cyp2a5+/+ mice but does not in Cyp2a5−/− mice. (A) Serum FGF21 (N=5). (B) Liver expression of FGF21 and PPARα by Western blotting analysis. (C) Quantitation of Western blots (N=4). *P<0.05, compared to Cyp2a5+/+ Control Group. Cont, Control; EtOH, Ethanol.

Article Snippet: Some mice were daily injected mouse recombinant FGF21 (rFGF21, purchased from Creative Biomart, Shirley, NY, USA) subcutaneously at 0.25 mg/kg body weight.

Techniques: Expressing, Western Blot, Quantitation Assay, Control

Journal: Toxicology

Article Title: Alcoholic fatty liver is enhanced in CYP2A5 knockout mice: the role of the PPARα-FGF21 axis

doi: 10.1016/j.tox.2017.01.016

Figure Lengend Snippet: Chronic ethanol induces FGF21 in Nrf2+/+ mice more than in Nrf2−/− mice. (A) Western blots. (B) Quantitation of Western blots (N=3). *P<0.05, compared to Nrf2+/+ Control Group; # P<0.05, compared to Nrf2−/− Control Group; & P<0.05, compared with Nrf2+/+ Ethanol group. Cont, Control; EtOH, Ethanol.

Article Snippet: Some mice were daily injected mouse recombinant FGF21 (rFGF21, purchased from Creative Biomart, Shirley, NY, USA) subcutaneously at 0.25 mg/kg body weight.

Techniques: Western Blot, Quantitation Assay, Control

Journal: Toxicology

Article Title: Alcoholic fatty liver is enhanced in CYP2A5 knockout mice: the role of the PPARα-FGF21 axis

doi: 10.1016/j.tox.2017.01.016

Figure Lengend Snippet: Recombinant FGF21 blunts ethanol-induced hypertriglyceridemia (HTG) in Pparα−/− mice. (A) Ethanol induction of FGF21 was blunted in Pparα−/− mice (N=5). (B) rFGF21 blunted ethanol-induced elevation of liver TG in WT mice but not in Pparα−/− mice (N=5). (C) rFGF21 blunted ethanol-induced HTG in Pparα−/− mice (N=5). (D) Ethanol induction of CYP2E1 and CYP2A5 was not affected in both Pparα+/+ and Pparα−/− mice (N=5). *P<0.05, compared to Control Group. # P<0.05, compared to WT Ethanol Group. $ P<0.05, compared to WT Control Group. ^ P<0.05, compared with PPARα KO Ethanol group. E+F, ethanol plus rFGF21; WT, wild-type; PPARα KO, Pparα−/−.

Article Snippet: Some mice were daily injected mouse recombinant FGF21 (rFGF21, purchased from Creative Biomart, Shirley, NY, USA) subcutaneously at 0.25 mg/kg body weight.

Techniques: Recombinant, Control

Journal: Toxicology

Article Title: Alcoholic fatty liver is enhanced in CYP2A5 knockout mice: the role of the PPARα-FGF21 axis

doi: 10.1016/j.tox.2017.01.016

Figure Lengend Snippet: Alcoholic fatty liver is enhanced in Fgf21alb-cre mice but is not in Fr1alb-cre mice. (A) Ethanol induction of FGF21 was blunted in Fgf21alb-cre mice but was not in Fr1alb-cre mice (N=5). (B) H&E staining in liver sections shows that alcoholic fatty liver was enhanced in Fgf21alb-cre mice but not in Fr1alb-cre mice. (C) Steatosis scores (N=5). (D) Liver TG contents (N=5). *P<0.05, compared to Fr1fl/fl Control Group. # P<0.05, compared to Fgf21fl/fl Ethanol Group. ^ P<0.05, compared with Fgf21fl/fl control group. $ P<0.05, compared to Fr1alb-cre Control Group. @ P<0.05, compared to Fr1alb-cre Control Group. Cont, Control; EtOH, Ethanol.

Article Snippet: Some mice were daily injected mouse recombinant FGF21 (rFGF21, purchased from Creative Biomart, Shirley, NY, USA) subcutaneously at 0.25 mg/kg body weight.

Techniques: Staining, Control

Journal: Toxicology

Article Title: Alcoholic fatty liver is enhanced in CYP2A5 knockout mice: the role of the PPARα-FGF21 axis

doi: 10.1016/j.tox.2017.01.016

Figure Lengend Snippet: Alcoholic fatty liver is more pronounced in Pparα−/−/Cyp2a5−/− mice than in Pparα+/+/Cyp2a5−/− mice. (A) Ethanol induction of FGF21 was blunted in Pparα−/−/Cyp2a5−/− mice (N=4). (B) H&E staining in liver sections shows that alcoholic fatty liver was more pronounced in Pparα−/−/Cyp2a5−/− mice than in Pparα+/+/Cyp2a5−/− mice. (C) Steatosis scores (N=5). (D) Liver TG contents (N=5). *P<0.05, compared to Pparα+/+/Cyp2a5−/− Control Group. # P<0.05, compared to Pparα−/−/Cyp2a5−/− Control Group. & P<0.05, compared to Pparα+/+/Cyp2a5−/− Ethanol Group. Cont, Control; EtOH, Ethanol.

Article Snippet: Some mice were daily injected mouse recombinant FGF21 (rFGF21, purchased from Creative Biomart, Shirley, NY, USA) subcutaneously at 0.25 mg/kg body weight.

Techniques: Staining, Control