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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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Sorted by citations
Items 201–300 of 1,021
Changes of Adiponectin Oligomer Composition by Moderate Weight Reduction
Bobbert, T., Rochlitz, H., Wegewitz, U. E., Akpulat, S., Mai, K., Weickert, M. O., Möhlig, M., Pfeiffer, A. F. H., & Spranger, J. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2712 · Cited by 273
Expression of adiponectin receptors in pancreatic β cells
Kharroubi, I., Rasschaert, J., Eizirik, D. L., & Cnop, M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.042 · Cited by 278
Chinetti, G., Zawadski, C., Fruchart, J., & Staels, B. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.058 · Cited by 267
Pathogenesis and management issues for non-alcoholic fatty liver disease
Duvnjak, M. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i34.4539 · Cited by 266
Housa, D., Housova, J., Vernerová, Z., & Haluzı́k, M. (2006) · Physiological Research · doi:10.33549/physiolres.930848 · Cited by 265
Fat as an Endocrine Organ: Relationship to the Metabolic Syndrome
Hutley, L. J., & Prins, J. B. (2005) · The American Journal of the Medical Sciences · doi:10.1097/00000441-200512000-00005 · Cited by 265
You, M., Considine, R. V., Leone, T. C., Kelly, D. P., & Crabb, D. W. (2005) · Hepatology · doi:10.1002/hep.20821 · Cited by 259
Civitarese, A. E., Jenkinson, C. P., Richardson, D. K., Bajaj, M., Cusi, K. J., Kashyap, S. R., Berria, R., Belfort, R., DeFronzo, R. A., Mandarino, L. J., et al. (2004) · Diabetologia · doi:10.1007/s00125-004-1359-x · Cited by 263
Adiponectin inhibits Toll‐like receptor family‐induced signaling
Yamaguchi, N., Argueta, J. G. M., Masuhiro, Y., Kagishita, M., Nonaka, K., Saito, T., Hanazawa, S., & Yamashita, Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.019 · Cited by 259
The adipocyte as an active participant in energy balance and metabolism
Badman, M. K., & Flier, J. S. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.058 · Cited by 256
Cardioprotection by Adiponectin
Ouchi, N., Shibata, R., & Walsh, K. X. (2006) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2006.03.001 · Cited by 260
Adipokines: implications for female fertility and obesity
Mitchell, M., Armstrong, D. T., Robker, R. L., & Norman, R. J. (2005) · Reproduction · doi:10.1530/rep.1.00521 · Cited by 262
Molecular Mechanism for Adiponectin-dependent M2 Macrophage Polarization
Mandal, P., Pratt, B. T., Barnes, M. A., McMullen, M. R., & Nagy, L. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204644 · Cited by 260
Plasma adiponectin is decreased in nonalcoholic fatty liver disease
Pagano, C., Soardo, G., Esposito, W., Fallo, F., Basan, L., Donnini, D., Federspil, G., Sechi, L. A., & Vettor, R. (2005) · European Journal of Endocrinology · doi:10.1530/eje.1.01821 · Cited by 266
Circulating Adiponectin and Endometrial Cancer Risk
Maso, L. D., Augustin, L. S. A., Karalis, A., Talamini, R., Franceschi, S., Trichopoulos, D., Mantzoros, C. S., & Vecchia, C. L. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031716 · Cited by 256
Exercise training is not associated with improved levels of C-reactive protein or adiponectin
MARCELL, T. J., McAuley, K. A., Traustadóttir, T., & Reaven, P. D. (2005) · Metabolism · doi:10.1016/j.metabol.2004.11.008 · Cited by 259
Baratta, R., Amato, S., Degano, C., Farina, M. G., Patanè, G., Vigneri, R., & Frittitta, L. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031777 · Cited by 249
Plasma Adiponectin and Gastric Cancer
Ishikawa, M., Kitayama, J., Kazama, S., Hiramatsu, T., Hatano, K., & Nagawa, H. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.466.11.2 · Cited by 253
Tilg, H., & Moschen, A. R. (2008) · Clinical Science · doi:10.1042/cs20070196 · Cited by 252
AMPK Mediates the Initiation of Kidney Disease Induced by a High-Fat Diet
Declèves, A., Mathew, A. V., Cunard, R. A., & Sharma, K. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2011010026 · Cited by 251
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
Metabolic function of the CTRP family of hormones
Seldin, M. M., Tan, S. Y., & Wong, G. W. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9255-7 · Cited by 249
Adiponectin, Cardiovascular Function, and Hypertension
Wang, Z. V., & Scherer, P. E. (2008) · Hypertension · doi:10.1161/hypertensionaha.107.099424 · Cited by 247
Shklyaev, S., Aslanidi, G., Tennant, M., Prima, V., Kohlbrenner, E., Kroutov, V., Campbell‐Thompson, M., Crawford, J. M., Shek, E. W., Scarpace, P. J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2333912100 · Cited by 249
Adiponectin: a versatile player of innate immunity
Luo, Y., & Liu, M. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw012 · Cited by 253
“AdipoR1, AdipoR2, and T-cadherin are present in monocytes/ macrophages with high abundance of AdipoR1 (Chinetti et al., 2004; Yamaguchi et al., 2005; Hui et al., 2015); however, whether these receptors play important roles in mediating antiinflammatory action of adiponectin in macrophages remains controversial.”
BackgroundInfluentialAdipocyte-Derived Hormones, Cytokines, and Mediators
Rondinone, C. M. (2006) · Endocrine · doi:10.1385/endo:29:1:81 · Cited by 252
Discrimination Between Obesity and Insulin Resistance in the Relationship With Adiponectin
Abbasi, F., Chu, J. W., Lamendola, C. A., McLaughlin, T., Hayden, J. M., Reaven, G. M., & Reaven, P. D. (2004) · Diabetes · doi:10.2337/diabetes.53.3.585 · Cited by 246
Molecular Pathways: Adiponectin and Leptin Signaling in Cancer
VanSaun, M. N. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0930 · Cited by 253
The Anti-Inflammatory Effects of Testosterone
Bianchi, V. E. (2018) · Journal of the Endocrine Society · doi:10.1210/js.2018-00186 · Cited by 261
“Adiponectin, the highest expressed cytokine in adipocytes [89], is inversely correlated with metabolic disorders and, CVD [90], with waist-to-hip ratio, and visceral fat [91, 92].”
Adiponectin, a key adipokine in obesity related liver diseases.
Buechler, C., Wanninger, J., & Neumeier, M. (2011) · PubMed · doi:10.3748/wjg.v17.i23.2801 · Cited by 264
Kubota, N., Kubota, T., Itoh, S., Kumagai, H., Kozono, H., Takamoto, I., Mineyama, T., Ogata, H., Tokuyama, K., Ohsugi, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.05.007 · Cited by 244
Self-citationAdiponectin and atherosclerotic disease
Shimada, K., Miyazaki, T., & Daida, H. (2004) · Clinica Chimica Acta · doi:10.1016/j.cccn.2004.02.020 · Cited by 244
Adipose tissue as an immunological organ: Toll-like receptors, C1q/TNFs and CTRPs
Schäffler, A., Schölmerich, J., & Salzberger, B. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.07.003 · Cited by 243
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
Induction of Adiponectin in Skeletal Muscle by Inflammatory Cytokines: in Vivo and in Vitro Studies
Delaigle, A. M., Jonas, J.-C., Bauche, I. B., Cornu, O., & Brichard, S. M. (2004) · Endocrinology · doi:10.1210/en.2004-0503 · Cited by 241
Expression and Regulation of Adiponectin and Receptor in Human and Rat Placenta
Caminos, J. E., Nogueiras, R., Gallego, R., Bravo, S. B., Tovar, S. A., García‐Caballero, T., Casanueva, F. F., & Diéguez, C. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0930 · Cited by 242
Schäffler, A., Schölmerich, J., & Büchler, C. (2005) · Nature Clinical Practice Gastroenterology & Hepatology · doi:10.1038/ncpgasthep0186 · Cited by 240
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
Adipokines and Non-Alcoholic Fatty Liver Disease: Multiple Interactions
Adolph, T. E., Grander, C., Grabherr, F., & Tilg, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081649 · Cited by 252
“Adiponectin exerts many of its functions via two distinct receptors (ADIPOR1 and ADIPOR2), both seven-transmembrane domain proteins with an internal N-terminus part and an extracellular C-terminus part [21,22].”
BackgroundAdiponectin Regulates Bone Mass via Opposite Central and Peripheral Mechanisms through FoxO1
Kajimura, D., Lee, H. W., Riley, K. J., Arteaga‐Solis, E., Ferron, M., Zhou, B., Clarke, C. J., Hannun, Y. A., DePinho, R. A., Guo, X.-D. E., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.009 · Cited by 244
Swarbrick, M. M., & Havel, P. J. (2008) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2007.0029 · Cited by 244
Adiposity and Cardiovascular Disorders
Katagiri, H., Yamada, T., & Oka, Y. (2007) · Circulation Research · doi:10.1161/circresaha.107.151621 · Cited by 241
Hong, J., Jia, Y., Pan, S., Jia, L., Li, H., Han, Z., Cai, D., & Zhao, R. (2016) · Oncotarget · doi:10.18632/oncotarget.11267 · Cited by 244
“The down-stream signaling of adiponectin receptors involves activation of 5′-adenosine monophosphate-activated protein kinase (AMPK) [26] and peroxisome proliferator-activated receptor-α (PPARα) [27], which subsequently induces mitochondria biogenesis and enhances fatty acid oxidation [28].”
BackgroundNagasawa, T., Inada, Y., Nakano, S., Tamura, T., Takahashi, T., Maruyama, K., Yamazaki, Y., Kuroda, J., & Shibata, N. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.02.028 · Cited by 233
Higuchi, K., Masaki, T., Gotoh, K., Chiba, S., Katsuragi, I., Tanaka, K., Kakuma, T., & Yoshimatsu, H. (2007) · Endocrinology · doi:10.1210/en.2006-1270 · Cited by 241
Role of adiponectin in human skeletal muscle bioenergetics
Civitarese, A. E., Ukropcova, B., Carling, S., Hulver, M., DeFronzo, R. A., Mandarino, L., Ravussin, E., & Smith, S. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.002 · Cited by 234
Kos, K., Harte, A. L., da Silva, N. F., Tonchev, A. B., Chaldakov, G., James, S. G., Snead, D. R. J., Hoggart, B., O’Hare, J. P., McTernan, P. G., et al. (2007) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2006-1841 · Cited by 237
Wijesekara, N., Krishnamurthy, M., Bhattacharjee, A., Suhail, A., Sweeney, G., & Wheeler, M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.085084 · Cited by 229
Regulation of lipid accumulation by AMK-activated kinase in high fat diet–induced kidney injury
Declèves, A., Zolkipli‐Cunningham, Z., Satriano, J. A., Wang, L., Nakayama, T., Rogač, M., Le, T. P., Nortier, J., Farquhar, M. G., Naviaux, R. K., et al. (2013) · Kidney International · doi:10.1038/ki.2013.462 · Cited by 233
Otake, S., Takeda, H., Suzuki, Y., Fukui, T., Watanabe, S., Ishihama, K., Saito, T., Togashi, H., Nakamura, T., Matsuzawa, Y., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1868 · Cited by 229
Côté, M., Mauriège, P., Bergeron, J., Alméras, N., Tremblay, A., Lemieux, I., & Després, J.-P. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1711 · Cited by 230
Regulation of Pituitary Cell Function by Adiponectin
Rodríguez‐Pacheco, F., Martínez‐Fuentes, A. J., Tovar, S. A., Pinilla, L., Tena‐Sempere, M., Diéguez, C., Castano, J. P., & Malagón, M. M. (2006) · Endocrinology · doi:10.1210/en.2006-1019 · Cited by 231
The Role of the Carnitine System in Human Metabolism
Foster, D. W. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1320.001 · Cited by 231
Adiponectin: Identification, physiology and clinical relevance in metabolic and vascular disease
Matsuzawa, Y. (2005) · Atherosclerosis Supplements · doi:10.1016/j.atherosclerosissup.2005.02.003 · Cited by 233
The Roles of Leptin and Adiponectin
Ding, X., Saxena, N. K., Lin, S., Xu, A., Srinivasan, S., & Anania, F. A. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62476-5 · Cited by 225
You, M., & Crabb, D. W. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00056.2004 · Cited by 223
Hepatic steatosis, low-grade chronic inflammation and hormone/growth factor/adipokine imbalance
Tarantino, G. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i38.4773 · Cited by 229
Adiponectin complexes in human cerebrospinal fluid: distinct complex distribution from serum
Kusminski, C. M., McTernan, P. G., Schraw, T., Kos, K., O’Hare, J. P., Ahima, R. S., Kumar, S., & Scherer, P. E. (2007) · Diabetologia · doi:10.1007/s00125-006-0577-9 · Cited by 225
Increased serum adiponectin levels in type 1 diabetic patients with microvascular complications
Frystyk, J., Tarnow, L., Hansen, T. K., Parving, H.-H., & Flyvbjerg, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1850-z · Cited by 223
Hoffstedt, J., Nordström, E. A., Sjölin, E., Wåhlén, K., & Arner, P. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031458 · Cited by 220
Adiponectin primes human monocytes into alternative anti-inflammatory M2 macrophages
Lovren, F., Pan, Y., Quan, A., Szmitko, P. E., Singh, K. K., Shukla, P. C., Gupta, M., Chan, L., Al-Omran, M. A., Teoh, H., et al. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00115.2010 · Cited by 220
Adiponectin: from obesity to cardiovascular disease
Antoniades, C. A., Antonopoulos, A. S., Tousoulis, D., & Stefanadis, C. (2009) · Obesity Reviews · doi:10.1111/j.1467-789x.2009.00571.x · Cited by 222
PPARγ-mediated insulin sensitization: the importance of fat versus muscle
Kintscher, U., & Law, R. E. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00440.2004 · Cited by 222
Spranger, J., Verma, S., Göhring, I., Bobbert, T., Seifert, J., Sindler, A. L., Pfeiffer, A. F. H., Hileman, S. M., Tschöp, M. H., & Banks, W. A. (2006) · Diabetes · doi:10.2337/diabetes.55.01.06.db05-1077 · Cited by 220
Role of AMP‐activated protein kinase in the metabolic syndrome and in heart disease
Hardie, D. G. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.018 · Cited by 221
Cytokines and the pathogenesis of non-alcoholic steatohepatitis
Diehl, A. M., Li, Z. P., Lin, H., & Yang, S. (2005) · Gut · doi:10.1136/gut.2003.024935 · Cited by 217
Narasimhan, M. L., Coca, M. A., Jin, J., Yamauchi, T., Ito, Y., Kadowaki, T., Kim, K. K., Pardo, J. M., Damsz, B., Hasegawa, P. M., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.050 · Cited by 216
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
Crystal structures of the human adiponectin receptors
Tanabe, H., Fujii, Y., Okada‐Iwabu, M., Iwabu, M., Nakamura, Y., Hosaka, T., Motoyama, K., Ikeda, M., Wakiyama, M., Terada, T., et al. (2015) · Nature · doi:10.1038/nature14301 · Cited by 220
Wei, G., Lu, K., Umar, M., Zhu, Z., Lu, W. W., Speakman, J. R., Chen, Y., Tong, L., & Chen, D. (2023) · Bone Research · doi:10.1038/s41413-023-00301-9 · Cited by 248
“Adiponectin exerts its biological effects through AdipoR1 and AdipoR2 receptors, which are expressed in various tissues, including the liver, articular cartilage, bone and synovium 179 – 181 .”
BackgroundAdiponectin and Cardiovascular Disease
Shibata, R., Ouchi, N., & Murohara, T. (2009) · Circulation Journal · doi:10.1253/circj.cj-09-0057 · Cited by 214
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
Structural insights into adiponectin receptors suggest ceramidase activity
Vasiliauskaité-Brooks, I., Sounier, R., Rochaix, P., Bellot, G., Fortier, M., Hoh, F., Colibus, L. D., Bechara, C., Saied, E. M., Arenz, C., et al. (2017) · Nature · doi:10.1038/nature21714 · Cited by 216
Zhou, L., Deepa, S. S., Etzler, J. C., Ryu, J., Mao, X., Fang, Q., Liu, D. D., Torres, J. M., Jia, W., Lechleiter, J. D., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028357 · Cited by 212
Tsuda, T., Ueno, Y., Aoki, H., Koda, T., Horio, F., Takahashi, N., Kawada, T., & Osawa, T. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.031 · Cited by 213
Wang, C., Mao, X., Wang, L., Liu, M., Wetzel, M. D., Guan, K.-L., Dong, L. Q., & Liu, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700098200 · Cited by 210
Metabolic adaptation in obesity and type ii diabetes: myokines, adipokines and hepatokines
Oh, K.-J., Lee, D., Kim, W., Han, B., Lee, S., & Bae, K.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010008 · Cited by 210
“Adiponectin exerts beneficial effects through the activation of its two receptors, adiponectin receptor 1 (AdipoR1) and adiponectin receptor 2 (AdipoR2) [165,166].”
BackgroundChen, J., Tan, B., Karteris, E., Zervou, S., Digby, J., Hillhouse, E. W., Vatish, M., & Randeva, H. S. (2006) · Diabetologia · doi:10.1007/s00125-006-0194-7 · Cited by 272
Adipokines, diabetes and atherosclerosis: an inflammatory association
Freitas‐Lima, L. C., Braga, V. A., de França-Silva, M. D. S., Cruz, J. C., Santos, S. H. S., Monteiro, M. M. D. O., & Balarini, C. M. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00304 · Cited by 218
“Adiponectin interacts with two different transmembrane receptors: AdipoR1 (expressed ubiquitously and at a high level in skeletal muscle) and AdipoR2 (expressed predominantly in the liver) (Yamauchi et al., 2003a; Scheid and Sweeney, 2014).”
BackgroundHeterotrimeric G Protein–Coupled Signaling in Plants
Urano, D., & Jones, A. M. (2013) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050213-040133 · Cited by 230
Parimisetty, A., Dorsemans, A.-C., Awada, R., Ravanan, P., Diotel, N., & Lefebvre d’Hellencourt, C. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0530-x · Cited by 188
“Their expression was documented in different brain structures such as the pituitary, the hypothalamus, and in cortical and subcortical neurons [97, 119, 121, 127–131].”
BackgroundAdipose tissue: an endocrine organ playing a role in metabolic regulation
Booth, A. D., Magnuson, A. M., Fouts, J. K., & Foster, M. T. (2016) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2015-0073 · Cited by 220
“AdipoR1 is found primarily on the outer membrane of skeletal muscle myocytes whereas AdipoR2 resides mostly on the outer membrane of hepatocytes within the liver [39].”
Globular adiponectin upregulates nitric oxide production in vascular endothelial cells
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Evidence for a protective role for adiponectin in osteoarthritis
Chen, T.-H., Chen, L., Hsieh, M., Chang, C., Chou, D., & Tsai, S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.008 · Cited by 210
Reed, B. D., Charos, A. E., Szekely, A. M., Weissman, S. M., & Snyder, M. P. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000133 · Cited by 214
Youn, B., Yu, K.-Y., Park, H. J., Lee, N. S., Min, S.-S., Youn, M. Y., Cho, Y. M., Park, Y. J., Kim, S. Y., Lee, H. K., et al. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031121 · Cited by 206
Sozio, M. S., & Crabb, D. W. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00011.2008 · Cited by 207
Immunological functions of leptin and adiponectin
Carbone, F., Rocca, C. L., & Matarese, G. (2012) · Biochimie · doi:10.1016/j.biochi.2012.05.018 · Cited by 213
The Role of Adiponectin in Obesity, Diabetes, and Cardiovascular Disease
Kawano, J., & Arora, R. R. (2009) · Journal of the CardioMetabolic Syndrome · doi:10.1111/j.1559-4572.2008.00030.x · Cited by 213
Taurine is Involved in Energy Metabolism in Muscles, Adipose Tissue, and the Liver
Wen, C., Li, F., Zhang, L., Duan, Y., Guo, Q., Wang, W., He, S., Li, J., & Yin, Y. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201800536 · Cited by 219
Differential Role of Leptin and Adiponectin in Cardiovascular System
Ghantous, C. M., Azrak, Z., Hanache, S., Abou-Kheir, W. G., & Zeidan, A. (2015) · International Journal of Endocrinology · doi:10.1155/2015/534320 · Cited by 211
Zheng, Q., Yuan, Y., Yi, W., Lau, W. B., Wang, Y., Wang, X., Sun, Y., Lopez, B. L., Christopher, T. A., Peterson, J. M., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.231050 · Cited by 202
Gender Differences in Cardiovascular Disease: Hormonal and Biochemical Influences
Pérez-López, F. R., Larrad-Mur, L., Kallen, A. N., Chedraui, P. A., & Taylor, H. S. (2010) · Reproductive Sciences · doi:10.1177/1933719110367829 · Cited by 204
Adiponectin Acts as an Endogenous Antithrombotic Factor
Kato, H., Kashiwagi, H., Shiraga, M., Tadokoro, S., Kamae, T., Ujiie, H., Honda, S., Miyata, S., Ijiri, Y., Yamamoto, J., et al. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000194076.84568.81 · Cited by 202
The Identification of Ligands at Orphan G-Protein Coupled Receptors
Wise, A., Jupe, S., & Rees, S. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121419 · Cited by 207
Ohashi, K., Iwatani, H., Kihara, S., Nakagawa, Y., Komura, N., Fujita, K., Maeda, N., Nishida, M., Katsube, F., Shimomura, I., et al. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.147645 · Cited by 201
Adipokines: masterminds of metabolic inflammation
Tilg, H., Ianiro, G., Gasbarrini, A., & Adolph, T. E. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01103-8 · Cited by 234
“Most effects of adiponectin are mediated via the seven-transmembrane domain adiponectin receptor type 1 (ADIPOR1), which is predominantly expressed in skeletal muscle, and ADIPOR2, which is mainly expressed in the liver 34 .”
Chen, M. B., McAinch, A. J., Macaulay, S. L., Castelli, L. A., O’Brien, P. E., Dixon, J. B., Cameron‐Smith, D., Kemp, B. E., & Steinberg, G. R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1980 · Cited by 201
Guerre-Millo, M. (2008) · Diabetes & Metabolism · doi:10.1016/j.diabet.2007.08.002 · Cited by 203
Fat Deposition and Fat Effects on Meat Quality—A Review
Schumacher, M. L., DelCurto-Wyffels, H. M., Thomson, J. M., & Boles, J. A. (2022) · Animals · doi:10.3390/ani12121550 · Cited by 220
“Adiponectin and the associated receptors increase AMPK and peroxisome proliferatoractivated receptor α (PPARα) activity [128].”
Background
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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