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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.
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“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]
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Adipose Structure (White, Brown, Beige)
Peirce, V. J., Pellegrinelli, V., & Vidal‐Puig, A. (2015) · Springer eBooks · doi:10.1007/978-3-319-12125-3_23-1 · Cited by 3
Chen, L., Lu, X., Li, Y., Mao, Z.-F., Xiao, L., & Yu, Y. (2017) · Europe PMC (PubMed Central) · doi:10.3969/j.issn.1673-4254.2017.05.08 · Cited by 2
Cardioprotective Actions of Adiponectin
Ouchi, N., Shibata, R., & Walsh, K. X. (2007) · High Blood Pressure & Cardiovascular Prevention · doi:10.2165/00151642-200714020-00003 · Cited by 1
The role of Ad-36 and its E4orf-1 protein in modulating glycemic control
Dhurandhar, E. J. (2011) · Louisiana State University · doi:10.31390/gradschool_dissertations.1411 · Cited by 2
“Lastly, adiponectin up-regulates angiogenesis, and therefore may prevent hypoxia in adipose tissue (149; 150).”
BackgroundAdiponectin Level in Women with Breast Cancer
Homaee, F., Ghaffarzadehgan, K., Aziminia, A., Ghodrati, H., Izanloo, A., Ziaolhagh, R., & Khales, S. A. (2017) · Asian Pacific Journal of Cancer Biology · doi:10.31557/apjcb.2017.2.4.91-94 · Cited by 1
“Researchers have shown that lower levels of total adiponectin or HMW are correlated with the increased risk of breast cancer in menopausal women [13-14].”
BackgroundTanyanskiy, D. A. (2024) · Complex Issues of Cardiovascular Diseases · doi:10.17802/2306-1278-2024-13-1-179-195 · Cited by 1
Comparative effects of fatty acid and glucose in cardiac remodeling
Duttaroy, A. K., & Mallick, R. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-99570-2.00001-1 · Cited by 1
Umapathy, P., Arumugam, K., Babu, R. B., Nadig, R. R., Raman, R., Rao, G. S., Bhende, M. P., Natarajan, V., Ramkumar, K. M., & Rajesh, B. S. (2025) · International Ophthalmology · doi:10.1007/s10792-025-03482-w · Cited by 1
“There are reports which show adiponectin to have a proangiogenic potential [26] and they say APN may have varied effects on the retina depending on the stage of DR, providing protection in the early stages and causing fibrosis in the later stages of the disease [27].”
Predictive Value of Adiponectin for Long-Term MACEs in Non-Diabetic STEMI Patients
Krasniqi, X., Vincelj, J., Bytyçi, I., Berisha, B., & Bakalli, A. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14227936 · Cited by 1
“Both adiponectin and HDL have also been reported to increase nitric oxide production via activation of the AMPK-Akt-eNOS phosphorylation pathway, thereby contributing to vasodilatory cardioprotective effects [58–62].”
Mallardo, M., Russo, R., Daniele, A., Chambery, A., & Nigro, E. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11183-x · Cited by 1
Endothelial function for the evaluation of anti-atherosclerotic drugs
Okumura, K., & Cheng, X. W. (2010) · Hypertension Research · doi:10.1038/hr.2010.104 · Cited by 1
ADIPONECTINA PLASMÁTICA EN PREECLAMPSIA Y ECLAMPSIA
Reyna‐Villasmil, E., Mejía-Montilla, J., Reyna-Villasmil, N., Torres-Cepeda, D., & Peña-Paredes, E. (2008) · Revista chilena de obstetricia y ginecología · doi:10.4067/s0717-75262008000600005 · Cited by 1
Adiponectin effects on osteonectin gene expression in vascular smooth muscle cell line
Niknam, S., Samani, K. G., Amini, S. A., & Farokhi, E. (2014) · Majallah-i dānishgāh-i ̒ulūm-i pizishkī-i Māzandarān/Journal of Mazandaran University of Medical Sciences · Cited by 1
Lee, K., Jo, K.-J., Kim, J., Baik, H., & Lee, S. (2016) · The Korean Journal of Obesity · doi:10.7570/kjo.2016.25.4.190 · Cited by 1
Shiga, T. (2016) · PubMed · Cited by 1
Obesity-Related Endothelial Dysfunction and Metabolic Syndrome
Yılmaz, B. A., & Törüner, F. B. (2013) · CRC Press eBooks · doi:10.1201/b14907-10 · Cited by 1
Adipose Structure (White, Brown, Beige)
Pellegrinelli, V., Vidal‐Puig, A., & Carobbio, S. (2023) · Springer eBooks · doi:10.1007/978-3-319-12125-3_23-2 · Cited by 1
Yoo, E., Choi, H. J., & Han, H. J. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.09.016 · Cited by 1
Hirose, H., Kawabe, H., & Saito, I. (2012) · Ningen dock : official journal of the Japanese Society of Human Dry Dock · doi:10.11320/ningendock.26.951 · Cited by 1
Leptin, Adiponectin, and Other Adipokines in Regulation of Adipose Tissue Angiogenesis
Bråkenhielm, E., & Cao, Y. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8069-3_10 · Cited by 1
Everaert, B., Nijenhuis, V. J., Reith, F. C. M., Hoymans, V. Y., Timmermans, J., & Vrints, C. J. (2013) · Stem Cells International · doi:10.1155/2013/260156 · Cited by 1
“In conditions associated with decreased oxygen tension, the 𝛼 subunit of hypoxia-inducible factor 1, HIF-1𝛼, is upregulated at both the mRNA and the protein level [25] and translocates to the nucleus, where it promotes angiogenesis and vascular remodeling by enhancing the expression ofmultiple proangiogenic factors, s…”
BackgroundResultInfluentialAdiponectin-Based Therapeutics for Cancer Treatment
Li, D., Cao, H., Chen, J., Liu, M. R., & Wang, Y. (2017) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781681084817117040007 · Cited by 1
“By contrast, the globular domain of adiponectin increases endothelial activation, proliferation, migration and angiogenesis, largely through its binding to AdipoR1 or AdipoR2 [306, 307, 316 - 322].”
BackgroundThe Role of Adipose Tissue in Canine Cranial Cruciate Ligament Disease
Saengsoi, W. (2018) · University of Liverpool · doi:10.17638/03027258 · Cited by 1
“There is evidence that adiponectin stimulates endothelial cell migration and differentiation, which results in stimulated blood vessel growth in vivo in mouse Matrigel® plug implantation and in rabbit corneal models of angiogenesis (Ouchi et al., 2004).”
BackgroundГормони жирової тканини і гестаційний цукровий діабет
Payenok, O. S., Коrytko, О. О., & Петруняк, Р. И. (2013) · INTERNATIONAL JOURNAL OF ENDOCRINOLOGY (Ukraine) · doi:10.22141/2224-0721.7.55.2013.84680 · Cited by 1
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
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