The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Adiponectin Stimulates Angiogenesis by Promoting Cross-talk between AMP-activated Protein Kinase and Akt Signaling in Endothelial Cells
Open accessAbstract
Adiponectin is an adipocyte-specific adipocytokine with anti-atherogenic and anti-diabetic properties. Here, we investigated whether adiponectin regulates angiogenic processes in vitro and in vivo. Adiponectin stimulated the differentiation of human umbilical vein endothelium cells (HUVECs) into capillary-like structures in vitro and functioned as a chemoattractant in migration assays. Adiponectin promoted the phosphorylation of AMP-activated protein kinase (AMPK), protein kinase Akt/protein kinase B, and endothelial nitric oxide synthesis (eNOS) in HUVECs. Transduction with either dominant-negative AMPK or dominant-negative Akt abolished adiponectin-induced eNOS phosphorylation as well as adiponectin-stimulated HUVEC migration and differentiation. Dominant-negative AMPK also inhibited adiponectin-induced Akt phosphorylation, suggesting that AMPK is upstream of Akt. Dominant-negative Akt or the phosphatidylinositol 3-kinase inhibitor LY294002 blocked adiponectin-stimulated Akt and eNOS phosphorylation, migration, and differentiation without altering AMPK phosphorylation. Finally, adiponectin stimulated blood vessel growth in vivo in mouse Matrigel plug implantation and rabbit corneal models of angiogenesis. These data indicate that adiponectin can function to stimulate the new blood vessel growth by promoting cross-talk between AMP-activated protein kinase and Akt signaling within endothelial cells.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“Further evidence also shows that AMPK lies upstream of the phosphatidylinositol-3-kinase-protein kinase B pathway, which also leads to eNOS activation and NO production [162,164,165].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [164]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Positional cloning of the mouse obese gene and its human homologue
Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419
Adipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance
Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518
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
Angiogenesis in health and disease
Carmeliet, P. (2003) · Nature Medicine · doi:10.1038/nm0603-653 · Cited by 4,379
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
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
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
Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D. J., Gratton, J., McCabe, T. J. D., Fontana, J. T., Fujio, Y., Walsh, K. X., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,616
Research works printed but not linked: 1
- Phillips, 1994, In Vivo (Athens)., 8, 961
Cited by
Sorted by citations
Items 401–500 of 757
Zhao, X., Balaji, P., Pachon, R. E., Beniamen, D., Vatner, D. E., Graham, R. M., & Vatner, S. F. (2015) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.115.305919 · Cited by 32
The Therapeutic Potential of the Adiponectin Pathway
Gu, W., & Li, Y. (2011) · BioDrugs · doi:10.2165/11594790-000000000-00000 · Cited by 32
Lee, S.-Y., Ku, H.-C., Kuo, Y., Chiu, H.-L., & Su, M. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0125-3 · Cited by 32
“Synergistic activation of AMPK and AKT has been shown to regulate glucose metabolism [37], implying the existence of cross-talk between AMPK and AKT as we found here.”
BackgroundQu, K., Cha, H., Ru, Y., Que, H., & Xing, M. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.113824 · Cited by 32
O’Shea, K. M., Chess, D. J., Khairallah, R. J., Rastogi, S., Hecker, P. A., Sabbah, H. N., Walsh, K. X., & Stanley, W. C. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00957.2009 · Cited by 31
“promotes capillary formation (27), this could explain the dif-”
BackgroundThe Vascular Adventitia: Its Role in the Arterial Injury Response
Havelka, G. E., & Kibbe, M. R. (2011) · Vascular and Endovascular Surgery · doi:10.1177/1538574411407698 · Cited by 31
“endothelial cell proliferation and inhibits endothelial cell apoptosis (ie, programmed cell death), both important in attenuating the progression of arterial disease.(29,30) Repair of damaged endothelium involves the recruitment and differentiation of circulating endothelial progenitor cells (EPCs).”
BackgroundHeart Failure With Preserved Ejection Fraction and Adipose Tissue: A Story of Two Tales
Oh, A., Okazaki, R. A., Sam, F., & Valero‐Muñoz, M. (2019) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00110 · Cited by 32
Mechanisms underlying the effects of caloric restriction on hypertension
Attar, A. A., Fahed, G., Hoballah, M. M., Pedersen, S., EL‐Yazbi, A. F., Nasser, S. A., Bitto, A., Orekhov, A. N., & Eid, A. H. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115035 · Cited by 32
“In contrast, other studies confirm the involvement of an adiponectin-AMPK- PI3k- Akt-eNOS axis, since dominant negative AMPK suppresses the activating Akt phosphorylation at Ser 473 in endothelial cells [69,70].”
Urs, S., Turner, B., Tang, Y., Rostama, B., Small, D. J., & Liaw, L. (2012) · Adipocyte · doi:10.4161/adip.19186 · Cited by 31
Matsuo, Y., Imanishi, T., Kuroi, A., Kitabata, H., Kubo, T., Hayashi, Y., Tomobuchi, Y., & Akasaka, T. (2007) · Circulation Journal · doi:10.1253/circj.71.1376 · Cited by 31
Tian, J., Liu, Y., Liu, Y., Chen, K., & Lyu, S. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9080869 · Cited by 32
“[69] showed that adiponectin-induced Akt phosphorylation, eNOS phosphorylation, and cell migration and differentiation in HUVECs were abolished when the cells were transduced with a dominant-negative form of AMP-activated protein kinase (AMPK).”
BackgroundMultifaced roles of adipokines in endothelial cell function
Yan, Y., Wang, L., Zhong, N., Wen, D., & Liu, L. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1490143 · Cited by 30
The Role of Adiponectin and ADIPOQ Variation in Metabolic Syndrome: A Narrative Review
Błażejewska, W., Dąbrowska, J., Michałowska, J., & Bogdański, P. (2025) · Genes · doi:10.3390/genes16060699 · Cited by 33
Essential Role of Bone Marrow for Microvascular Endothelial and Metabolic Functions in Mice
Nakajima, S., Ohashi, J., Sawada, A., Noda, K., Fukumoto, Y., & Shimokawa, H. (2012) · Circulation Research · doi:10.1161/circresaha.112.270215 · Cited by 30
Adiponectin modulates the function of endothelial progenitor cells via AMPK/eNOS signaling pathway
Wang, S., Miao, J., Qu, M., Yang, G., & Shen, L. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.09.073 · Cited by 30
Lindgren, A., Levin, M. C., Blomqvist, S. R., Wikström, J., Ahnmark, A., Mogensen, C., Böttcher, G., Bohlooly‐Y, M., Borén, J., Gan, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080330 · Cited by 30
“Interestingly, adiponectin has been shown to stimulate angiogenesis both in vitro and in vivo [30,31], and it would be of interest for future studies to explore the contribution of the two adiponectin receptors in this process.”
BackgroundYang, C.-C., Chang, S., Chao, J., Lai, Y., Chang, W.-E., Hsu, W., & Kuo, W. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-112 · Cited by 30
“AMPK is known to be an energy sensor that controls the cellular metabolisms in normal cells [34-38].”
BackgroundWang, Y., Li, Y., Qiao, J., Li, N., & Qiao, S. (2019) · Cell Biochemistry and Function · doi:10.1002/cbf.3440 · Cited by 30
“Adiponectin‐ induced Akt phosphorylation is one of the downstream effectors of AMPK activation.(40) Actually, previous studies have described that adiponectin elevated insulin‐induced Akt phosphorylation.”
BackgroundHypoadiponectinemia is Associated With Coronary Artery Spasm in Men
Maruyoshi, H., Kojima, S., Otsuka, F., Funahashi, T., Kaikita, K., Sugiyama, S., Sakamoto, T., Yoshimura, M., Shimomura, I., & Ogawa, H. (2005) · Circulation Journal · doi:10.1253/circj.69.1154 · Cited by 29
Association between High Molecular Weight Adiponectin Levels and Metabolic Parameters
Fujimatsu, D., Kotooka, N., Inoue, T., Nishiyama, M., & Node, K. (2009) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.1073 · Cited by 28
Vascular endothelial adiponectin signaling across the life span
Cohen, K. E., Katunaric, B., SenthilKumar, G., McIntosh, J. J., & Freed, J. K. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00533.2021 · Cited by 30
Tumor expression of adiponectin receptor 2 and lethal prostate cancer
Rider, J. R., Fiorentino, M., Kelly, R. S., Gerke, T. A., Jordahl, K. M., Sinnott, J. A., Giovannucci, E. L., Loda, M. F., Mucci, L. A., Finn, S. P., et al. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv048 · Cited by 28
Functional Adiponectin Resistance and Exercise Intolerance in Heart Failure
Berendoncks, A. M. V., & Conraads, V. M. (2011) · Current Heart Failure Reports · doi:10.1007/s11897-011-0056-6 · Cited by 31
“It has been suggested that the HMW form is biologically active in the liver [19] and in endothelial cells [20] and is more strongly associated with IR, obesity, and cardiovascular disease [21].”
BackgroundAdiponectin resistance and vascular dysfunction in the hyperlipidemic state
Li, R., Lau, W. B., & Liang, X. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.95 · Cited by 28
Tabandeh, M. R., Golestani, N., Kafi, M., Hosseini, A., Saeb, M., & Sarkoohi, P. (2012) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2012.02.006 · Cited by 28
Fenofibrate promotes ischemia-induced revascularization through the adiponectin-dependent pathway
Li, P., Shibata, R., Maruyama, S., Kondo, M., Ohashi, K., Ouchi, N., & Murohara, T. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00284.2010 · Cited by 28
“Similarly, adiponectin enhances angiogenic responses in mouse ischemic hindlimb and rabbit cornea angiogenesis assays (18, 25, 33), whereas adiponectin suppresses tumor angiogenesis in vivo (6, 20).”
BackgroundLiu, F., Tan, A., Yang, R., Xue, Y., Zhang, M., Chen, L., Xiao, L., Yang, X., & Yu, Y. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2842-7 · Cited by 28
“Adiponectin (ACRP30), another wellstudied C1q family member, which possesses direct antidiabetic, anti-atherogenic, and anti-inflammatory properties, is demonstrated to stimulate the new blood vessel growth in endothelial cells [13].”
BackgroundMaternal serum adiponectin multimers in patients with a small-for-gestational-age newborn
Mazaki‐Tovi, S., Romero, R. J., Vaisbuch, E., Erez, O., Mittal, P., Chaiworapongsa, T., Kim, S. K., Pacora, P., Yeo, L., Gotsch, F., et al. (2009) · Journal of Perinatal Medicine · doi:10.1515/jpm.2009.128 · Cited by 28
Nakata, T., Ikeda, S., Koga, S., Yonekura, T., Tsuneto, A., Doi, Y., Fukae, S., Minami, T., Kawano, H., & Maemura, K. (2020) · International Heart Journal · doi:10.1536/ihj.20-114 · Cited by 26
Kato, M., Tsunekawa, S., Nakamura, N., Miura‐Yura, E., Yamada, Y., Hayashi, Y., Nakai‐Shimoda, H., Asano, S., Hayami, T., Motegi, M., et al. (2020) · Cells · doi:10.3390/cells9112385 · Cited by 30
“Endothelial cell infiltration into the plugs was assessed by immunohistochemical analysis of CD31-positive cells in accordance with a previous report [32].”
ResultCrosstalk Between Adipose and Lymphatics in Health and Disease
Westcott, G. P., & Rosen, E. D. (2021) · Endocrinology · doi:10.1210/endocr/bqab224 · Cited by 27
Roles of hydroxyeicosatetraenoic acids in diabetes (HETEs and diabetes)
Dong, L., Wang, H., Chen, K., & Li, Y. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113981 · Cited by 27
Adiponectin promotes endothelial cell differentiation from human peripheral CD14+monocytesin vitro
Yang, H., Zhang, R., Mu, H. H., Li, M., Yao, Q. C., & Chen, C. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00411.x · Cited by 27
“In addition, adiponectin is recently revealed to stimulate AMPactivated protein kinase (AMPK)-PI3-AKT signaling pathway to enhance EC proliferation and migration [13, 14] and inhibit EC apoptosis [15, 16].”
BackgroundInfluentialTran, T. T. P., Kim, H. G., Choi, J. H., Na, M., & Jeong, H. G. (2013) · Phytomedicine · doi:10.1016/j.phymed.2013.01.014 · Cited by 27
Expression levels of adiponectin receptors and periodontitis
Yamaguchi, N., Hamachi, T., Kamio, N., Akifusa, S., Masuda, K., Nakamura, Y., Nonaka, K., Maeda, K., Hanazawa, S., & Yamashita, Y. (2010) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2009.01222.x · Cited by 27
de Abreu, V. G., Martins, C. J. D. M., de Oliveira, P. A. C., & Francischetti, E. A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180947 · Cited by 27
Activation of liver X receptor suppresses angiogenesis via induction of ApoD
Lai, C., Cheng, H., Lin, C., Huang, S., Chen, T., Chung, C., Chang, C., Wang, H., & Chuu, C. (2017) · The FASEB Journal · doi:10.1096/fj.201700374r · Cited by 29
“Cross talkbetweenAkt, eNOS, andAMPKis involved in promotion of HUVEC angiogenesis induced by adiponectin (29).”
BackgroundKim, J.-Y., Jo, K.-J., Kim, B.-J., Baik, H., & Lee, S. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1070 · Cited by 27
Matar, D. B., Elahi, M. A., Sukkarieh, H. H., Nassar, W. K., & Aljada, A. (2025) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2025.120424 · Cited by 27
Pham, T. H., Jin, S. W., Lee, G. H., Park, J. S., Kim, J. Y., Thai, T. N., Han, E. H., & Jeong, H. G. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b07909 · Cited by 26
AMP-activated protein kinase: implications on ischemic diseases
Ahn, Y., Kim, H.-W., Lim, H., Lee, M., Kang, Y.-H., Moon, S.-J., Kim, H. S., & Kim, H.-H. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.9.169 · Cited by 25
“Compound C and adenosine 9-β-D-arabinofurano- 491http://bmbreports.org BMB Reports Anabolic processes AMPK activators (supplemental and drug) AMPK activators (natural) AMPK inhibitors Hepatic Fatty Acid Oxidation (17) Ketogenesis (17) Lipogenesis (35) Mitochondrial Biogenesis (36) Triglyceride Synthesis (36) Inhibitio…”
BackgroundBéjaoui, M., Zaoualí, M. A., Folch‐Puy, E., Pantazi, E. D., Bardag‐Gorce, F., Carbonell, T., Oliva, J., Rimola, A., Abdennebi, H. B., & Roselló‐Catafau, J. (2013) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12154 · Cited by 25
“A number of recent reports have studied both AMPK and Akt in the context of eNOS activation or NO release, but the relative role of these protein kinases remains controversial, with evidence for and against an AMPK/Akt interaction upstream of eNOS.([36,37]) Chen et al.”
Hou, H., Ge, S., Zhao, L., Wang, C., Wang, W., Zhao, X., & Sun, Z. (2017) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2017.0007 · Cited by 25
“Adiponectin, an adipocytokine composed of 244 amino acids, also named as ADIPOQ, is specifically secreted by adipose tissue (Ouchi et al., 2004; Yang et al., 2012).”
Non-viral adiponectin gene therapy into obese type 2 diabetic mice ameliorates insulin resistance
Park, J. H., Lee, M., & Kim, S. W. (2006) · Journal of Controlled Release · doi:10.1016/j.jconrel.2006.05.008 · Cited by 26
Aoki, C., Suzuki, K., Yanagi, K., Satoh, H., Niitani, M., & Aso, Y. (2012) · Journal of Pharmacological Sciences · doi:10.1254/jphs.12108fp · Cited by 25
Protective role of adiponectin against ethanol-induced gastric injury in mice
Yamamoto, S., Watabe, K., Araki, H., Kamada, Y., Kato, M., Kizu, T., Kiso, S., Tsutsui, S., Tsujii, M., Kihara, S., et al. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00324.2011 · Cited by 25
“Adiponectin promotes migration of endothelial cells and endothelial progenitor cells (31, 36).”
BackgroundSupplementation of Creatine and Ribose Prevents Apoptosis in Ischemic Cardiomyocytes
Caretti, A., Bianciardi, P., Sala, G., Terruzzi, C., Lucchina, F., & Samaja, M. (2010) · Cellular Physiology and Biochemistry · doi:10.1159/000323992 · Cited by 25
Adiponectin Stimulates Glucose Uptake in Rabbit Blastocysts1
Fischer, S., Santos, A. N., Thieme, R., Ramin, N., & Fischer, B. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.110.084665 · Cited by 25
“Interestingly, the dominant-negative PRKAA1/2 also inhibited the phosphorylation of AKT after adiponectin stimulation, whereas the dominant-negative AKT or pretreatment with a PIK3C2 inhibitor (LY294002 or wortmannin) did not [39].”
BackgroundKang, D. R., Yadav, D., Koh, S. B., Kim, J., & Ahn, S. V. (2017) · Yonsei Medical Journal · doi:10.3349/ymj.2017.58.2.339 · Cited by 25
Kaempferol improves glucose uptake in skeletal muscle via an AMPK-dependent mechanism
Moore, W. T., Luo, J., & Liu, D. (2023) · Food Science and Human Wellness · doi:10.1016/j.fshw.2023.03.028 · Cited by 26
CXC chemokine ligand 1 mediates adiponectin-induced angiogenesis in ovarian cancer
Ouh, Y., Cho, H., Lee, J. K., Choi, S. H., Choi, H. J., & Hong, J. H. (2019) · Tumor Biology · doi:10.1177/1010428319842699 · Cited by 24
Wang, Y., Zheng, Y., & Li, W. (2021) · Science China Life Sciences · doi:10.1007/s11427-020-1869-7 · Cited by 24
Optimization of adiponectin‐derived peptides for inhibition of cancer cell growth and signaling
Otvos, L. J., Kovalszky, I., Oláh, J., Coroniti, R., Knappe, D., Nollmann, F. I., Hoffmann, R., Wade, J. D., Lovas, S., & Surmacz, E. (2015) · Biopolymers · doi:10.1002/bip.22627 · Cited by 25
Kreth, S., Ledderose, C., Schütz, S. V., Beiras, A., Heyn, J., Weis, F. C., & Beiras-Fernández, A. (2013) · The Journal of Heart and Lung Transplantation · doi:10.1016/j.healun.2013.10.014 · Cited by 25
Komiya, N., Hirose, H., Kawabe, H., Itoh, H., & Saito, I. (2009) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.e588 · Cited by 24
Zhang, S., Guo, S., Gao, X., Liu, A., Jiang, W., Chen, X., Yang, P., Liu, L., Shi, L., & Zhang, Y. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14180 · Cited by 24
Sasaki, M., Kawano, T., Saitô, T., Yuzawa, M., Saito, T., Ikoma, A., Tamemoto, H., Kawakami, M., & Ishikawa, S. (2007) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e318031b7af · Cited by 24
Pathophysiological dual action of adiponectin after transient focal ischemia in mouse brain
Yatomi, K., Miyamoto, N., Komine‐Kobayashi, M., Liu, M., Oishi, H., Arai, H., Hattori, N., & Urabe, T. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.039 · Cited by 22
Increased adiponectin associated with poor survival in hepatocellular carcinoma
Wang, S., Yang, S., Tsai, H.-H., Lee, K., & Yeh, Y. (2013) · Journal of Gastroenterology · doi:10.1007/s00535-013-0898-7 · Cited by 23
Nigro, E., Mallardo, M., Polito, R., Scialò, F., Bianco, A., & Daniele, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147516 · Cited by 24
“Furthermore, in addition with our data, several studies have suggested that adiponectin may act as a chemotactic agent of endothelial cells [10].”
ResultDiabetes Mellitus and Heart Failure With Preserved Ejection Fraction: Role of Obesity
Dhore-Patil, A., Thannoun, T., Samson, R., & Jemtel, T. H. L. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2021.785879 · Cited by 27
Constantin, A. L., Dumitrescu, M., Mihai, M. C., Jianu, D. M., & Simionescu, M. (2016) · Lasers in Medical Science · doi:10.1007/s10103-016-2093-6 · Cited by 23
Gu, N., Wang, J., Di, Z., Liu, Z., Jia, X.-T., Yan, Y., Chen, X., Zhang, Q., & Qian, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00383 · Cited by 23
“The formation of vascularlike structures was evaluated according to the instructions (24).”
Duan, F., Wu, J., Chang, J., Peng, H., Liu, Z., Liu, P., Han, X., Sun, T., Shang, D., Yang, Y., et al. (2024) · Differentiation · doi:10.1016/j.diff.2024.100832 · Cited by 27
Miao, L., Cheong, M. S., Zhou, C., Farag, M. A. F., Cheang, W. S., & Xiao, J. (2022) · Food Frontiers · doi:10.1002/fft2.192 · Cited by 22
Adiponectinemia Controls Pro-Angiogenic Cell Therapy
Eren, P., Camus, S. M., Matrone, G., Ebrahimian, T. G., François, D., Tedgui, A., Silvestre, J., & Blanc‐Brude, O. (2009) · Stem Cells · doi:10.1002/stem.219 · Cited by 22
Hou, C., Tan, T., & Tang, C. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.01.013 · Cited by 22
Guo, M.-M., Duan, X., Cui, S., Tian, F.-G., Cao, X.-C., Geng, C., Fan, Z.-M., Wang, X., Wang, S., Jiang, H.-C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129246 · Cited by 23
“Among the different forms, HMW adiponectin may mediate the majority of adiponectin’s effects in endothelial cells[18].”
BackgroundBostancıoğlu, R. B., Demirel, S., Cin, G. T., & Koparal, A. T. (2013) · Drug and Chemical Toxicology · doi:10.3109/01480545.2013.776579 · Cited by 22
Bushra, S., Al‐Sadeq, D. W., Bari, R., Sahara, A. S., Fadel, A., & Rizk, N. M. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s358594 · Cited by 22
“Furthermore, adiponectin was found to counteract the angiogenesis in different microvascular endothelial cell types,(8) while on the contrary, it has been reported that APN has an angiogenic effect on HUVEC cells.(9) Human studies concerning the level of circulating adiponectin and its association with diabetic retino…”
BackgroundAngiogenesis in the New Zealand obese mouse model fed with high fat diet
Balwierz, A., Polus, A., Raźny, U., Wątor, Ł., Dyduch, G., Tomaszewska, R., Scherneck, S., Joost, H., & Dembinska-Kiec, A. (2009) · Lipids in Health and Disease · doi:10.1186/1476-511x-8-13 · Cited by 22
“Adiponectin induces NO release and acts protectively to vessels endothelium [17,18].”
Jalil, J., Gabrielli, L., Ocaranza, M. P., MacNab, P., Fernández, R., Grassi, B. A., Jofré, P., Verdejo, H., Mónica Acevedo, B., Samuel Córdova, A., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084407 · Cited by 25
“…it stimulates AMP-activated protein kinase (AMPK)-dependent and extracellular signal-regulated kinase signaling in cardiac myocytes and endothelial cells [38], reduces hypertrophy and fibrosis, activates the endothelial nitric oxide synthase system, and increases nitric oxide production [39,40].”
BackgroundCardiovascular Risk Factors in Obese Children and Adolescents
Rumińska, M., Majcher, A., Pyrżak, B., Czerwonogrodzka–Senczyna, A., Brzewski, M., & Demkow, U. A. (2015) · Advances in experimental medicine and biology · doi:10.1007/5584_2015_168 · Cited by 21
Song, Y., Yu, Q., Zhang, J., Huang, W., Liu, Y., Pei, H., Liu, J., Sun, L., Lü, Y., Li, C., et al. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00428.2013 · Cited by 21
Hypoadiponectinemia as a Marker of Adipocyte Dysfunction—Part I: The Biology of Adiponectin
Stern, N., Osher, E., & Greenman, Y. (2007) · Journal of the CardioMetabolic Syndrome · doi:10.1111/j.1559-4564.2007.06597.x · Cited by 21
Ni, M., Yang, Z., Li, D., Li, Q., Zhang, S., Su, D., Xie, H., & Shen, F. (2010) · Journal of Pharmacological Sciences · doi:10.1254/jphs.09335fp · Cited by 21
The potential of adipokines as therapeutic agents for cardiovascular disease
Shibata, R., Ohashi, K., Murohara, T., & Ouchi, N. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.07.005 · Cited by 21
“endothelial cell survival and differentiation into vascular-like structures in vitro [20,21].”
BackgroundKyrou, I., Mattu, H. S., Chatha, K. K., & Randeva, H. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803111-7.00007-5 · Cited by 21
Adiponectin protects against lung ischemia-reperfusion injury in rats with type 2 diabetes mellitus
Li, D., Song, L., Wang, J., Meng, C., & Cui, X. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8748 · Cited by 21
“increased risk of cardiovascular disease (CVD) development and obesity-associated types of cancer, including colon, breast, endometrial and prostate cancer (7,11-16).”
BackgroundIto, H., Wakatsuki, T., Yamaguchi, K., Fukuda, D., Kawabata, Y., Matsuura, T., Kusunose, K., Ise, T., Tobiume, T., Yagi, S., et al. (2020) · Circulation Journal · doi:10.1253/circj.cj-19-0914 · Cited by 21
Bostancıoğlu, R. B., Pekşen, C., Genç, H., Gürbüz, M., Karel, F. B., Koparal, A. S., Doğan, A., Köse, N., & Koparal, A. T. (2015) · Biomedical Materials · doi:10.1088/1748-6041/10/4/045024 · Cited by 21
“The matrigel tube formation assay was performed as previously described [30].”
MethodAdiponectin in the Heart and Vascular System
Ding, M., Rzucidlo, E. M., Davey, J. C., Xie, Y., Liu, R., Jin, Y., Stavola, L. K., & Martin, K. A. (2012) · Vitamins and hormones · doi:10.1016/b978-0-12-398313-8.00011-7 · Cited by 21
“Early studies revealed that adiponectin stimulates the differentiation and migration of human umbilical vein EC in vitro and stimulated blood vessel growth in vivo using mouse Matrigel plug implantation and rat corneal models (Ouchi et al., 2004).”
MethodMazaki‐Tovi, S., Romero, R. J., Vaisbuch, E., Chaiworapongsa, T., Erez, O., Mittal, P., Kim, S. K., Gotsch, F., Lamont, R., Oggè, G., et al. (2009) · Journal of Perinatal Medicine · doi:10.1515/jpm.2009.134 · Cited by 21
AlZaim, I., Al-Saidi, A., Hammoud, S. H., Darwiche, N., Al-Dhaheri, Y., Eid, A. H., & EL‐Yazbi, A. F. (2022) · Cancers · doi:10.3390/cancers14071679 · Cited by 23
Sopariwala, D. H., Rios, A. S., Park, M. K., Song, M. S., Kumar, A., & Narkar, V. A. (2022) · FASEB BioAdvances · doi:10.1096/fba.2022-00015 · Cited by 19
Sabouri, S., Ghayour‐Mobarhan, M., Moohebati, M., Hassani, M., Kasaian, J., Tatari, F., Kordi, F. M., Esmaeili, H. A., Tavallaie, S., Paydar, R., et al. (2011) · The Scientific World JOURNAL · doi:10.1100/tsw.2011.3 · Cited by 20
“The cardiovascular protective effects of adiponectin could be ascribed to different mechanisms, such as stimulation of angiogenesis, endothelial cell migration and differentiation, prevention of endothelial apoptosis, and reduction of the expression of TNF-α and vascular cell adhesion molecule-1[16,17,18,19].”
BackgroundBaldasseroni, S., Mannucci, E., Orso, F., Serio, C. D., Pratesi, A., Bartoli, N., Marella, G. A., Colombi, C., Foschini, A., Valoti, P., et al. (2011) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2011.03.012 · Cited by 20
Yoo, Y. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12064 · Cited by 20
Anti-breast cancer and anti-angiogenic potential of a lichen-derived small-molecule: barbatolic acid
Varol, M. (2018) · Cytotechnology · doi:10.1007/s10616-018-0249-x · Cited by 20
Regulation of Obesity by Antiangiogenic Herbal Medicines
Shin, S. S., & Yoon, M. (2020) · Molecules · doi:10.3390/molecules25194549 · Cited by 21
Lyzogubov, V. V., Tytarenko, R. G., Thotakura, S., Viswanathan, T., Bora, N. S., & Bora, P. S. (2009) · Cell Biology International · doi:10.1016/j.cellbi.2009.04.013 · Cited by 20
“, 2005), cell proliferation (Arita et al., 2002; Motoshima et al., 2004; Ouchi et al., 2004; Shibata et al., 2004), and apoptosis (Kobayashi et al.”
BackgroundHypoadiponectinemia: A common basis for diseases associated with overnutrition
Funahashi, T., & Matsuzawa, Y. (2006) · Current Atherosclerosis Reports · doi:10.1007/s11883-006-0042-8 · Cited by 21
“When we administrated adiponectin in vascular endothelial cells, adiponectin activated adenosine monophosphate (AMP) kinase, Akt, and subsequently phosphorylated endothelial NO synthase [ 26 ].”
BackgroundPlacental Endocrine Function and Hormone Action
Albrecht, E. D., & Pepe, G. J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397175-3.00040-5 · Cited by 20
Negi, S., Jeong, E.-M., Shukrullah, I., Veleder, E., Jones, D. P., Fan, T. M., Varadarajan, S., Danilov, S. M., Fukai, T., & Dudley, S. C. (2015) · BioMed Research International · doi:10.1155/2015/825027 · Cited by 20
“Adiponectin, a member of complement factor C1q family, is believed to prevent endothelial injury in the heart and vasculature by multiple mechanisms, including promoting eNOS activity and preserving bioactive NO [38].”
Effects of Chronic and Intermittent Calorie Restriction on Adropin Levels in Breast Cancer
Tuna, B. G., Atalay, P., Altunbek, M., Kalkan, B. M., & Doğan, S. (2017) · Nutrition and Cancer · doi:10.1080/01635581.2017.1359314 · Cited by 20
“Similar to adropin, adiponectin induces angiogenesis in endothelial cells (38).”
BackgroundInhibition of C1-Ten PTPase activity reduces insulin resistance through IRS-1 and AMPK pathways
Jeong, H., Koh, A., Lee, J., Park, D., Lee, J. O., Lee, M. N., Jo, K.-J., Tran, H. N. K., Kim, E., Min, B.-S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-18081-8 · Cited by 20
Xie, X., Yang, C., Cui, Q., Ma, W., Liu, J., Yao, Q., Zhang, Z., Xiao, L., & Wang, N. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b03501 · Cited by 20
Krenning, G., Moonen, J.-R. A. J., & Harmsen, M. C. (2009) · Circulation Research · doi:10.1161/circresaha.109.198044 · Cited by 20
Aging at the Crossroads of Organ Interactions: Implications for the Heart
Sen, I., Trzaskalski, N. A., Hsiao, Y., Liu, P. P., Shimizu, I., & Dérumeaux, G. (2025) · Circulation Research · doi:10.1161/circresaha.125.325637 · Cited by 20
“80 Notably, AT is one of the most vulnerable tissues during aging, and age-related immune response is first detected in white AT.”
Kim, H.-S., Lim, J., Lee, D. Y., Ryu, J., & Lim, J. (2014) · Oncology Reports · doi:10.3892/or.2014.3601 · Cited by 19
Metadata
- Authors
- Ouchi, N., Kobayashi, H., Kihara, S., Kumada, M., Sato, K., Inoue, T., Funahashi, T., & Walsh, K.
- Affiliations
- Boston University (US)
- The University of Osaka (JP)
- Corresponding author
- Walsh, Kenneth
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 2
- Pages
- 1304-1309
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4374490
- OpenAlex
- W2008967025
- Cited by
- 759
- References
- 49
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 20 · 2023: 15 · 2022: 21 · 2021: 23 · 2020: 23 · 2019: 25 · 2018: 22 · 2017: 40 · 2016: 26 · 2015: 39 · 2014: 30 · 2013: 58 · 2012: 58
- FWCI
- 14.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Uehara Memorial Foundation
- National Institutes of Health (HD23681, AG15052)
- National Institute on Aging (R01AG015052, AG17241, R37AG015052, AG15052, R01AG017241)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-40197, R01AR040197)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P01HD023681, HD23681)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- adiponectin, angiogenesis, AMPK, Akt signaling, endothelial cells, endothelial nitric oxide synthase, endothelial cell migration, endothelial differentiation, capillary tube formation, phosphatidylinositol 3-kinase, signaling crosstalk, blood vessel development
- MeSH terms
- Adenoviridae, Animals, Cell Differentiation, Cell Movement, Cells, Cultured, Chromones, Collagen, Drug Combinations, Endothelium, Vascular, Enzyme Inhibitors, Genes, Dominant, Humans, Laminin, Models, Biological, Morpholines, Multienzyme Complexes, Neovascularization, Pathologic, Phosphorylation, Proteins, Proteoglycans, Rabbits, Recombinant Proteins, Time Factors, Umbilical Veins, Blotting, Western, Signal Transduction, Protein Serine-Threonine Kinases, Nitric Oxide Synthase, Phosphatidylinositol 3-Kinases, Intercellular Signaling Peptides and Proteins, Endothelial Cells, Mice, Adiponectin, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type III, 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
