Adiponectin Stimulates Angiogenesis in Response to Tissue Ischemia through Stimulation of AMP-activated Protein Kinase Signaling
Open accessAbstract
Obesity is a risk factor for the development of cardiovascular diseases that are associated with impaired angiogenesis. Adiponectin is an adipocyte-specific adipocytokine with anti-atherogenic and anti-diabetic properties, and its plasma levels are reduced in association with obesity-linked diseases. Here, we investigated whether adiponectin regulates angiogenesis in response to tissue ischemia using adiponectin knock-out (KO) mice. Angiogenic repair of ischemic hind limbs was impaired in adiponectin-KO mice compared with wild-type (WT) mice as evaluated by laser Doppler flow method and capillary density analyses. Adenovirus-mediated supplement of adiponectin accelerated angiogenic repair in both adiponectin-KO and WT mice. Intramuscular injection of an adenovirus encoding dominant-negative AMP-activated kinase diminished the improvement in limb perfusion seen in WT mice and abolished the adiponectin-induced enhancement of perfusion. These data indicate that adiponectin can function to stimulate angiogenesis in response to ischemic stress by promoting AMP-activated kinase signaling. Therefore, adiponectin may be useful in the treatment for obesity-related vascular deficiency diseases.
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Adipose tissue secretes several adipokines and endogenous angiogenesis inhibitors that modulate new blood vessel formation, including adiponectin, leptin, resistin, visfatin/thrombospondin 1, and plasminogen activator inhibitor.
“In addition to authentic angiogenic factors, AT secretes several important adipokines and endogenous angiogenesis inhibitors to modulate the balance of new blood vessel formation, including adiponectin (36,37), leptin (34), resistin (38), visfatin/thrombospondin 1 (39), and plasminogen activator inhibitor (40).”
From The ominous triad of adipose tissue dysfunction: inflammation, fibrosis, and impaired angiogenesis. (2017) · cites this paper as [37]
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Adiponectin promotes endothelial progenitor cell number and function
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Self-citation
- Authors
- Shibata, R., Ouchi, N., Kihara, S., Sato, K., 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
- 2004-07
- Volume
- 279
- Issue
- 27
- Pages
- 28670-28674
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1990840335
- Cited by
- 336
- References
- 35
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 10 · 2023: 10 · 2022: 7 · 2021: 7 · 2020: 13 · 2019: 7 · 2018: 6 · 2017: 16 · 2016: 5 · 2015: 13 · 2014: 21 · 2013: 19 · 2012: 23
- FWCI
- 13.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HD23681, AG15052)
- U.S. Public Health Service (HE 23641)
- National Institute on Aging (AG17241, AG15052, R01AG017241)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-40197, R01AR040197)
- Topics
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- adiponectin, angiogenesis, tissue ischemia, AMPK, AMPK signaling, hindlimb ischemia, limb perfusion, adiponectin knockout mice, adenoviral gene transfer, obesity, adipokines
- MeSH terms
- Adenoviridae, Animals, Antibodies, Monoclonal, Capillaries, Genes, Dominant, Ischemia, Mice, Inbred C57BL, Multienzyme Complexes, Neovascularization, Pathologic, Obesity, Proteins, Time Factors, Blotting, Western, Signal Transduction, Protein Serine-Threonine Kinases, Adipocytes, Gene Transfer Techniques, Mice, Knockout, Platelet Endothelial Cell Adhesion Molecule-1, Intercellular Signaling Peptides and Proteins, Mice, Adiponectin, AMP-Activated Protein Kinases
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