Effect of excess iron on oxidative stress and gluconeogenesis through hepcidin during mitochondrial dysfunction Hyo Jung Lee, Joo Sun Choi, Hye Ja Lee,

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Effect of excess iron on oxidative stress and gluconeogenesis through hepcidin during mitochondrial dysfunction Hyo Jung Lee, Joo Sun Choi, Hye Ja Lee, Won-Ho Kim, Sang Ick Park, Jihyun Song Journal of Nutritional Biochemistry Volume 26, Issue 12, Pages 1414-1423 (December 2015) DOI: 10.1016/j.jnutbio.2015.07.008 Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 1 Iron accumulation induces oxidative stress and mitochondrial dysfunction. (A) The SK-HEP-1 cells were treated with 10 or 20 μM Fe–NTA complex for 24h, followed by Western blot. (B) Twenty micromolars of DFO was treated for 2h before Fe–NTA complex treatment, followed by Western blot. (C) The levels of ferric iron and ROS were analyzed in SK-HEP-1 cells treated with Fe–NTA complex (20 μM) w/o DFO (20 μM) or NAC (40 μM) for 24h. DFO and NAC were pretreated for 2h. (D) The SK-HEP-1 cells were treated with Fe–NTA complex (20 μM) w/o DFO (20 μM) or NAC (40 μM) for 24h, followed Western blot and cellular ATP content analysis. *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 2 Oligomycin-induced mitochondrial dysfunction increases oxidative stress and gluconeogenesis. (A) ROS production assessed in SK-HEP-1 cells treated with oligomycin (40 μM) w/o NAC (40 μM) for 24h. NAC was pretreated for 2h before oligomycin treatment. (B–C) The expression levels of protein and transcription factors that related to MAPK activity, gluconeogenesis and oxidative stress were analyzed in whole-cell lysate by Western blot. *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 3 Oligomycin-induced mitochondrial dysfunction triggered changes in iron metabolism. (A–B) The SK-HEP-1 cells treated with oligomycin (40 μM) w/o DFO (20 μM) or NAC (40 μM) for 24h. DFO and NAC were pretreated for 2h before oligomycin treatment. Iron metabolism-related protein expression was analyzed by Western blot. (C) The levels of ferric iron and ROS were analyzed in SK-HEP-1 cells treated with oligomycin (40 μM) w/o DFO (20 μM) or NAC (40 μM) for 24h. (D) Twenty micromolars of DFO was treated for 2h before oligomycin treatment, analyzed C/EBPα phosphorylation by Western blot. *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 4 Excessive iron induced abnormal gluconeogenesis. (A–B) Forty micromolars of NAC or 20 μM of DFO was pretreated for 2h before Fe–NTA complex (20 μM), and gluconeogenic enzymes were measured in whole-cell lysate by Western blot. *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 5 Hepcidin shRNA recovered abnormal iron metabolism, gluconeogenesis and oxidative stress in oligomycin-induced mitochondrial dysfunction. (A) The SK-HEP-1 cells were infected with hepcidin shRNA plasmid for 48h and then treated with oligomycin (24h, 40 μM), followed by Western blot. (B) Ferric iron and ROS were assessed in SK-HEP-1 cells infected with hepcidin shRNA plasmid for 48h and then treated with oligomycin (24h, 40 μM). *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 6 Overexpression of hepcidin synergistically deteriorated abnormal iron metabolism, gluconeogenesis and oxidative stress in oligomycin-induced mitochondrial dysfunction. (A) The SK-HEP-1 cells were infected with hepcidin-pcDNA 3.1 for 48h and then treated with oligomycin (24h, 40 μM), followed by Western blot. (B) Ferric iron and ROS were assessed in SK-HEP-1 cell infected with hepcidin-pcDNA 3.1 for 48h and then treated with oligomycin (24h, 40 μM). *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Fig. 7 Change of iron metabolism and gluconeogenesis in diabetic mice. Whole lysate was extracted from hepatic tissues of 10-week-old male db/db and age-matched lean mice, and Western blot was performed. *Indicates statistical difference between groups at P<.05. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions

Supplementary Fig. 1 Excessive iron induced SMAD1/5/8 phosphorylation. (A) Twenty micromolars of 20 μM DFO was pretreated for 2h before Fe–NTA complex (20 μM). (B) The SK-HEP-1 cells treated with oligomycin (40 μM) for 24h. SMAD1/5/8 phosphorylation was measured in whole-cell lysate. Journal of Nutritional Biochemistry 2015 26, 1414-1423DOI: (10.1016/j.jnutbio.2015.07.008) Copyright © 2015 Elsevier Inc. Terms and Conditions