Skip Navigation
Skip to contents

Endocrinol Metab : Endocrinology and Metabolism

clarivate
OPEN ACCESS
SEARCH
Search

Search

Page Path
HOME > Search
3 "Reactive oxygen species"
Filter
Filter
Article type
Keywords
Publication year
Authors
Funded articles
Original Articles
Diabetes, obesity and metabolism
Inhibition of Fatty Acid β-Oxidation by Fatty Acid Binding Protein 4 Induces Ferroptosis in HK2 Cells Under High Glucose Conditions
Jiasi Chen, Keping Wu, Yan Lei, Mingcheng Huang, Lokyu Cheng, Hui Guan, Jiawen Lin, Ming Zhong, Xiaohua Wang, Zhihua Zheng
Endocrinol Metab. 2023;38(2):226-244.   Published online April 27, 2023
DOI: https://doi.org/10.3803/EnM.2022.1604
  • 3,607 View
  • 179 Download
  • 3 Web of Science
  • 4 Crossref
AbstractAbstract PDFPubReader   ePub   
Background
Ferroptosis, which is caused by an iron-dependent accumulation of lipid hydroperoxides, is a type of cell death linked to diabetic kidney disease (DKD). Previous research has shown that fatty acid binding protein 4 (FABP4) is involved in the regulation of ferroptosis in diabetic retinopathy. The present study was constructed to explore the role of FABP4 in the regulation of ferroptosis in DKD.
Methods
We first detected the expression of FABP4 and proteins related to ferroptosis in renal biopsies of patients with DKD. Then, we used a FABP4 inhibitor and small interfering RNA to investigate the role of FABP4 in ferroptosis induced by high glucose in human renal proximal tubular epithelial (HG-HK2) cells.
Results
In kidney biopsies of DKD patients, the expression of FABP4 was elevated, whereas carnitine palmitoyltransferase-1A (CP-T1A), glutathione peroxidase 4, ferritin heavy chain, and ferritin light chain showed reduced expression. In HG-HK2 cells, the induction of ferroptosis was accompanied by an increase in FABP4. Inhibition of FABP4 in HG-HK2 cells changed the redox state, sup-pressing the production of reactive oxygen species, ferrous iron (Fe2+), and malondialdehyde, increasing superoxide dismutase, and reversing ferroptosis-associated mitochondrial damage. The inhibition of FABP4 also increased the expression of CPT1A, reversed lipid deposition, and restored impaired fatty acid β-oxidation. In addition, the inhibition of CPT1A could induce ferroptosis in HK2 cells.
Conclusion
Our results suggest that FABP4 mediates ferroptosis in HG-HK2 cells by inhibiting fatty acid β-oxidation.

Citations

Citations to this article as recorded by  
  • Fatty Acid Binding Protein-4 Silencing Inhibits Ferroptosis to Alleviate Lipopolysaccharide-induced Injury of Renal Tubular Epithelial Cells by Blocking Janus Kinase 2/Signal Transducer and Activator of Transcription 3 Signaling
    Suo Xu, Jiye Luo, Yanli Wang, Xiaobing Chen
    Chinese Journal of Physiology.2024; 67(1): 47.     CrossRef
  • Ferroptosis in Liver Disease: Natural Active Compounds and Therapeutic Implications
    Zhili Wu, Yanru Zhu, Wenchao Liu, Balamuralikrishnan Balasubramanian, Xiao Xu, Junhu Yao, Xinjian Lei
    Antioxidants.2024; 13(3): 352.     CrossRef
  • Mechanisms and regulations of ferroptosis
    Xu-Dong Zhang, Zhong-Yuan Liu, Mao-Sen Wang, Yu-Xiang Guo, Xiang-Kun Wang, Kai Luo, Shuai Huang, Ren-Feng Li
    Frontiers in Immunology.2023;[Epub]     CrossRef
  • Targeting epigenetic and posttranslational modifications regulating ferroptosis for the treatment of diseases
    Yumin Wang, Jing Hu, Shuang Wu, Joshua S. Fleishman, Yulin Li, Yinshi Xu, Wailong Zou, Jinhua Wang, Yukuan Feng, Jichao Chen, Hongquan Wang
    Signal Transduction and Targeted Therapy.2023;[Epub]     CrossRef
Close layer
Ghrelin Inhibits Oligodendrocyte Cell Death by Attenuating Microglial Activation
Jee Youn Lee, Tae Young Yune
Endocrinol Metab. 2014;29(3):371-378.   Published online September 25, 2014
DOI: https://doi.org/10.3803/EnM.2014.29.3.371
  • 4,304 View
  • 30 Download
  • 25 Web of Science
  • 23 Crossref
AbstractAbstract PDFPubReader   
Background

Recently, we reported the antiapoptotic effect of ghrelin in spinal cord injury-induced apoptotic cell death of oligodendrocytes. However, how ghrelin inhibits oligodendrocytes apoptosis, is still unknown. Therefore, in the present study, we examined whether ghrelin inhibits microglia activation and thereby inhibits oligodendrocyte apoptosis.

Methods

Using total cell extracts prepared from BV-2 cells activated by lipopolysaccharide (LPS) with or without ghrelin, the levels of p-p38 phosphor-p38 mitogen-activated protein kinase (p-p38MAPK), phospho-c-Jun N-terminal kinase (pJNK), p-c-Jun, and pro-nerve growth factor (proNGF) were examined by Western blot analysis. Reactive oxygen species (ROS) production was investigated by using dichlorodihydrofluorescein diacetate. To examine the effect of ghrelin on oligodendrocyte cell death, oligodendrocytes were cocultured in transwell chambers of 24-well plates with LPS-stimulated BV-2 cells. After 48 hours incubation, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay and terminal deoxynucleotidyl transferase 2'-deoxyuridine, 5'-triphosphate nick end labeling staining were assessed.

Results

Ghrelin treatment significantly decreased levels of p-p38MAPK, p-JNK, p-c-Jun, and proNGF in LPS-stimulated BV-2 cells. ROS production increased in LPS-stimulated BV-2 cells was also significantly inhibited by ghrelin treatment. In addition, ghrelin significantly inhibited oligodendrocyte cell death when cocultured with LPS-stimulated BV-2 cells.

Conclusion

Ghrelin inhibits oligodendrocyte cell death by decreasing proNGF and ROS production as well as p38MAPK and JNK activation in activated microglia as an anti-inflammatory hormone.

Citations

Citations to this article as recorded by  
  • Ghrelin Represses Thymic Stromal Lymphopoietin Gene Expression through Activation of Glucocorticoid Receptor and Protein Kinase C Delta in Inflamed Skin Keratinocytes
    Hayan Jeong, Hyo-Jin Chong, Jangho So, Yejin Jo, Tae-Young Yune, Bong-Gun Ju
    International Journal of Molecular Sciences.2022; 23(7): 3977.     CrossRef
  • Inflammation: A Target for Treatment in Spinal Cord Injury
    Ximena Freyermuth-Trujillo, Julia J. Segura-Uribe, Hermelinda Salgado-Ceballos, Carlos E. Orozco-Barrios, Angélica Coyoy-Salgado
    Cells.2022; 11(17): 2692.     CrossRef
  • The Interplay between Ghrelin and Microglia in Neuroinflammation: Implications for Obesity and Neurodegenerative Diseases
    Cristina Russo, Maria Stella Valle, Antonella Russo, Lucia Malaguarnera
    International Journal of Molecular Sciences.2022; 23(21): 13432.     CrossRef
  • Early low-dose ghrelin intervention via miniosmotic pumps could protect against the progressive dopaminergic neuron loss in Parkinson's disease mice
    Lingling Jiao, Xixun Du, Fengju Jia, Yong Li, Dexiao Zhu, Tinging Tang, Qian Jiao, Hong Jiang
    Neurobiology of Aging.2021; 101: 70.     CrossRef
  • Ghrelin-Mediated Regeneration and Plasticity After Nervous System Injury
    Irina Stoyanova, David Lutz
    Frontiers in Cell and Developmental Biology.2021;[Epub]     CrossRef
  • Microglial Lipid Biology in the Hypothalamic Regulation of Metabolic Homeostasis
    Andrew Folick, Suneil K. Koliwad, Martin Valdearcos
    Frontiers in Endocrinology.2021;[Epub]     CrossRef
  • Acylated Ghrelin as a Multi-Targeted Therapy for Alzheimer's and Parkinson's Disease
    Niklas Reich, Christian Hölscher
    Frontiers in Neuroscience.2020;[Epub]     CrossRef
  • Effects of Ghrelin on the Apoptosis of Rheumatoid Arthritis Fibroblast-Like Synoviocyte MH7A Cells
    Junxian Ma, Xinbo Wang, Tingting Lv, Jie Liu, Ying Ren, Jinshan Zhang, Yan Zhang
    Biological and Pharmaceutical Bulletin.2019; 42(2): 158.     CrossRef
  • Direct and indirect effects of lipids on microglia function
    Q. Leyrolle, S. Layé, A. Nadjar
    Neuroscience Letters.2019; 708: 134348.     CrossRef
  • Dopamine neuronal protection in the mouse Substantia nigra by GHSR is independent of electric activity
    Bernardo Stutz, Carole Nasrallah, Mariana Nigro, Daniel Curry, Zhong-Wu Liu, Xiao-Bing Gao, John D. Elsworth, Liat Mintz, Tamas L. Horvath
    Molecular Metabolism.2019; 24: 120.     CrossRef
  • MK-0677, a Ghrelin Agonist, Alleviates Amyloid Beta-Related Pathology in 5XFAD Mice, an Animal Model of Alzheimer’s Disease
    Yu-on Jeong, Soo Shin, Jun Park, Bo Ku, Ji Song, Jwa-Jin Kim, Seong Jeon, Sang Lee, Minho Moon
    International Journal of Molecular Sciences.2018; 19(6): 1800.     CrossRef
  • Involvement of Astrocytes in Mediating the Central Effects of Ghrelin
    Laura Frago, Julie Chowen
    International Journal of Molecular Sciences.2017; 18(3): 536.     CrossRef
  • The neurological effects of ghrelin in brain diseases: Beyond metabolic functions
    Qian Jiao, Xixun Du, Yong Li, Bing Gong, Limin Shi, Tingting Tang, Hong Jiang
    Neuroscience & Biobehavioral Reviews.2017; 73: 98.     CrossRef
  • Neuropeptides and Microglial Activation in Inflammation, Pain, and Neurodegenerative Diseases
    Lila Carniglia, Delia Ramírez, Daniela Durand, Julieta Saba, Juan Turati, Carla Caruso, Teresa N. Scimonelli, Mercedes Lasaga
    Mediators of Inflammation.2017; 2017: 1.     CrossRef
  • Non-Neuronal Cells in the Hypothalamic Adaptation to Metabolic Signals
    Alejandra Freire-Regatillo, Pilar Argente-Arizón, Jesús Argente, Luis Miguel García-Segura, Julie A. Chowen
    Frontiers in Endocrinology.2017;[Epub]     CrossRef
  • The Ghrelin/GOAT System Regulates Obesity-Induced Inflammation in Male Mice
    Rebecca E. Harvey, Victor G. Howard, Moyra B. Lemus, Tara Jois, Zane B. Andrews, Mark W. Sleeman
    Endocrinology.2017; 158(7): 2179.     CrossRef
  • Central Modulation of Neuroinflammation by Neuropeptides and Energy-Sensing Hormones during Obesity
    Roger Maldonado-Ruiz, Lizeth Fuentes-Mera, Alberto Camacho
    BioMed Research International.2017; 2017: 1.     CrossRef
  • Lifestyle Shapes the Dialogue between Environment, Microglia, and Adult Neurogenesis
    Jorge Valero, Iñaki Paris, Amanda Sierra
    ACS Chemical Neuroscience.2016; 7(4): 442.     CrossRef
  • Signaling of ghrelin and its functional receptor, the growth hormone secretagogue receptor, promote tumor growth in glioblastomas
    Yousuke Okada, Yasuo Sugita, Koichi Ohshima, Motohiro Morioka, Satoru Komaki, Junko Miyoshi, Hideyuki Abe
    Neuropathology.2016; 36(6): 535.     CrossRef
  • Ghrelin-AMPK Signaling Mediates the Neuroprotective Effects of Calorie Restriction in Parkinson's Disease
    Jacqueline A. Bayliss, Moyra B. Lemus, Romana Stark, Vanessa V. Santos, Aiysha Thompson, Daniel J. Rees, Sandra Galic, John D. Elsworth, Bruce E. Kemp, Jeffrey S. Davies, Zane B. Andrews
    The Journal of Neuroscience.2016; 36(10): 3049.     CrossRef
  • MMP-3 secreted from endothelial cells of blood vessels after spinal cord injury activates microglia, leading to oligodendrocyte cell death
    Jee Y. Lee, Hae Y. Choi, Tae Y. Yune
    Neurobiology of Disease.2015; 82: 141.     CrossRef
  • Role of Non-Neuronal Cells in Body Weight and Appetite Control
    Pilar Argente-Arizón, Alejandra Freire-Regatillo, Jesús Argente, Julie A. Chowen
    Frontiers in Endocrinology.2015;[Epub]     CrossRef
  • Articles in 'Endocrinology and Metabolism' in 2014
    Won-Young Lee
    Endocrinology and Metabolism.2015; 30(1): 47.     CrossRef
Close layer
Review Article
Adrenal gland
Role of Reactive Oxygen Species in Hypothalamic Regulation of Energy Metabolism
Sabrina Diano
Endocrinol Metab. 2013;28(1):3-5.   Published online March 25, 2013
DOI: https://doi.org/10.3803/EnM.2013.28.1.3
  • 3,947 View
  • 43 Download
  • 21 Crossref
AbstractAbstract PDFPubReader   

To understand the etiology of metabolic disorders, including obesity and type II diabetes, it is essential to gain better insight into how stored and available energy sources are monitored by the central nervous system. In particular, a comprehension of the fine cellular interplay and intracellular mechanisms that enable appropriate hypothalamic and consequent endocrine and behavioral responses to both circulating hormonal and nutrient signals remains elusive. Recent data, including those from our laboratories, raised the notion that reactive oxygen species (ROS) generation is not merely a by-product of substrate oxidation, but it plays a crucial role in modulating cellular responses involved in the regulation of energy metabolism. These review summarizes the published recent data on the effect of ROS levels in the regulation of neuronal function, including that of hypothalamic melanocortin neurons, pro-opiomelanocortin and neuropeptide Y-/agouti related peptide-neurons, in the modulation of food intake.

Citations

Citations to this article as recorded by  
  • Regulation of hypothalamic reactive oxygen species and feeding behavior by phosphorylation of the beta 2 thyroid hormone receptor isoform
    Svetlana Minakhina, Sun Young Kim, Fredric E. Wondisford
    Scientific Reports.2024;[Epub]     CrossRef
  • Overexpression of PpmTERF18 enhances the antioxidant capacity of peach fruit to alleviate oxidative damage
    Xiaoshan Guo, Guangqin Jing, Shuhua Zhu, Jianrong Feng, Dandan Huang
    Scientia Horticulturae.2023; 318: 112123.     CrossRef
  • Insights into the promising prospect of pharmacological approaches targeting mitochondrial dysfunction in major human diseases: At a glance
    Md.Mominur Rahman, Md.Taslim Sarker, Sabbir Ahmed, Md.Nur Uddin, Md.Shariful Islam, Md.Rezaul Islam, Shanto Das, Nobendu Mukherjee, Hassan A. Hemeg, Abdur Rauf, Bimal Kumar Ghimire, Muthu Thiruvengadam
    Process Biochemistry.2023; 132: 41.     CrossRef
  • Structure-based analysis and rational design of human peroxiredoxin-1's C-terminus-derived peptides to target sulfiredoxin-1 in pancreatic cancer
    Xiaoqiong Wu, Rongyuan Qiu, Wei Yi, Juan Chen, Zhou Zhang, Ji Zhang, Zhiyuan Zhu
    Biophysical Chemistry.2022; 288: 106857.     CrossRef
  • Drp1 is required for AgRP neuronal activity and feeding
    Sungho Jin, Nal Ae Yoon, Zhong-Wu Liu, Jae Eun Song, Tamas L Horvath, Jung Dae Kim, Sabrina Diano
    eLife.2021;[Epub]     CrossRef
  • Mechanism of deoxynivalenol mediated gastrointestinal toxicity: Insights from mitochondrial dysfunction
    Shuai Wang, Kuntan Wu, Dongfang Xue, Cong Zhang, Shahid Ali Rajput, Desheng Qi
    Food and Chemical Toxicology.2021; 153: 112214.     CrossRef
  • Redox Signaling from and to Peroxisomes: Progress, Challenges, and Prospects
    Marc Fransen, Celien Lismont
    Antioxidants & Redox Signaling.2019; 30(1): 95.     CrossRef
  • The melanocortin pathway and control of appetite-progress and therapeutic implications
    Giulia Baldini, Kevin D Phelan
    Journal of Endocrinology.2019; 241(1): R1.     CrossRef
  • Melanocortin Receptor 4 Signaling Regulates Vertebrate Limb Regeneration
    Mengshi Zhang, Youwei Chen, Hanqian Xu, Li Yang, Feng Yuan, Lei Li, Ying Xu, Ying Chen, Chao Zhang, Gufa Lin
    Developmental Cell.2018; 46(4): 397.     CrossRef
  • Hypothalamic Mitochondrial Dysfunction as a Target in Obesity and Metabolic Disease
    Juan Cunarro, Sabela Casado, Javier Lugilde, Sulay Tovar
    Frontiers in Endocrinology.2018;[Epub]     CrossRef
  • Role of oxidative stress and antioxidants in daily nutrition and human health
    Geir Bjørklund, Salvatore Chirumbolo
    Nutrition.2017; 33: 311.     CrossRef
  • DRP1 Suppresses Leptin and Glucose Sensing of POMC Neurons
    Anna Santoro, Michela Campolo, Chen Liu, Hiromi Sesaki, Rosaria Meli, Zhong-Wu Liu, Jung Dae Kim, Sabrina Diano
    Cell Metabolism.2017; 25(3): 647.     CrossRef
  • Administration of a leptin antagonist during the neonatal leptin surge induces alterations in the redox and inflammatory state in peripubertal /adolescent rats
    Virginia Mela, Oskarina Hernandez, Caroline Hunsche, Francisca Diaz, Julie A. Chowen, Mónica De la Fuente
    Molecular and Cellular Endocrinology.2017; 454: 125.     CrossRef
  • Effects of chlorogenic acid on intracellular calcium regulation in lysophosphatidylcholine-treated endothelial cells
    Hye-Jin Jung, Seung-Soon Im, Dae-Kyu Song, Jae-Hoon Bae
    BMB Reports.2017; 50(6): 323.     CrossRef
  • Trimetazidine attenuates pressure overload-induced early cardiac energy dysfunction via regulation of neuropeptide Y system in a rat model of abdominal aortic constriction
    Ailan Chen, Wanglin Li, Xinyu Chen, Yuechun Shen, Wenjun Dai, Qi Dong, Xinchun Li, Caiwen Ou, Minsheng Chen
    BMC Cardiovascular Disorders.2016;[Epub]     CrossRef
  • Corosolic acid ameliorates acute inflammation through inhibition of IRAK-1 phosphorylation in macrophages
    Seung-Jae Kim, Ji-Young Cha, Hye Suk Kang, Jae-Ho Lee, Ji Yoon Lee, Jae-Hyung Park, Jae-Hoon Bae, Dae-Kyu Song, Seung-Soon Im
    BMB Reports.2016; 49(5): 276.     CrossRef
  • The sulfiredoxin–peroxiredoxin (Srx–Prx) axis in cell signal transduction and cancer development
    Murli Mishra, Hong Jiang, Lisha Wu, Hedy A. Chawsheen, Qiou Wei
    Cancer Letters.2015; 366(2): 150.     CrossRef
  • Effects of methanolic extracts of edible plants on RAGE in high-glucose-induced human endothelial cells
    Mizue Okada, Yoshinori Okada
    Bio-Medical Materials and Engineering.2015; 25(3): 257.     CrossRef
  • Reactive oxygen species are physiological mediators of the noradrenergic signaling pathway in the mouse supraoptic nucleus
    Ronald St-Louis, Caroline Parmentier, Valérie Grange-Messent, Sakina Mhaouty-Kodja, Hélène Hardin-Pouzet
    Free Radical Biology and Medicine.2014; 71: 231.     CrossRef
  • Reactive oxygen species play a role in muscle wasting during thyrotoxicosis
    Sara Santos Bernardes, Flávia Alessandra Guarnier, Poliana Camila Marinello, André Armani, Andréa Name Colado Simão, Rubens Cecchini, Alessandra Lourenço Cecchini
    Cell and Tissue Research.2014; 357(3): 803.     CrossRef
  • Brief Review of Articles in 'Endocrinology and Metabolism' in 2013
    Won-Young Lee
    Endocrinology and Metabolism.2014; 29(3): 251.     CrossRef
Close layer

Endocrinol Metab : Endocrinology and Metabolism