fgf1 growth factor  (PeproTech)

Journal: Cell Death Discovery

Article Title: FGF1-FGFR2 axis regulated by nuclear receptor RORγ represents an effective strategy in intrahepatic cholangiocarcinoma

doi: 10.1038/s41420-025-02844-8

Figure Lengend Snippet: A Heatmap of mRNA expression changes of FGF family genes and FGFR family genes in HUCCT-1 cells treated for 2 days with 5 μM XY101. B Oncoprint display from cBioPortal of FGF family genes and FGFR family genes alterations in iCCA tumors. C , D qRT-PCR analysis of FGFR2 mRNA in iCCA cells treated with DMSO or RORγ antagonists (GSK805 and XY101) at indicated concentrations for 2 days. n = 3 biological replicates. E qRT-PCR assay of FGF1 mRNA in RBE and HUCCT-1 cells after treatment with DMSO, 5 μM GSK805 or XY101 for 2 days. n = 3 biological replicates. F Immunoblotting assay of indicated proteins in RBE and HUCCT-1 cells after treatment with DMSO, or RORγ antagonists (GSK805 and XY101) at indicated concentrations for 2 days. n = 3 biological replicates. G The genome browser illustrates RORγ-binding events on the promoters of the FGF1 and FGFR2 genes in triple-negative breast cancer cells, as previously reported. These findings are derived from our previous ChIP-seq dataset (GEO: GSE126380 ). H ChIP-qPCR analysis was performed to assess the relative enrichment of RORγ or H3K27ac at the promoters of the FGF1 and FGFR2 genes in iCCA cells treated with 5 μM GSK805 or XY101 for 2 days. The fold change indicates the enrichment of these factors at the gene promoters in response to GSK805 and XY101, normalized to the IgG enrichment in vehicle-treated cells, which was set as 1. All data from in vitro experiments shown above are the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: The sources of chemicals are as follows: GSK805, and XY101 were obtained from WuXi AppTec (China); Pemigatinib was purchased from TargetMol (USA); Recombinant human FGF1 was obtained from MedChemExpress (USA).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Binding Assay, Derivative Assay, ChIP-sequencing, ChIP-qPCR, In Vitro

Journal: Cell Death Discovery

Article Title: FGF1-FGFR2 axis regulated by nuclear receptor RORγ represents an effective strategy in intrahepatic cholangiocarcinoma

doi: 10.1038/s41420-025-02844-8

Figure Lengend Snippet: A Immunoblotting analysis of FGF1 protein in iCCA cells transfected with FGF1 siRNAs or control. n = 3 biological replicates. B RBE and HUCCT-1 cells were transfected with FGF1 siRNAs or control. Live cells were counted at the indicated time points after transfection. n = 3 biological replicates. C Transfection of FGF1 siRNAs or control into wild-type or RORγ-overexpressing RBE and HUCCT-1 cells, with or without 5 ng/ml human recombinant FGF1. Viable cells were counted after 4 days. n = 3 biological replicates. D RBE and HUCCT-1 cells were incubated with recombinant human FGF1 at the indicated concentrations for 4 days, after which live cells were counted. n = 3 biological replicates. E Colony formation assays were conducted to detect the survival of RBE and HUCCT-1 cells treated with recombinant human FGF1 at the indicated concentrations for 14 days. n = 3 biological replicates. F FGFR2, phosphorylated FGFR2 (p-FGFR2), and its downstream proteins were detected by immunoblotting in RBE and HUCCT-1 cells treated with recombinant human FGF1 at the specified concentrations for 20 min. n = 3 biological replicates. G Recombinant human FGF1 was added to iCAA cells transfected with RORC siRNAs or control, and live cells were counted after a 4-day incubation. n = 3 biological replicates. H Live cells were counted to detect the survival of RBE and HUCCT-1 cells treated with GSK805, either alone or in combination with human recombinant FGF1 at a concentration of 5 ng/ml. n = 3 biological replicates. I ELISA assay was performed to detect FGF1 levels in the supernatant of RORγ-overexpression and RORC -silenced iCAA cells. n = 3 biological replicates. All data presented above are shown as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: The sources of chemicals are as follows: GSK805, and XY101 were obtained from WuXi AppTec (China); Pemigatinib was purchased from TargetMol (USA); Recombinant human FGF1 was obtained from MedChemExpress (USA).

Techniques: Western Blot, Transfection, Control, Recombinant, Incubation, Concentration Assay, Enzyme-linked Immunosorbent Assay, Over Expression

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: Hepatic FGF1 was down‐regulated by INH and RIF. A–C) Eight‐week‐old male C57BL/6J mice were challenged with 135 mg kg −1 isoniazid and 270 mg kg −1 rifampicin or vehicle by gavage for three weeks. At the end of this experiment, liver tissues and serum samples were collected for analysis. (A) Relative mRNA levels of all Fgfs in the liver tissues from vehicle and INH and RIF‐treated mice were detected by qRT‐PCR and normalized to that of β‐Actin ( n = 4). (B) The hepatic FGF1 expression was determined by western blotting analysis and its semi‐quantitation using Image J. The relative FGF1 expression level was determined after normalization with GAPDH ( n = 5). (C) Representative image and quantification of liver sections stained with FGF1 (green), albumin (red) and DAPI (blue) from the vehicle and INH and RIF‐treated mice ( n = 10, two fields per mouse). The FGF1 stains were quantified using Image J software. Scale bar = 25 µm. D–F) The expression level of FGF1 was detected by qRT‐PCR (D) ( n = 6) and western blotting analysis (E) ( n = 3) in primary hepatocytes extracted from vehicle and INH/RIF‐treated mice. The concentrations of FGF1 in the cell supernatant were determined by ELISA (F) ( n = 3). G–I) Primary hepatocytes from C57BL/6J mice were stimulated with DMSO or different dosages of INH and RIF (L‐INH/RIF: 4 µg mL −1 INH and 8 µg mL −1 RIF, M‐INH/RIF: 20 µg mL −1 INH and 40 µg mL −1 RIF, H‐INH/RIF: 100 µg mL −1 INH and 200 µg mL −1 RIF) for 6 h. The expression level of FGF1 was detected by qRT‐PCR (G), western blotting (H); the relative Fgf1 mRNA level was normalized to that of β‐Actin ( n = 6), the relative FGF1 expression level was determined after normalization with GAPDH ( n = 3). FGF1 levels in the supernatant were determined by ELISA (I) ( n = 3). J) The expression of FGF1 (green), hepatocyte marker albumin (red) and DAPI (blue) were detected by IF staining in the liver tissues from healthy individuals and patients with ATB‐DILI ( n = 10–11). The IF intensity was quantified using Image J software. Scale bar = 25 µm. Data are presented as mean ± SEM; (A, D, F, right panel of B, C, J, lower panel of E) two‐tailed unpaired t ‐test; (G, I, lower panel of H) ordinary one‐way ANOVA, followed by Dunnett. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns, not significant; nd, not detectable.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: Quantitative RT-PCR, Expressing, Western Blot, Quantitation Assay, Staining, Software, Enzyme-linked Immunosorbent Assay, Marker, Two Tailed Test

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: Hepatocyte‐specific Fgf1 deficiency aggregates liver damage induced by INH and RIF. A) Eight‐week‐old male Fgf1 fl/fl and Fgf1 ‐LKO mice were daily challenged with 135 mg kg −1 isoniazid and 270 mg kg −1 rifampicin or vehicle for three weeks. Liver tissues and serum samples were collected at the end of this experiment. B,C) Liver‐specific Fgf1 deficiency was verified by qRT‐PCR (B) and western blotting analysis (C). The relative Fgf1 mRNA level was normalized to that of β‐Actin ( n = 6). FGF1 expression level was determined after normalization with GAPDH ( n = 3). D–F) Serum ALT (D), AST (E) activity and serum TBIL contents (F) ( n = 4). G) Representative TUNEL staining of liver sections and quantification by TUNEL positive cells ( n = 8, two fields per mouse). Scale bar = 25 µm. H) Hepatic TBA contents ( n = 4). I–K) The mRNA levels of BAs synthase ( Cyp7a1 , Cyp8b1 , Cyp27a1 and Cyp7b1 ) (I), BAs transporters of uptake ( Ntcp , Oatp1 and Oatp2 ) (J) and efflux ( Bsep , Mdr2 and Mrp2 ) (K) in liver tissues were analyzed by qRT‐PCR and normalized to that of β‐Actin ( n = 4). L‐N) The mRNA levels of BAs synthase ( Cyp7a1 , Cyp8b1 , Cyp27a1 and Cyp7b1 ) (L), BAs transporters of uptake ( Ntcp , Oatp1 and Oatp2 ) (M) and efflux ( Bsep , Mdr2 and Mrp2 ) (N) in primary hepatocytes extracted from Fgf1 fl/fl and Fgf1 ‐LKO mice treated with vehicle or INH and RIF were analyzed by qRT‐PCR and normalized to that of β‐Actin ( n = 6). Data are presented as mean ± SEM; (D–F, H, I–N, right panel of G) ordinary two‐way ANOVA, followed by Sidak; (B, C) two‐tailed unpaired t ‐test. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns, not significant.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: Quantitative RT-PCR, Western Blot, Expressing, Activity Assay, TUNEL Assay, Staining, Two Tailed Test

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: Administration of the non‐mitogenic FGF1 (FGF1 ΔHBS ) alleviated INH and RIF‐induced liver injury by normalizing hepatic BAs homeostasis. A) Eight‐week‐old male C57BL/6J mice were challenged with vehicle or 135 mg kg −1 isoniazid and 270 mg kg −1 rifampicin by gavage, followed by daily i.p. administration of PBS or FGF1 ΔHBS (0.1 mg kg −1 BW/day) for three weeks. B‐D) Serum ALT (B), AST (C) and serum TBIL contents (D) ( n = 5). E) TUNEL staining of liver sections and quantification by TUNEL positive cells ( n = 10, two fields per mice). Scale bar = 25 µm. F‐H) Hepatic TBA contents (F) ( n = 5), primary free BAs (G), and detailed components of primary BAs analyzed by mass spectrometry (H) ( n = 4). I) Hepatic protein expressions of Cyp7a1, Cyp8b1 and Cyp27a1 in the liver tissues from INH and RIF‐treated mice treated with PBS or FGF1 ΔHBS were determined by western blotting analysis and its semi‐quantitation using Image J. The relative protein levels were determined after normalization with GAPDH ( n = 4). J‐L) The mRNA levels of BA synthases ( Cyp7a1 , Cyp8b1 , Cyp27a1 and Cyp7b1 ) (J), transporters of reuptake (K) and efflux (L) in the liver tissues from INH and RIF‐treated mice treated with PBS or FGF1 ΔHBS were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 5). M) Eight‐week‐old male C57BL/6J mice fed by standard diet (SD) or diet containing 0.5% CA were challenged with vehicle or 135 mg kg −1 isoniazid and 270 mg kg −1 rifampicin by gavage, followed by daily i.p. administration of PBS or FGF1 ΔHBS (0.1 mg kg −1 BW/day) for three weeks. N‐R) Serum BA level (N), hepatic TBA contents (O), serum ALT (P), AST (Q) and serum TBIL contents (R) ( n = 5). Data are presented as mean ± SEM; (B‐D, right panel of E, F‐H) ordinary one‐way ANOVA, followed by Dunnett; (right panel of I, J‐L) two‐tailed unpaired t ‐test; (N‐R) ordinary two‐way ANOVA, followed by Sidak. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns, not significant.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: TUNEL Assay, Staining, Mass Spectrometry, Western Blot, Quantitation Assay, Quantitative RT-PCR, Two Tailed Test

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: HNF4 α mediated the BAs regulatory activity of FGF1 in the INH and RIF‐induced liver injury mouse model. A,B) The mRNA levels of Hnf4α , Shp , Lrh‐1 , Lxr (A) and the target genes of Hnf4α ( G6pc and Pklr ) (B) in primary hepatocytes extracted from INH and RIF‐treated Fgf1 fl/fl and Fgf1 ‐LKO mice were analyzed by qRT‐PCR and normalized to that of β‐Actin ( n = 6). C‐E) The expression levels of HNF4 α in the liver tissues from vehicle or INH and RIF‐treated Fgf1 fl/fl and Fgf1 ‐LKO mice were determined by western blotting analysis (C) and IF staining (D‐E). The relative HNF4 α expression level was determined after normalization with GAPDH ( n = 3). The HNF4 α stains were quantified using Image J software (E) ( n = 8, two fields per mice). Scale bar = 25 µm. F,G) The expression levels of HNF4 α in the liver tissues from ATB‐DILI mice treated with PBS or FGF1 ΔHBS were determined by western blotting analysis (F) and IF staining (G). The relative HNF4 α expression level was determined after normalization with GAPDH ( n = 3). The HNF4 α stains were quantified using Image J software ( n = 10, two fields per mice). Scale bar = 25 µm. H,I) Knockdown of Hnf4α in HepG2 cells transfected with shRNA were verified by qRT‐PCR (H) and western blotting analysis (I). The relative Hnf4α mRNA level was normalized to that of β‐Actin ( n = 6). The relative HNF4 α expression level was determined after normalization with GAPDH ( n = 3). J) The mRNA levels of BAs synthases in shNC or sh Hnf4α ‐transfected HepG2 cells after treated with PBS or FGF1 ΔHBS for 6 h were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 6). K) Male C57BL/6J mice transfected by AAV‐TBG‐shRNA NC (shNC) or AAV‐TBG‐shRNA Hnf4α (sh Hnf4α ) were challenge with INH and RIF, followed by daily i.p. administration of PBS or FGF1 ΔHBS for three weeks. Liver tissues and serum were collected at the end of this experiment. L,M) Liver‐specific Hnf4α knockdown were verified by qRT‐PCR (L) and western blotting analysis (M). The relative Hnf4α mRNA level was normalized to that of β‐Actin ( n = 6). The relative HNF4 α expression level was determined after normalization with GAPDH ( n = 3). N) Hepatic TBA contents ( n = 5). O) Hepatic mRNA levels of Cyp7a1 , Cyp8b1 , Cyp27a1 and Cyp7b1 were determined by qRT‐PCR and normalized to β‐Actin ( n = 5). P‐R) Serum ALT (P), AST (Q), serum TBIL contents (R) ( n = 5). S) TUNEL staining of liver sections and quantification by TUNEL positive cells ( n = 10, two fields per mice). Scale bar = 25 µm. Data are presented as mean ± SEM; (A, B, right panel of F, G, H, lower panel of I, L, M) two‐tailed unpaired t ‐test; (lower panel of C, E, J, N‐R, right panel of S) ordinary two‐way ANOVA, followed by Sidak. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns, not significant.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: Activity Assay, Quantitative RT-PCR, Expressing, Western Blot, Staining, Software, Knockdown, Transfection, shRNA, TUNEL Assay, Two Tailed Test

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: FGF1 ΔHBS inhibited HNF4 α ‐mediated BA biosynthesis via FGFR4‐EKR1/2 pathway. A,B) Primary hepatocytes extracted from INH and RIF‐treated mice were stimulated by PBS or 1000 ng mL −1 FGF1 ΔHBS for 5 min. The protein expression of p‐ERK1/2, ERK1/2, p‐PI3K, p‐AKT, AKT, p‐JNK and JNK were determined by western blotting analysis and its semi‐quantitation using Image J. The relative protein levels were determined after normalization with corresponding total protein ( n = 3). C) The activation of ERK1/2 in INH and RIF‐treated Fgf1 fl/fl and Fgf1 fl/fl ‐LKO mice were detected by western blotting analysis and its semi‐quantitation using Image J. The relative p‐ERK1/2 protein levels were determined after normalization with ERK ( n = 3). D,E) Primary hepatocytes extracted from INH and RIF‐treated mice were pretreated with 10 uM U0126 for 2 h, followed by PBS or 1000 ng mL −1 FGF1 ΔHBS stimulation for 6 h. The protein levels of p‐ERK1/2 and ERK1/2 were determined by western blotting analysis (D) and its semi‐quantitation by Image J ( n = 3). The mRNA levels of Hnf4α were analyzed by qRT‐PCR (E) and normalized to β‐Actin ( n = 6). F‐I) The mRNA levels of Cyp7a1 (F), Cyp8b1 (G), Cyp27a1 (H) and Cyp7b1 (I) in primary hepatocytes were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 6). J,K) Deficiency of Fgfr4 was verified by qRT‐PCR (J) and western blotting analysis (K). The relative Fgfr4 mRNA level was normalized to that of β‐Actin ( n = 6). The relative FGFR4 expression level was determined after normalization with GAPDH ( n = 2). L) Primary hepatocytes extracted from INH and RIF‐treated Fgfr4 fl/fl or Fgfr4 ‐LKO mice were stimulated by PBS or 1000 ng mL −1 FGF1 ΔHBS . M) The protein levels of p‐ERK1/2 and ERK1/2 in primary hepatocytes were determined by western blotting analysis and its semi‐quantitation using Image J. The relative p‐ERK1/2 expression level was determined after normalization with ERK1/2 ( n = 3). N) The mRNA levels of Hnf4α in primary hepatocytes were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 6). O‐R) The mRNA levels of Cyp7a1 (O), Cyp8b1 (P), Cyp27a1 (Q) and Cyp7b1 (R) in primary hepatocytes were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 6). Data are presented as mean ± SEM; (B, right panel of C and L, K) two‐tailed unpaired t ‐test; (E‐I, lower panel of D, right panel of M, N‐R) ordinary two‐way ANOVA, followed by Sidak. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns, not significant.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: Expressing, Western Blot, Quantitation Assay, Activation Assay, Quantitative RT-PCR, Two Tailed Test

Journal: Advanced Science

Article Title: Hepatocyte‐Derived FGF1 Alleviates Isoniazid and Rifampicin‐Induced Liver Injury by Regulating HNF4 α ‐Mediated Bile Acids Synthesis

doi: 10.1002/advs.202408688

Figure Lengend Snippet: Hepatic Fgfr4 deficiency abolished the protective effects of FGF1 ΔHBS in the mouse model of INH and RIF‐induced liver injury. A) The expression profile of all FGFRs in the liver tissues of normal C57BL/6J mice by qRT‐PCR analysis. The relative Fgfr4 mRNA level was normalized to that of β‐Actin ( n = 4). B,C) Liver‐specific Fgfr4 deficiency was verified by qRT‐PCR (B) and western blotting analysis (C). The relative Fgfr4 mRNA level was normalized to that of β‐Actin ( n = 3). D‐N) Eight‐week‐old male Fgfr4 fl/fl and Fgfr4 ‐LKO mice were challenge with 135 mg kg −1 isoniazid and 270 mg kg −1 rifampicin by gavage, followed by i.p. daily administration of PBS or FGF1 ΔHBS (0.1 mg kg −1 BW/day) for three weeks ( n = 6). Liver tissues and serum were collected for analysis at the end of this experiment. (D‐F) Serum ALT (D), AST (E), serum TBIL contents (F). (G) TUNEL staining of liver sections and quantification by TUNEL positive cells ( n = 12, two fields per mice). Scale bar = 25 µm. (H) Hepatic TBA contents. (I) The protein levels of p‐ERK1/2, ERK1/2 and HNF4 α in liver tissues were determined by western blotting analysis and its semi‐quantitation using Image J ( n = 3). (J) Analysis of the expression levels of HNF4 α in liver tissues from the Fgfr4 fl/fl and Fgfr4 ‐LKO mice by IF staining. The IF intensity was quantified using ImageJ software ( n = 12, two fields per mice). Scale bar = 25 µm. (K‐N) The mRNA levels of Cy p7a1 (K), Cyp8b1 (L), Cyp27a1 (M) and Cyp7b1 (N) in liver tissues were analyzed by qRT‐PCR and normalized to β‐Actin ( n = 6). O) A graphical model depicting the roles of FGF1 in protecting against ATB‐DILI by maintaining FGFR4‐ERK1/2‐HNF4 α signaling axis‐mediated BAs homeostasis. Image created using BioRender. Data are presented as mean ± SEM; (D‐F, right panel of G and I and J, H, K‐N) ordinary two‐way ANOVA, followed by Sidak; (B, lower panel of C) two‐tailed unpaired t ‐test. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001, ns, not significant.

Article Snippet: To mimic ATB‐DILI, HepG2 cells were seeded at an appropriate density in six well plates for 24h and then exposed to 100 µg mL −1 INH and 200 µg mL −1 RIF (dissolved with DMSO) with PBS or 1000 ng mL −1 FGF1 ΔHBS for 6 h. Pre‐treated HepG2 cells with 10 µM of U0126 (MedChem Express) for 1 h to selectively inhibit the MEK1 and MEK2 signaling pathways.

Techniques: Expressing, Quantitative RT-PCR, Western Blot, TUNEL Assay, Staining, Quantitation Assay, Software, Two Tailed Test