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Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Abstract
Adiponectin (also known as 30-kDa adipocyte complement-related protein; Acrp30) is a hormone secreted by adipocytes that acts as an antidiabetic and anti-atherogenic adipokine. Levels of adiponectin in the blood are decreased under conditions of obesity, insulin resistance and type 2 diabetes. Administration of adiponectin causes glucose-lowering effects and ameliorates insulin resistance in mice. Conversely, adiponectin-deficient mice exhibit insulin resistance and diabetes. This insulin-sensitizing effect of adiponectin seems to be mediated by an increase in fatty-acid oxidation through activation of AMP kinase and PPAR-alpha. Here we report the cloning of complementary DNAs encoding adiponectin receptors 1 and 2 (AdipoR1 and AdipoR2) by expression cloning. AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. These two adiponectin receptors are predicted to contain seven transmembrane domains, but to be structurally and functionally distinct from G-protein-coupled receptors. Expression of AdipoR1/R2 or suppression of AdipoR1/R2 expression by small-interfering RNA supports our conclusion that they serve as receptors for globular and full-length adiponectin, and that they mediate increased AMP kinase and PPAR-alpha ligand activities, as well as fatty-acid oxidation and glucose uptake by adiponectin.
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“This translocation results from stimulating p38 MAPK via either AMPK [10,44] or interaction with APPL1 [55].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [10]
In the citing paper
“Third, ApN induces the translocation of GLUT4 to the plasma membrane, thereby promoting glucose uptake [10,54].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [10]
Citations
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,927
Initial sequencing and comparative analysis of the mouse genome
Mouse Genome Sequencing Consortium (2002) · Nature · doi:10.1038/nature01262 · Cited by 7,187
Efficient selection for high-expression transfectants with a novel eukaryotic vector
Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,149
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
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
Self-citationA 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
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
Diet-induced insulin resistance in mice lacking adiponectin/ACRP30
Maeda, N., Shimomura, I., Kishida, K., Nishizawa, H., Matsuda, M., Nagaretani, H., Furuyama, N., Kondo, H., Takahashi, M., Arita, Y., et al. (2002) · Nature Medicine · doi:10.1038/nm724 · Cited by 2,114
Maeda, K., Okubo, K., Shimomura, I., Funahashi, T., Matsuzawa, Y., & Matsubara, K. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0587 · Cited by 2,081
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Adipose Tissue as an Endocrine Organ
Kershaw, E. E., & Flier, J. S. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0395 · Cited by 5,522
Adipokines in inflammation and metabolic disease
Ouchi, N., Parker, J. L., Lugus, J. J., & Walsh, K. (2011) · Nature Reviews Immunology · doi:10.1038/nri2921 · Cited by 4,625
Pathophysiology of type 2 diabetes mellitus
Galicia-Garcia, U., Benito-Vicente, A., Jebari, S., Larrea-Sebal, A., Siddiqi, H., Uribe, K. B., Ostolaza, H., & Martín, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176275 · Cited by 3,360
“Adiponectin acts through ADIPOR1 and ADIPOR2 receptors [262] and the peroxisome proliferator-activated receptor α (PPARα) pathway, leading to decreased hepatic gluconeogenesis, increased liver and skeletal muscle fatty acid oxidation, increased glucose uptake in skeletal muscle and white adipose tissue, and decreased…”
BackgroundAdipocytokines: mediators linking adipose tissue, inflammation and immunity
Tilg, H., & Moschen, A. R. (2006) · Nature reviews. Immunology · doi:10.1038/nri1937 · Cited by 3,272
Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
Kadowaki, T. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29126 · Cited by 2,824
Self-citationAdiponectin and Adiponectin Receptors
Kadowaki, T., & Yamauchi, T. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0005 · Cited by 2,634
Adipocytes as regulators of energy balance and glucose homeostasis
Rosen, E. D., & Spiegelman, B. M. (2006) · Nature · doi:10.1038/nature05483 · Cited by 2,170
Recent advances in the relationship between obesity, inflammation, and insulin resistance.
Bastard, J., Maachi, M., Lagathu, C., Kim, M. J., Caron, M., Vidal, H., Capeau, J., & Fève, B. (2006) · PubMed · Cited by 2,090
PPARs and the complex journey to obesity
Evans, R. M., Barish, G. D., & Wang, Y.-X. (2004) · Nature Medicine · doi:10.1038/nm1025 · Cited by 1,650
Adipose tissue as an endocrine organ
Galić, S., Oakhill, J. S., & Steinberg, G. R. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.08.018 · Cited by 1,654
Chait, A., & den Hartigh, L. J. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00022 · Cited by 1,529
“Adiponectin signals through two related receptors, ADIPOR1 and ADIPOR2, followed by docking of the adaptor protein APPL1 (98).”
BackgroundAdipose tissue dysfunction in obesity, diabetes, and vascular diseases
Hajer, G. R., van Haeften, T. W., & Visseren, F. L. J. (2008) · European Heart Journal · doi:10.1093/eurheartj/ehn387 · Cited by 1,410
Yamauchi, T., Nio, Y., Maki, T., Kobayashi, M., Takazawa, T., Iwabu, M., Okada-Iwabu, M., Kawamoto, S., Kubota, N., Kubota, T., et al. (2007) · Nature Medicine · doi:10.1038/nm1557 · Cited by 1,396
Self-citationAdapting to obesity with adipose tissue inflammation
Reilly, S. M., & Saltiel, A. R. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.90 · Cited by 1,204
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
“Unlike all other GPCRs reported, AdipoR1 and AdipoR2 have an inverte membrane topology with a cyt plasmic NH2 terminus and a short, extracellular COOH terminal domain of approximately 25 amino acids [31].”
BackgroundInfluentialManna, P., & Jain, S. K. (2015) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2015.0095 · Cited by 1,211
“The gAd transgenetic ob/ob mice (a cross between the gAd transgenetic mice and leptin-deficient ob/ob mice) exhibit higher plasma insulin levels, along with increased insulin sensitivity, compared to those seen in ob/ob litter-mates, indicating that adiponectin protects b-cells.(242,243) A direct effect of adiponectin…”
BackgroundFlier, J. S. (2004) · Cell · doi:10.1016/s0092-8674(03)01081-x · Cited by 1,124
Scherer, P. E. (2006) · Diabetes · doi:10.2337/db06-0263 · Cited by 1,092
Stern, J. H., Rutkowski, J. M., & Scherer, P. E. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.011 · Cited by 1,031
“Ectopic Lipid Accumulation in the Pancreatic b Cell Adiponectin: Subsequent to the cloning of the adiponectin receptors adipoR1 and adipoR2, (Yamauchi et al., 2003), Kharroubi and colleagues showed that both human and rodent pancreatic b cells express mRNAs for the adiponectin receptors, adipoR1…”
BackgroundAdipose 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
Meier, U., & Gressner, A. M. (2004) · Clinical Chemistry · doi:10.1373/clinchem.2004.032482 · Cited by 1,048
Adipokine dysregulation, adipose tissue inflammation and metabolic syndrome
Maury, E., & Brichard, S. M. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.07.031 · Cited by 1,026
Adiponectin Stimulates Production of Nitric Oxide in Vascular Endothelial Cells
Chen, H., Montagnani, M., Funahashi, T., Shimomura, I., & Quon, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307878200 · Cited by 995
Adiponectin and AdipoR1 Regulate PGC-1α and Mitochondria by Ca2+ and AMPK/SIRT1
Iwabu, M., Yamauchi, T., Okada-Iwabu, M., Sato, K., Nakagawa, T., Funata, M., Yamaguchi, M., Namiki, S., Nakayama, R., Tabata, M., et al. (2010) · Nature · doi:10.1038/nature08991 · Cited by 971
Receptor-mediated activation of ceramidase activity initiates the pleiotropic actions of adiponectin
Holland, W. L., Miller, R. A., Wang, Z. V., Sun, K., Barth, B. M., Bui, H. H., Davis, K. E., Bikman, B. T., Halberg, N., Rutkowski, J. M., et al. (2011) · Nature Medicine · doi:10.1038/nm.2277 · Cited by 892
Adiponectin as an anti-inflammatory factor
Ouchi, N., & Walsh, K. X. (2007) · Clinica Chimica Acta · doi:10.1016/j.cca.2007.01.026 · Cited by 910
T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin
Hug, C., Wang, J., Ahmad, N. S., Bogan, J. S., Tsao, T., & Lodish, H. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403382101 · Cited by 873
Adiponectin Stimulates AMP-Activated Protein Kinase in the Hypothalamus and Increases Food Intake
Kubota, N., Yano, W., Kubota, T., Yamauchi, T., Itoh, S., Kumagai, H., Kozono, H., Takamoto, I., Okamoto, S., Shiuchi, T., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.06.003 · Cited by 844
Metabolic Syndrome and Insulin Resistance: Underlying Causes and Modification by Exercise Training
Roberts, C. K., Hevener, A. L., & Barnard, R. J. (2012) · Comprehensive physiology · doi:10.1002/cphy.c110062 · Cited by 966
Regulation of energy metabolism by long-chain fatty acids
Nakamura, M., Yudell, B. E., & Loor, J. J. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.12.001 · Cited by 858
Adipokines and Insulin Resistance
Rabe, K., Lehrke, M., Parhofer, K. G., & Broedl, U. C. (2008) · Molecular Medicine · doi:10.2119/2008-00058.rabe · Cited by 828
Adiponectin acts in the brain to decrease body weight
Qi, Y., Takahashi, N., Hileman, S. M., Patel, H. R., Berg, A. H., Pajvani, U. B., Scherer, P. E., & Ahima, R. S. (2004) · Nature Medicine · doi:10.1038/nm1029 · Cited by 809
Inflammatory mechanisms in the regulation of insulin resistance
Tilg, H., & Moschen, A. R. (2008) · Molecular Medicine · doi:10.2119/2007-00119.tilg · Cited by 779
Adiponectin – journey from an adipocyte secretory protein to biomarker of the metabolic syndrome
TRUJILLO, M. E., & Scherer, P. E. (2005) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2004.01426.x · Cited by 782
Ouchi, N., Kobayashi, H., Kihara, S., Kumada, M., Sato, K., Inoue, T., Funahashi, T., & Walsh, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310389200 · Cited by 759
A small-molecule AdipoR agonist for type 2 diabetes and short life in obesity
Okada-Iwabu, M., Yamauchi, T., Iwabu, M., Honma, T., Hamagami, K.-I., Matsuda, K., Yamaguchi, M., Tanabe, H., Kimura-Someya, T., Shirouzu, M., et al. (2013) · Nature · doi:10.1038/nature12656 · Cited by 757
Self-citationAdipokines: The missing link between insulin resistance and obesity
Antuna-Puente, B., Fève, B., Fellahi, S., & Bastard, J. (2008) · Diabetes & Metabolism · doi:10.1016/j.diabet.2007.09.004 · Cited by 760
Bråkenhielm, E., Veitonmäki, N., Cao, R., Kihara, S., Matsuzawa, Y., Zhivotovsky, B., Funahashi, T., & Cao, Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308671100 · Cited by 736
Insulin signaling in health and disease
White, M. F. (2003) · Science · doi:10.1126/science.1092952 · Cited by 733
Adipocytokines in Obesity and Metabolic Disease
Cao, H. (2014) · Journal of Endocrinology · doi:10.1530/joe-13-0339 · Cited by 705
Targeting adipose tissue in the treatment of obesity-associated diabetes
Kusminski, C. M., Bickel, P. E., & Scherer, P. E. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.75 · Cited by 678
Overproduction of large VLDL particles is driven by increased liver fat content in man
Adiels, M., Taskinen, M.-R., Packard, C., Caslake, M. J., Soro-Paavonen, A., Westerbacka, J., Vehkavaara, S., Häkkinen, A., Olofsson, S.-O., Yki-Järvinen, H., et al. (2006) · Diabetologia · doi:10.1007/s00125-005-0125-z · Cited by 690
The endocrine function of adipose tissues in health and cardiometabolic disease
Scheja, L., & Heeren, J. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-019-0230-6 · Cited by 663
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
Adiponectin promotes adipocyte differentiation, insulin sensitivity, and lipid accumulation
Fu, Y., Luo, N., Klein, R. L., & Garvey, W. T. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m400373-jlr200 · Cited by 666
Fuster, J. J., Ouchi, N., Gokce, N., & Walsh, K. X. (2016) · Circulation Research · doi:10.1161/circresaha.115.306885 · Cited by 691
“Early, it was reported that the beneficial actions of adiponectin on metabolic function and AMPK signaling pathway is mediated through combined signaling through its cell surface receptors adiponectin receptor (AdipoR) 1 and AdipoR2.”
Adipose Tissue Dysfunction in Obesity
Blüher, M. (2009) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-0029-1192044 · Cited by 679
APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function
Mao, X., Kikani, C. K., Riojas, R. A., Langlais, P. R., Wang, L., Ramos, F. J., Fang, Q., Christ-Roberts, C. Y., Hong, J., Kim, R. Y., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1404 · Cited by 671
Adiponectin: action, regulation and association to insulin sensitivity
Lihn, A. S., Pedersen, S. B., & Richelsen, B. (2005) · Obesity Reviews · doi:10.1111/j.1467-789x.2005.00159.x · Cited by 660
Selective Suppression of Endothelial Cell Apoptosis by the High Molecular Weight Form of Adiponectin
Kobayashi, H., Ouchi, N., Kihara, S., Walsh, K. X., Kumada, M., Abe, Y., Funahashi, T., & Matsuzawa, Y. (2004) · Circulation Research · doi:10.1161/01.res.0000119921.86460.37 · Cited by 666
Adiponectin: A Novel Adipokine Linking Adipocytes and Vascular Function
Goldstein, B. J., & Scalia, R. G. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0518 · Cited by 647
Adiponectin – a key adipokine in the metabolic syndrome
Whitehead, J. P., Richards, A. A., Hickman, I. J., Macdonald, G. A., & Prins, J. B. (2005) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2005.00510.x · Cited by 655
Felice, F. G. D., & Ferreira, S. T. (2014) · Diabetes · doi:10.2337/db13-1954 · Cited by 676
SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice
Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 648
The Role of Adiponectin in Cancer: A Review of Current Evidence
Dalamaga, Μ., Diakopoulos, K. N., & Mantzoros, C. S. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1015 · Cited by 653
Adipose Tissue as an Endocrine Organ
Ahima, R. S. (2006) · Obesity · doi:10.1038/oby.2006.317 · Cited by 646
Characterizing the profile of obese patients who are metabolically healthy
Primeau, V., Coderre, L., Karelis, A. D., Brochu, M., Lavoie, M.-È., Messier, V., SLADEK, R. M., & RABASA-LHORET, R. P. R. (2010) · International Journal of Obesity · doi:10.1038/ijo.2010.216 · Cited by 648
Role of leptin and adiponectin in insulin resistance
Yadav, A., Kataria, M. A., Saini, V., & Yadav, A. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.12.007 · Cited by 657
Adiponectin: mechanistic insights and clinical implications
Turer, A. T., & Scherer, P. E. (2012) · Diabetologia · doi:10.1007/s00125-012-2598-x · Cited by 650
Adiponectin regulation and function
Fang, H., & Judd, R. L. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170046 · Cited by 631
“In 2003, through a sequence of expression cloning experiments, AdipoR1 and AdipoR2 were first identified as receptors for adiponectin (381).”
InfluentialMetabolic Syndrome: A Clinical and Molecular Perspective
Moller, D. E., & Kaufman, K. D. (2004) · Annual Review of Medicine · doi:10.1146/annurev.med.56.082103.104751 · Cited by 636
Targeting Early Atherosclerosis: A Focus on Oxidative Stress and Inflammation
Marchio, P., Guerra‐Ojeda, S., Vila, J. M., Aldasoro, M., Víctor, V. M., & Mauricio, M. D. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8563845 · Cited by 651
“There are two receptors for adiponectin, AdipoR1 and AdipoR2, both with antiatherogenic activity [126] through modulation of AMPK and PPAR ligand activity [127].”
BackgroundAdipose Tissue-Derived Factors: Impact on Health and Disease
Trujillo, M. E., & Scherer, P. E. (2006) · Endocrine Reviews · doi:10.1210/er.2006-0033 · Cited by 624
Adiponectin regulates albuminuria and podocyte function in mice
Sharma, K., RamachandraRao, S., Qiu, G., Usui, H. K., Zhu, Y., Dunn, S., Ouedraogo, R., Hough, K., McCue, P. A., Chan, L., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32691 · Cited by 609
Adiponectin, the past two decades
Wang, Z. V., & Scherer, P. E. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw011 · Cited by 609
“Scatchard plot analysis and ligand binding assays revealed that AdipoR1 can act as a high-affinity receptor for globular adiponectin, but it can also bind full-length adiponectin, and AdipoR2 shows intermediate affinity for both globular and full-length adiponectin molecules (Yamauchi et al., 2003).”
BackgroundThe role of adipose tissue dysfunction in the pathogenesis of obesity-related insulin resistance
Goossens, G. H. (2008) · Physiology & Behavior · doi:10.1016/j.physbeh.2007.10.010 · Cited by 591
Valasek, M. A., & Repa, J. J. (2005) · AJP Advances in Physiology Education · doi:10.1152/advan.00019.2005 · Cited by 619
Adipokines: A link between obesity and cardiovascular disease
Nakamura, K., Fuster, J. J., & Walsh, K. X. (2013) · Journal of Cardiology · doi:10.1016/j.jjcc.2013.11.006 · Cited by 597
Recent insights into the pathogenesis of nonalcoholic fatty liver disease
Arab, J. P., Arrese, M., & Trauner, M. (2018) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020117-043617 · Cited by 573
Adipokines as novel biomarkers and regulators of the metabolic syndrome
Deng, Y., & Scherer, P. E. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05875.x · Cited by 578
Fleishman, J. S., & Kumar, S. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01811-6 · Cited by 615
Combs, T. P., Pajvani, U. B., Berg, A. H., Lin, Y., Jelicks, L. A., Laplante, M., Nawrocki, A. R., Rajala, M. W., Parlow, A. F., Cheeseboro, L., et al. (2004) · Endocrinology · doi:10.1210/en.2003-1068 · Cited by 545
Tsuchida, A., Yamauchi, T., Ito, Y., Hada, Y., Maki, T., Takekawa, S., Kamon, J., Kobayashi, M., Suzuki, R., Hara, K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402367200 · Cited by 550
Self-citationYoon, M. J., Lee, G. Y., Chung, J.-J., Ahn, Y. H., Hong, S. H., & Kim, J. B. (2006) · Diabetes · doi:10.2337/db05-1322 · Cited by 546
Regulation of adipocytokines and insulin resistance
Faßhauer, M., & Paschke, R. (2003) · Diabetologia · doi:10.1007/s00125-003-1228-z · Cited by 552
The metabolic syndrome and adipocytokines
Matsuzawa, Y. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.028 · Cited by 541
Insulin resistance and endothelial dysfunction: the road map to cardiovascular diseases
Cersósimo, E., & DeFronzo, R. A. (2006) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.634 · Cited by 531
Adipocytokines and Insulin Resistance
Pittas, A. G., Joseph, N. A., & Greenberg, A. S. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031005 · Cited by 513
Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing
Hopf, T. A., Colwell, L. J., Sheridan, R., Rost, B., Sander, C., & Marks, D. S. (2012) · Cell · doi:10.1016/j.cell.2012.04.012 · Cited by 509
Multifaceted Physiological Roles of Adiponectin in Inflammation and Diseases
Choi, H. M., Doss, H. M., & Kim, K. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041219 · Cited by 536
“In addition, the tissue expression profile of AdipoR1 nd R2 showed AdipoR1 was ubiquitously expressed in skel tal muscle and the liver, whil AdipoR2 was mainly expressed in the liver [13].”
BackgroundAdiponectin and its receptors are expressed in bone-forming cells
Berner, H. S., Lyngstadaas, S. P., Spahr, A., Monjo, M., Thommesen, L., Drevon, C. A., Syversen, U., & Reseland, J. E. (2004) · Bone · doi:10.1016/j.bone.2004.06.008 · Cited by 507
Adiponectin and cancer: a systematic review
Kelesidis, I., Kelesidis, T., & Mantzoros, C. S. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6603051 · Cited by 495
Enhanced carbon tetrachloride-induced liver fibrosis in mice lacking adiponectin
Kamada, Y., Tamura, S., Kiso, S., Matsumoto, H., Saji, Y., Yoshida, Y., Fukui, K., Maeda, N., Nishizawa, H., Nagaretani, H., et al. (2003) · Gastroenterology · doi:10.1053/j.gastro.2003.08.029 · Cited by 479
Adiponectin Multimeric Complexes and the Metabolic Syndrome Trait Cluster
Lara‐Castro, C., Luo, N., Wallace, P., Klein, R. L., & Garvey, W. T. (2006) · Diabetes · doi:10.2337/diabetes.55.01.06.db05-1105 · Cited by 480
Leptin and Cardiovascular Disease
Koh, K. K., Park, S. M., & Quon, M. J. (2008) · Circulation · doi:10.1161/circulationaha.107.741645 · Cited by 481
Role of Disulfide Bonds in Acrp30/Adiponectin Structure and Signaling Specificity
Tsao, T., Tomás, E., Murrey, H. E., Hug, C., Lee, D. H., Ruderman, N. B., Heuser, J. E., & Lodish, H. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309469200 · Cited by 479
Mitochondrial dysfunction in obesity
Bournat, J. C., & Brown, C. (2010) · Current Opinion in Endocrinology Diabetes and Obesity · doi:10.1097/med.0b013e32833c3026 · Cited by 488
Koerner, A., Kratzsch, J., & Kiess, W. (2005) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2005.07.008 · Cited by 471
Kawanami, D., Maemura, K., Takeda, N., Harada, T., Nojiri, T., Imai, Y., Manabe, I., Utsunomiya, K., & Nagai, R. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.104 · Cited by 470
Yanai, H., & Yoshida, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051190 · Cited by 485
“Adiponectin receptors include two similar transmembrane receptors which are known as AdipoR1 and AdipoR2, and another type of receptor without a transmembrane domain which may act as a co-receptor for the high-molecular weight (HMW) form of adiponectin on endothelial and smooth muscle cells [6,7].”
BackgroundWhite Adipose Tissue as Endocrine Organ and Its Role in Obesity
Frigolet, M. E., Torres, N., & Tovar, A. R. (2008) · Archives of Medical Research · doi:10.1016/j.arcmed.2008.09.005 · Cited by 475
Obesity and asthma: Possible mechanisms
Shore, S. A. (2008) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2008.03.004 · Cited by 459
Global view of the evolution and diversity of metazoan neuropeptide signaling
Jékely, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221833110 · Cited by 451
Adipose tissue angiogenesis as a therapeutic target for obesity and metabolic diseases
Cao, Y. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3055 · Cited by 453
Molecular links between obesity and breast cancer
Lorincz, A., & Sukumar, S. V. (2006) · Endocrine Related Cancer · doi:10.1677/erc.1.00729 · Cited by 447
C1q and tumor necrosis factor superfamily: modularity and versatility
Kishore, U., Gaboriaud, C., Waters, P. J., Shrive, A. K., Greenhough, T. J., Reid, K. B. M., Sim, R. B., & Arlaud, G. J. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.08.006 · Cited by 437
Stiles, B., Wang, Y., Stahl, A., Bassilian, S., Lee, W. P., Kim, Y.-J., Sherwin, R., Devaskar, S., Lesche, R., Magnuson, M. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308617100 · Cited by 436
Therapy Insight: adipocytokines in metabolic syndrome and related cardiovascular disease
Matsuzawa, Y. (2006) · Nature Clinical Practice Cardiovascular Medicine · doi:10.1038/ncpcardio0380 · Cited by 434
Gustafson, B., Hammarstedt, A., Andersson, C. X., & Smith, U. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.147835 · Cited by 447
Adiponectin: a key adipocytokine in metabolic syndrome
Okamoto, Y., Kihara, S., Funahashi, T., Matsuzawa, Y., & Libby, P. (2006) · Clinical Science · doi:10.1042/cs20050182 · Cited by 445
Metadata
- Authors
- Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., Murakami, K., Ohteki, T., Uchida, S., Takekawa, S., Waki, H., Tsuno, N. H., Shibata, Y., Terauchi, Y., Froguel, P., Tobe, K., Koyasu, S., Taira, K., Kitamura, T., Shimizu, T., Nagai, R., & Kadowaki, T.
- Affiliations
- The University of Tokyo (JP)
- Nissan Chemical Corporation (Japan) (JP)
- Japan Science and Technology Agency (JP)
- National Institute of Advanced Industrial Science and Technology (JP)
- Keio University (JP)
- Centre National de la Recherche Scientifique (FR)
- Institute of Medical Science, The University of Tokyo (JP)
- Corresponding author
- Kadowaki, Takashi
- ORCID
- Venue
- Nature
- Published
- 2003-06-12
- Volume
- 423
- Issue
- 6941
- Pages
- 762-769
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1997978122
- Cited by
- 3,176
- References
- 28
- Citations by year
- 2026: 43 · 2025: 50 · 2024: 77 · 2023: 102 · 2022: 89 · 2021: 136 · 2020: 114 · 2019: 120 · 2018: 114 · 2017: 117 · 2016: 117 · 2015: 154 · 2014: 173 · 2013: 190 · 2012: 170
- FWCI
- 115.85
- Type
- journal article
- Language
- en
- Update notices
- erratum (2004-10-28)
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Novartis Foundation
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- adiponectin, adiponectin receptors, AdipoR1, AdipoR2, insulin resistance, type 2 diabetes, AMP kinase, PPARα, fatty acid oxidation, glucose uptake, skeletal muscle, liver, adipokines, obesity, receptor cloning
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Cloning, Molecular, Diabetes Mellitus, Endothelium, Vascular, Fatty Acids, Glucose, Humans, Hypoglycemic Agents, Ligands, Molecular Sequence Data, Oxidation-Reduction, Proteins, Receptors, Cell Surface, Transcription Factors, Receptors, Cytoplasmic and Nuclear, Hepatocytes, Muscle Cells, RNA Interference, RNA, Small Interfering, Intercellular Signaling Peptides and Proteins, Mice, Adiponectin, Receptors, Adiponectin
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