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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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“Adiponectin-activated AMPK signaling in endothelial cells is proangiogeni”
BackgroundSelf-citation
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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