Cited by 549Peroxisome Proliferator-Activated ReceptorsAdipose Tissue and MetabolismMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.

Adiponectin Increases Fatty Acid Oxidation in Skeletal Muscle Cells by Sequential Activation of AMP-Activated Protein Kinase, p38 Mitogen-Activated Protein Kinase, and Peroxisome Proliferator–Activated Receptor α

Open access

Yoon, Myeong Jin, Lee, Gha Young, Chung, Jun-Jae, Ahn, Young Ho, Hong, Seung Hwan, Kim, Jae Bum·2006·Diabetes

Open this paper in CoChat — free account Open PDF

Abstract

Adiponectin has recently received a great deal of attention due to its beneficial effects on insulin resistance and metabolic disorders. One of the mechanisms through which adiponectin exerts such effects involves an increase in fatty acid oxidation in muscle and liver. In the present study, we demonstrate that 5'-AMP-activated protein kinase (AMPK) and p38 mitogen-activated protein kinase (MAPK) are involved in the activation of peroxisome proliferator-activated receptor (PPAR)alpha by adiponectin in muscle cells. Adiponectin increases the transcriptional activity of PPARalpha and the expression of its target genes, including ACO, CPT1, and FABP3 in C2C12 myotubes. These effects were suppressed by the overexpression of a dominant-negative form of AMPK. Moreover, chemical inhibitors of AMPK and p38 MAPK potently repressed fatty acid oxidation and the induction of PPARalpha target gene expression by adiponectin. Interestingly, araA, an AMPK inhibitor, prevented the activation of p38 MAPK, whereas SB203580, a p38 MAPK inhibitor, did not affect AMPK activation, suggesting that p38 MAPK is a downstream signaling factor of AMPK. Taken together, these results suggest that adiponectin stimulates fatty acid oxidation in muscle cells by the sequential activation of AMPK, p38 MAPK, and PPARalpha.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.2337/db05-1322

Cites

48 of 48 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity
Yamauchi, T., Kamon, J., Waki, H., Terauchi, Y., Kubota, N., Hara, K., Mori, Y., Ide, T., Murakami, K., Tsuboyama-Kasaoka, N., et al. (2001) · Nature Medicine · doi:10.1038/90984 · Cited by 4,915
Paradoxical Decrease of an Adipose-Specific Protein, Adiponectin, in Obesity
Arita, Y., Kihara, S., Ouchi, N., Takahashi, M., Maeda, K., Miyagawa, J.-I., Hotta, K., Shimomura, I., Nakamura, T., Miyaoka, K., et al. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0255 · Cited by 4,856
Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
A Novel Serum Protein Similar to C1q, Produced Exclusively in Adipocytes
Scherer, P. E., Williams, S. P., Fogliano, M., Baldini, G., & Lodish, H. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26746 · Cited by 3,238
Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176
Plasma Concentrations of a Novel, Adipose-Specific Protein, Adiponectin, in Type 2 Diabetic Patients
Hotta, K., Funahashi, T., Arita, Y., Takahashi, M., Matsuda, M., Okamoto, Y., Iwahashi, H., Kuriyama, H., Ouchi, N., Maeda, K., et al. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.6.1595 · Cited by 3,133
Adiponectin and Adiponectin Receptors
Kadowaki, T., & Yamauchi, T. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0005 · Cited by 2,634
The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
Berg, A. H., Combs, T. P., Du, X., Brownlee, M., & Scherer, P. E. (2001) · Nature Medicine · doi:10.1038/90992 · Cited by 2,526
AdipoQ Is a Novel Adipose-specific Gene Dysregulated in Obesity
Hu, E., Liang, P., & Spiegelman, B. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10697 · Cited by 2,261
Novel Modulator for Endothelial Adhesion Molecules
Ouchi, N., Kihara, S., Arita, Y., Maeda, K., Kuriyama, H., Okamoto, Y., Hotta, K., Nishida, M., Takahashi, M., Nakamura, T., et al. (1999) · Circulation · doi:10.1161/01.cir.100.25.2473 · Cited by 2,158

Flagged first, then by citations

Show all 48 references

Sorted by citations

Molecular mechanism of PPARα action and its impact on lipid metabolism, inflammation and fibrosis in non-alcoholic fatty liver disease
Pawlak, M., Lefebvre, P., & Staels, B. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2014.10.039 · Cited by 1,578
Adipose Tissue Remodeling: Its Role in Energy Metabolism and Metabolic Disorders
Choe, S. S., Huh, J. Y., Hwang, I. J., Kim, J. I., & Kim, J. B. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00030 · Cited by 1,206
Adiponectin, a Therapeutic Target for Obesity, Diabetes, and Endothelial Dysfunction
Elumalai, A., & Jain, S. K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061321 · Cited by 1,206
Adiponectin, Leptin, and Fatty Acids in the Maintenance of Metabolic Homeostasis through Adipose Tissue Crosstalk
Stern, J. H., Rutkowski, J. M., & Scherer, P. E. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.011 · Cited by 1,031
Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism
Yu, P. B., Hong, C. C., Sachidanandan, C., Babitt, J. L., Deng, D. Y., Hoyng, S. A., Lin, H. Y.-F., Bloch, K. D., & Peterson, R. T. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.54 · Cited by 1,059
The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation
Plotnikov, A. N., Zehorai, E., Procaccia, S., & Seger, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.012 · Cited by 1,021
Osteocalcin differentially regulates β cell and adipocyte gene expression and affects the development of metabolic diseases in wild-type mice
Ferron, M., Hinoi, E., Karsenty, G., & Ducy, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711119105 · Cited by 900
Molecular Actions of PPARα in Lipid Metabolism and Inflammation
Bougarne, N., Weyers, B., Desmet, S. J., Deckers, J., Ray, D. W., Staels, B., & De Bosscher, K. (2018) · Endocrine Reviews · doi:10.1210/er.2018-00064 · Cited by 898
Health Implications of High Dietary Omega-6 Polyunsaturated Fatty Acids
Patterson, E., Wall, R., Fitzgerald, G. F., Ross, R. P., & Stanton, C. (2012) · Journal of Nutrition and Metabolism · doi:10.1155/2012/539426 · Cited by 944
Cardiac Metabolism and its Interactions With Contraction, Growth, and Survival of Cardiomyocytes
Kolwicz, S. C., Purohit, S., & Tian, R. (2013) · Circulation Research · doi:10.1161/circresaha.113.302095 · Cited by 838
Recent insights into hepatic lipid metabolism in non-alcoholic fatty liver disease (NAFLD)
Musso, G., Gambino, R. J., & Cassader, M. (2008) · Progress in Lipid Research · doi:10.1016/j.plipres.2008.08.001 · Cited by 691
Transcriptional Control of Mitochondrial Biogenesis and Function
Hock, M. B., & Kralli, A. (2009) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163119 · Cited by 626
Autophagy: The spotlight for cellular stress responses
Ravanan, P., Florance, I., & Talwar, P. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.08.029 · Cited by 595
Modulation of PPAR activity via phosphorylation
Burns, K. H., & VANDENHEUVEL, J. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.04.018 · Cited by 455
Molecular Mechanisms and Therapeutic Targets in Steatosis and Steatohepatitis
Anderson, N., & Borlak, J. T. (2008) · Pharmacological Reviews · doi:10.1124/pr.108.00001 · Cited by 395
Adiponectin: Role in Physiology and Pathophysiology
Nguyen, T. M. D. (2020) · International Journal of Preventive Medicine · doi:10.4103/ijpvm.ijpvm_193_20 · Cited by 390
AMP-Activated Protein Kinase in the Heart
Arad, M., Seidman, C. E., & Seidman, J. G. (2007) · Circulation Research · doi:10.1161/01.res.0000258446.23525.37 · Cited by 357
Adiponectin in relation to malignancies: a review of existing basic research and clinical evidence
Barb, D., Williams, C. J., Neuwirth, A., & Mantzoros, C. S. (2007) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/86.3.858s · Cited by 343
Aging human body: changes in bone, muscle and body fat with consequent changes in nutrient intake
JafariNasabian, P., Inglis, J. E., Reilly, W., Kelly, O. J., & Ilich, J. Z. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0603 · Cited by 310
Adiponectin action from head to toe
Brochu‐Gaudreau, K., Rehfeldt, C., Blouin, R., Bordignon, V., Murphy, B. D., & Palin, M. (2009) · Endocrine · doi:10.1007/s12020-009-9278-8 · Cited by 330
Review on leptin and adiponectin responses and adaptations to acute and chronic exercise
Bouassida, A., Chamari, K., Zaouali, M., Feki, Y., Zbidi, A., & Tabka, Z. (2010) · British Journal of Sports Medicine · doi:10.1136/bjsm.2008.046151 · Cited by 290
Myokines and Adipokines: Involvement in the Crosstalk between Skeletal Muscle and Adipose Tissue
Li, F., Li, Y., Duan, Y., Hu, C.-A. A., Tang, Y., & Yin, Y. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.10.003 · Cited by 288
APPL1: role in adiponectin signaling and beyond
Deepa, S. S., & Dong, L. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90731.2008 · Cited by 295
Interrelationship among muscle, fat, and bone: Connecting the dots on cellular, hormonal, and whole body levels
Ilich, J. Z., Kelly, O. J., Inglis, J. E., Panton, L. B., Duque, G., & Ormsbee, M. J. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.02.007 · Cited by 282
AdPLA ablation increases lipolysis and prevents obesity induced by high-fat feeding or leptin deficiency
Jaworski, K., Ahmadian, M., Duncan, R. E., Sarkadi‐Nagy, E., Varady, K. A., Hellerstein, M. K., Lee, H., Samuel, V. T., Shulman, G. I., Kim, K.-H., et al. (2009) · Nature Medicine · doi:10.1038/nm.1904 · Cited by 267
C1q/TNF-related Protein-3 (CTRP3), a Novel Adipokine That Regulates Hepatic Glucose Output
Peterson, J. M., Wei, Z., & Wong, G. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.180695 · Cited by 255
Adiponectin, driver or passenger on the road to insulin sensitivity?
Ye, R., & Scherer, P. E. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.04.001 · Cited by 251
Adiponectin Enhances IL-6 Production in Human Synovial Fibroblast via an AdipoR1 Receptor, AMPK, p38, and NF-κB Pathway
Tang, C., Chiu, Y., Tan, T., Yang, R., & Fu, W. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.8.5483 · Cited by 247
Clinical review: Adiponectin biology and its role in inflammation and critical illness
Robinson, K., Prins, J. B., & Venkatesh, B. (2011) · Critical Care · doi:10.1186/cc10021 · Cited by 243
Adiponectin, Obesity, and Cancer: Clash of the Bigwigs in Health and Disease
Parida, S., Siddharth, S., & Sharma, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102519 · Cited by 248
Alteration of fatty acid oxidation by increased CPT1A on replicative senescence of placenta-derived mesenchymal stem cells
Seok, J., Jung, H. S., Park, S., Lee, J. O., Kim, C. J., & Kim, G. J. (2020) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1471-y · Cited by 242
Berberine decreases PCSK9 expression in HepG2 cells
Cameron, J., Ranheim, T., Kulseth, M. A., Leren, T. P., & Berge, K. E. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.02.004 · Cited by 232
Nonalcoholic fatty liver disease in adults: current concepts in etiology, outcomes, and management
Marjot, T., Moolla, A., Cobbold, J. F., Hodson, L., & Tomlinson, J. W. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnz009 · Cited by 228
Dietary methionine restriction enhances metabolic flexibility and increases uncoupled respiration in both fed and fasted states
Hasek, B. E., Stewart, L. K., Henagan, T. M., Boudreau, A., Lenard, N. R., Black, C. L., Shin, J., Huypens, P., Malloy, V. L., Plaisance, E. P., et al. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00837.2009 · Cited by 223
Metabolic syndrome: an update on diagnostic criteria, pathogenesis, and genetic links
Zafar, U., Khaliq, S., Ahmad, H., Manzoor, S., & Lone, K. P. (2018) · HORMONES · doi:10.1007/s42000-018-0051-3 · Cited by 230
Lipid metabolism in mammalian tissues and its control by retinoic acid
Bonet, M. L., Ribot, J., & Palou, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.06.001 · Cited by 218
Adiponectin Represses Colon Cancer Cell Proliferation via AdipoR1- and -R2-Mediated AMPK Activation
Kim, A. Y., Lee, Y. S., Kim, K. H., Lee, J. H., Lee, H. K., Jang, S. H., Kim, S., Lee, G. Y., Lee, J.-W., Jung, S.-A., et al. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0498 · Cited by 214
Pathophysiology of Sepsis-Related Cardiac Dysfunction: Driven by Inflammation, Energy Mismanagement, or Both?
Drosatos, K., Lymperopoulos, A., Kennel, P. J., Pollak, N. M., Schulze, P. C., & Goldberg, I. J. (2014) · Current Heart Failure Reports · doi:10.1007/s11897-014-0247-z · Cited by 219
Leptin Stimulates Fatty Acid Oxidation and Peroxisome Proliferator-Activated Receptor α Gene Expression in Mouse C2C12 Myoblasts by Changing the Subcellular Localization of the α2 Form of AMP-Activated Protein Kinase
Suzuki, A., Okamoto, S., Lee, S. P., Saito, K., Shiuchi, T., & Minokoshi, Y. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02222-06 · Cited by 213
Exercise Alleviates Obesity-Induced Metabolic Dysfunction via Enhancing FGF21 Sensitivity in Adipose Tissues
Geng, L., Liao, B., Jin, L., Huang, Z. P., Triggle, C. R., Ding, H., Zhang, J., Huang, Y., Lin, Z., & Xu, A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.014 · Cited by 208
The Emerging Role of Adipokines as Mediators of Cardiovascular Function: Physiologic and Clinical Perspectives
Gualillo, O., González-Juanatey, J. R., & Lago, F. (2007) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2007.09.005 · Cited by 193
Probiotics as an emerging therapeutic strategy to treat NAFLD: focus on molecular and biochemical mechanisms
Iacono, A., Raso, G. M., Canani, R. B., Calignano, A., & Meli, R. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.10.002 · Cited by 197
PPARγ inhibits NF-κB-dependent transcriptional activation in skeletal muscle
Remels, A. H. V., LANGEN, R. C. J., Gosker, H. R., Russell, A. P., Spaapen, F., Voncken, J. W., Schrauwen, P., & Schols, A. M. W. J. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90632.2008 · Cited by 194
Regulation of adiponectin and its receptors in rat ovary by human chorionic gonadotrophin treatment and potential involvement of adiponectin in granulosa cell steroidogenesis
Chabrolle, C., Tosca, L., & Dupont, J. (2007) · Reproduction · doi:10.1530/rep-06-0244 · Cited by 191
The Adipokine Hypothesis of Heart Failure With a Preserved Ejection Fraction
Packer, M. (2025) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2025.06.055 · Cited by 213
Obesity and Kidney Disease
Lakkis, J. I., & Weir, M. R. (2018) · Progress in Cardiovascular Diseases · doi:10.1016/j.pcad.2018.07.005 · Cited by 191
Adiponectin suppresses gluconeogenic gene expression in mouse hepatocytes independent of LKB1-AMPK signaling
Miller, R., Chu, Q., Lay, J. E. L., Scherer, P. E., Ahima, R. S., Kaestner, K. H., Foretz, M., Viollet, B., & Birnbaum, M. J. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45942 · Cited by 188
Effects of experimental weight perturbation on skeletal muscle work efficiency, fuel utilization, and biochemistry in human subjects
Goldsmith, R., Joanisse, D. R., Gallagher, D., Pavlovich, K., Shamoon, E., Leibel, R. L., & Rosenbaum, M. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00053.2009 · Cited by 171
LKB1 is required for adiponectin-mediated modulation of AMPK–S6K axis and inhibition of migration and invasion of breast cancer cells
Taliaferro-Smith, L., Nagalingam, A., Zhong, D., Zhou, W., Saxena, N. K., & Sharma, D. (2009) · Oncogene · doi:10.1038/onc.2009.129 · Cited by 173
Adiponectin and energy homeostasis
Lee, B., & Shao, J. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9283-3 · Cited by 179
Activation of AMPKα2 in adipocytes is essential for nicotine-induced insulin resistance in vivo
Wu, Y., Song, P., Zhang, W., Liu, J., Dai, X., Liu, Z., Lu, Q., Ouyang, C., Xie, Z., Zhao, Z., et al. (2015) · Nature Medicine · doi:10.1038/nm.3826 · Cited by 169
Adiponectin is expressed by skeletal muscle fibers and influences muscle phenotype and function
Krause, M. P., Liu, Y., Vu, V., Chan, L., Xu, A., Riddell, M. C., Sweeney, G., & Hawke, T. J. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00030.2008 · Cited by 168
Lipotoxicity in obesity and diabetes-related cardiac dysfunction
Zlobine, I., Gopal, K., & Ussher, J. R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.02.011 · Cited by 172
Lactobacillus plantarum KLDS1.0344 and Lactobacillus acidophilus KLDS1.0901 Mixture Prevents Chronic Alcoholic Liver Injury in Mice by Protecting the Intestinal Barrier and Regulating Gut Microbiota and Liver-Related Pathways
Li, H., Shi, J., Zhao, L. M., Guan, J., Liu, F., Huo, G., & Li, B. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c06346 · Cited by 172
Clock Genes and Clock-Controlled Genes in the Regulation of Metabolic Rhythms
Mazzoccoli, G., Pazienza, V., & Vinciguerra, M. (2012) · Chronobiology International · doi:10.3109/07420528.2012.658127 · Cited by 173
AdipoR1 mediates the anorexigenic and insulin/leptin‐like actions of adiponectin in the hypothalamus
Coope, A., Milanski, M., ARAUJO, E. P. D., Tambascia, M. A., Saad, M. J. A., Geloneze, B., & Velloso, L. A. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.037 · Cited by 168
Adiponectin receptors are expressed in hypothalamus and colocalized with proopiomelanocortin and neuropeptide Y in rodent arcuate neurons
Guillod-Maximin, E., Roy, A.-F., Vacher, C., Aubourg, A., Bailleux, V., Lorsignol, A., Pénicaud, L., Parquet, M., & Taouis, M. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0348 · Cited by 168
Adiponectin knockout accentuates high fat diet-induced obesity and cardiac dysfunction: Role of autophagy
Guo, R., Zhang, Y., Turdi, S., & Ren, J. T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.013 · Cited by 165
PHD3 Loss in Cancer Enables Metabolic Reliance on Fatty Acid Oxidation via Deactivation of ACC2
German, N. J., Yoon, H., Yusuf, R. Z., Murphy, J. P., Finley, L. W. S., Laurent, G., Haas, W., Satterstrom, F. K., Guarnerio, J., Zaganjor, E., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.014 · Cited by 156
Adiponectin Modulates C-Jun N-Terminal Kinase and Mammalian Target of Rapamycin and Inhibits Hepatocellular Carcinoma
Saxena, N. K., Fu, P. P., Nagalingam, A., Wang, J., Handy, J. A., Cohen, C., Tighiouart, M., Sharma, D., & Anania, F. A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.07.001 · Cited by 157
Functional Adiponectin Resistance at the Level of the Skeletal Muscle in Mild to Moderate Chronic Heart Failure
Berendoncks, A. M. V., Garnier, A., Beckers, P. J., Hoymans, V. Y., Possemiers, N. M., Fortin, D., Martinet, W., Hoof, V. O. V., Vrints, C. J., Ventura‐Clapier, R., et al. (2010) · Circulation Heart Failure · doi:10.1161/circheartfailure.109.885525 · Cited by 154
Review: Adiponectin – The missing link between maternal adiposity, placental transport and fetal growth?
Aye, I. L. M. H., Powell, T. L., & Jansson, T. (2012) · Placenta · doi:10.1016/j.placenta.2012.11.024 · Cited by 158
Role of peroxisome proliferators-activated receptors in the pathogenesis and treatment of nonalcoholic fatty liver disease
Kallwitz, E. R., McLachlan, A., & Cotler, S. J. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.22 · Cited by 152
Exogenous cell-permeable C6 ceramide sensitizes multiple cancer cell lines to Doxorubicin-induced apoptosis by promoting AMPK activation and mTORC1 inhibition
Ji, C., Yang, B., Yang, Y.-L., He, S.-H., Miao, D.-S., He, L., & Bi, Z.-G. (2010) · Oncogene · doi:10.1038/onc.2010.379 · Cited by 149
Deciphering the Nutraceutical Potential of Raphanus sativus—A Comprehensive Overview
Manivannan, A., Kim, J., Kim, D., Lee, E.-S., & Lee, H. (2019) · Nutrients · doi:10.3390/nu11020402 · Cited by 157
Resveratrol ameliorates diabetes‐related metabolic changes via activation of AMP‐activated protein kinase and its downstream targets in db/db mice
Do, G., Jung, U. J., Park, H., Kwon, E., Jeon, S.-M., McGregor, R. A., & Choi, M. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200067 · Cited by 142
High-fat diet delays and fasting advances the circadian expression of adiponectin signaling components in mouse liver
Barnea, M., Madar, Z., & Froy, O. (2009) · Endocrinology · doi:10.1210/en.2008-0944 · Cited by 138
Adipokines as regulators of muscle metabolism and insulin sensitivityThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process.
Dyck, D. J. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-037 · Cited by 136
Adiponectin Stimulates Osteoblast Differentiation Through Induction of COX2 in Mesenchymal Progenitor Cells
Lee, H. W., Kim, S., Kim, A., Lee, E. J., Choi, J., & Kim, J. B. (2009) · Stem Cells · doi:10.1002/stem.144 · Cited by 139
Carnitine palmitoyltransferase 1A functions to repress FoxO transcription factors to allow cell cycle progression in ovarian cancer
Shao, H., Mohamed, E., Xu, G. G., Waters, M. R., Jing, K., Ma, Y., Zhang, Y., Spiegel, S., Idowu, M. O., & Fang, X. (2015) · Oncotarget · doi:10.18632/oncotarget.6757 · Cited by 137
Mechanisms of enhanced insulin secretion and sensitivity with n-3 unsaturated fatty acids
Bhaswant, M., Poudyal, H., & Brown, L. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.02.001 · Cited by 133
Berberine Promotes Osteoblast Differentiation by Runx2 Activation With p38 MAPK
Lee, H. W., Suh, J. H., Kim, H.-N., Kim, A., Park, S. Y., Shin, C. S., Choi, J., & Kim, J. B. (2008) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.080325 · Cited by 130
Adiponectin as a potential biomarker of vascular disease
Mohammadi, S., Arefhosseini, S. R., Ebrahimi‐Mameghani, M., Fallah, P., & Bazi, Z. (2015) · Vascular Health and Risk Management · doi:10.2147/vhrm.s48753 · Cited by 129
Full-Length Adiponectin Attenuates Insulin Signaling and Inhibits Insulin-Stimulated Amino Acid Transport in Human Primary Trophoblast Cells
Jones, H. N., Jansson, T., & Powell, T. L. (2010) · Diabetes · doi:10.2337/db09-0824 · Cited by 136
The role of adipokines in skeletal muscle inflammation and insulin sensitivity
Nicholson, T. A., Church, C., Baker, D. J., & Jones, S. W. (2018) · Journal of Inflammation · doi:10.1186/s12950-018-0185-8 · Cited by 133
Activated AMPK inhibits PPAR-α and PPAR-γ transcriptional activity in hepatoma cells
Sozio, M. S., Lu, C., Zeng, Y., Liangpunsakul, S., & Crabb, D. W. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00432.2010 · Cited by 131
Anti‐obesity and hypolipidemic effects of Fuzhuan brick tea water extract in high‐fat diet‐induced obese rats
Li, Q., Liu, Z., Huang, J., Luo, G., Liang, Q., Wang, D., Ye, X., Wu, C., Wang, L., & Hu, J. (2012) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.5887 · Cited by 125
Anti‐Obesity and Anti‐Diabetic Effects of Acacia Polyphenol in Obese Diabetic KKAy Mice Fed High‐Fat Diet
Ikarashi, N., Toda, T., Okaniwa, T., Ito, K., Ochiai, W., & Sugiyama, K. (2010) · Evidence-based Complementary and Alternative Medicine · doi:10.1093/ecam/nep241 · Cited by 124
Enhancing cancer‐associated fibroblast fatty acid catabolism within a metabolically challenging tumor microenvironment drives colon cancer peritoneal metastasis
Peng, S., Chen, D., Cai, J. Q., Yuan, Z., Huang, B., Li, Y., Wang, H., Luo, Q., Kuang, Y., Liang, W., et al. (2021) · Molecular Oncology · doi:10.1002/1878-0261.12917 · Cited by 123
Regulation of longevity by FGF21: interaction between energy metabolism and stress responses
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.05.004 · Cited by 121
Adiponectin: A Promising Target for the Treatment of Diabetes and Its Complications
Begum, M., Choubey, M., Tirumalasetty, M. B., Arbee, S., Mohib, M. M., Wahiduzzaman, M., Mamun, M. A., Uddin, M. B., & Mohiuddin, M. S. (2023) · Life · doi:10.3390/life13112213 · Cited by 138
Selective activation of PPARγ in skeletal muscle induces endogenous production of adiponectin and protects mice from diet-induced insulin resistance
Amin, R., Mathews, S. T., Camp, H. S., Ding, L., & Leff, T. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00446.2009 · Cited by 120
Adipose Tissue: Physiology to Metabolic Dysfunction
Richard, A. J., White, U. A., Elks, C. M., & Stephens, J. M. (2020) · Europe PMC (PubMed Central) · Cited by 118
Adiponectin triggers breast cancer cell death via fatty acid metabolic reprogramming
Pham, D., & Park, P. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02223-y · Cited by 123
Role of adipokines and peroxisome proliferator-activated receptors in nonalcoholic fatty liver disease
Giby, V. G., & Ajith, T. A. (2014) · World Journal of Hepatology · doi:10.4254/wjh.v6.i8.570 · Cited by 118
An APPL1-AMPK signaling axis mediates beneficial metabolic effects of adiponectin in the heart
Fang, X., Palanivel, R., Cresser, J., Schram, K., Ganguly, R., Thong, F. S. L., Tuinei, J., Xu, A., Abel, E. D., & Sweeney, G. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00086.2010 · Cited by 119
Adiponectin: Probe of the molecular paradigm associating diabetes and obesity
Ghoshal, K. (2015) · World Journal of Diabetes · doi:10.4239/wjd.v6.i1.151 · Cited by 125
Adiponectin: an adipokine with protective features against metabolic syndrome.
Esfahani, M., Movahedian, A., Baranchi, M., & Goodarzi, M. T. (2015) · Europe PMC (PubMed Central) · Cited by 111
Maternal Overweight Programs Insulin and Adiponectin Signaling in the Offspring
Shankar, K., Kang, P., Harrell, A., Zhong, Y., Marecki, J. C., Ronis, M. J. J., & Badger, T. M. (2010) · Endocrinology · doi:10.1210/en.2010-0017 · Cited by 107
Adiponectin action in skeletal muscle
Liu, Y., & Sweeney, G. (2013) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2013.08.003 · Cited by 111
Influence of Acute and Chronic Exercise on Glucose Uptake
Röhling, M., Herder, C., Stemper, T., & Müssig, K. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2868652 · Cited by 114
C1q Tumor Necrosis Factor α-related Protein Isoform 5 Is Increased in Mitochondrial DNA-depleted Myocytes and Activates AMP-activated Protein Kinase
Park, S., Choi, J. H., Ryu, H. S., Pak, Y. K., Park, K. S., Lee, H. K., & Lee, W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.005611 · Cited by 107
Placental Function and the Development of Fetal Overgrowth and Fetal Growth Restriction
Dumolt, J. H., Powell, T. L., & Jansson, T. (2021) · Obstetrics and Gynecology Clinics of North America · doi:10.1016/j.ogc.2021.02.001 · Cited by 111
AMP-activated Protein Kinase Contributes to UV- and H2O2-induced Apoptosis in Human Skin Keratinocytes
Cao, C., Lü, S., Kivlin, R., Wallin, B., Card, E., Bagdasarian, A., Tamakloe, T., Chu, W., Guan, K., & Wan, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804144200 · Cited by 104
Retracted
Regulation of adiponectin production by insulin: interactions with tumor necrosis factor-α and interleukin-6
Hajri, T., Tao, H., Wattacheril, J. J., Marks–Shulman, P. A., & Abumrad, N. N. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00307.2010 · Cited by 105
Maternal-fetal cross-talk via the placenta: influence on offspring development and metabolism
Kramer, A. C., Jansson, T., Bale, T. L., & Powell, T. L. (2023) · Development · doi:10.1242/dev.202088 · Cited by 119
Molecular mechanisms of signal transduction via adiponectin and adiponectin receptors
Heiker, J. T., Kosel, D., & Beck‐Sickinger, A. G. (2010) · Biological Chemistry · doi:10.1515/bc.2010.104 · Cited by 105
Gender-Related Differences in the Metabolic Response to Fasting
Soeters, M. R., Sauerwein, H. P., Groener, J. E. M., Aerts, J. M. F. G., Ackermans, M. T., Glatz, J. F. C., Fliers, E., & Serlie, M. J. M. (2007) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-0552 · Cited by 107
Elevated Production of Docosahexaenoic Acid in Females: Potential Molecular Mechanisms
Kitson, A. P., Stroud, C. K., & Stark, K. D. (2010) · Lipids · doi:10.1007/s11745-010-3391-6 · Cited by 106
AMPK activation with glabridin ameliorates adiposity and lipid dysregulation in obesity
Lee, J.-W., Choe, S. S., Jang, H., Kim, J., Jeong, H. W., Jo, H., Jeong, K.-H., Tadi, S., Park, M. G., Kwak, T. H., et al. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m022897 · Cited by 102

Authors: Yoon, M. J., Lee, G. Y., Chung, J.-J., Ahn, Y. H., Hong, S. H., & Kim, J. B.
Affiliations: Seoul National University (KR)
ORCID: Chung, Jun-Jae
Hong, Seung Hwan
Kim, Jae Bum
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2006-09-01
Volume: 55
Issue: 9
Pages: 2562-2570
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/db05-1322
OpenAlex: W2139409926
Cited by: 546
References: 48
Citations by year: 2026: 18 · 2025: 27 · 2024: 20 · 2023: 24 · 2022: 20 · 2021: 26 · 2020: 32 · 2019: 28 · 2018: 28 · 2017: 24 · 2016: 25 · 2015: 31 · 2014: 34 · 2013: 33 · 2012: 27
FWCI: 11.89
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Diabetes (publishedVersion)
PubMed (publishedVersion)
Funders: Ministry of Education and Human Resources Development
Directorate for Education and Human Resources
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: adiponectin, fatty acid oxidation, skeletal muscle, AMPK, p38 MAPK, PPARα, C2C12 myotubes, PPARα target genes, acetyl-CoA oxidase, carnitine palmitoyltransferase 1, fatty acid binding protein 3, insulin resistance
MeSH terms: Animals, Carnitine O-Palmitoyltransferase, Cells, Cultured, Enzyme Activation, Fatty Acids, Humans, Multienzyme Complexes, Oxidation-Reduction, Transcription, Genetic, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Acyl-CoA Oxidase, PPAR alpha, p38 Mitogen-Activated Protein Kinases, Mice, Adiponectin, AMP-Activated Protein Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Adiponectin Increases Fatty Acid Oxidation in Skeletal Muscle Cells by Sequential Activation of AMP-Activated Protein Kinase, p38 Mitogen-Activated Protein Kinase, and Peroxisome Proliferator–Activated Receptor α

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks