Adiponectin Inhibits Tumor Necrosis Factor-α–Induced Vascular Inflammatory Response via Caveolin-Mediated Ceramidase Recruitment and Activation
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Rationale: Anti-inflammatory and vascular protective actions of adiponectin are well recognized. However, many fundamental questions remain unanswered. Objective: The current study attempted to identify the adiponectin receptor subtype responsible for adiponectin’s vascular protective action and investigate the role of ceramidase activation in adiponectin anti-inflammatory signaling. Methods and Results: Adiponectin significantly reduced tumor necrosis factor (TNF)α–induced intercellular adhesion molecule-1 expression and attenuated TNFα-induced oxidative/nitrative stress in human umbilical vein endothelial cells. These anti-inflammatory actions were virtually abolished by adiponectin receptor 1 (AdipoR1-), but not AdipoR2-, knockdown (KD). Treatment with adiponectin significantly increased neutral ceramidase (nCDase) activity (3.7-fold; P <0.01). AdipoR1-KD markedly reduced globular adiponectin–induced nCDase activation, whereas AdipoR2-KD only slightly reduced. More importantly, small interfering RNA-mediated nCDase-KD markedly blocked the effect of adiponectin on TNFα-induced intercellular adhesion molecule-1 expression. AMP-activated protein kinase-KD failed to block adiponectin-induced nCDase activation and modestly inhibited adiponectin anti-inflammatory effect. In contrast, in caveolin-1 KD (Cav1-KD) cells, >87% of adiponectin-induced nCDase activation was lost. Whereas adiponectin treatment failed to inhibit TNFα-induced intercellular adhesion molecule-1 expression, treatment with sphingosine-1-phosphate or SEW (sphingosine-1-phosphate receptor agonist) remained effective in Cav1-KD cells. AdipoR1 and Cav1 colocalized and coprecipitated in human umbilical vein endothelial cells. Adiponectin treatment did not affect this interaction. There is weak basal Cav1/nCDase interaction, which significantly increased after adiponectin treatment. Knockout of AdipoR1 or Cav1 abolished the inhibitory effect of adiponectin on leukocyte rolling and adhesion in vivo. Conclusions: These results demonstrate for the first time that adiponectin inhibits TNFα-induced inflammatory response via Cav1-mediated ceramidase recruitment and activation in an AdipoR1-dependent fashion.
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Elevated TNF directly suppresses adiponectin, halting muscle protein synthesis and mitochondrial processes.
“Elevated TNF directly inhibits adiponectin63, arresting muscle protein synthesis and mitochondrial processes64.”
From Sarcopenic obesity in older adults: aetiology, epidemiology and treatment strategies (2018) · cites this paper as [63]
Citation 63 is attached to the assertion that elevated TNF directly inhibits adiponectin; the muscle-process assertion has a separate citation. The Results section describes adiponectin inhibiting TNFα-induced inflammation in endothelial cells, but the passages found when searching for TNF suppression of adiponectin do not address whether TNF directly inhibits adiponectin. No page number is available in our copy. (LLM, conf=0.74)
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- Authors
- Wang, Y., Wang, X., Lau, W. B., Yuan, Y., Booth, D., Li, J.-J., Scalia, R., Preston, K., Gao, E., Koch, W., & Ma, X.-L.
- Affiliations
- Thomas Jefferson University (US)
- From the Department of Emergency Medicine (Y.W., X.W., W.B.L., Y.Y., J.-J.L., X.-L.M.) and Department of Pathology (D.B.), Thomas Jefferson University, Philadelphia, PA; and Department of Physiology, Cardiovascular Research Center (R.S., K.P.) and Center for Translational Medicine (E.G., W.K.), Temple University, Philadelphia, PA.
- Venue
- Circulation Research
- Published
- 2014-02-28
- Volume
- 114
- Issue
- 5
- Pages
- 792-805
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC3961763
- OpenAlex
- W2081966889
- Cited by
- 104
- References
- 51
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 8 · 2023: 9 · 2022: 9 · 2021: 11 · 2020: 12 · 2019: 7 · 2018: 9 · 2017: 12 · 2016: 11 · 2015: 4 · 2014: 4
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- The Medicine Forum (submittedVersion)
- Funders
- National Institutes of Health (1s10od010408-01)
- National Heart, Lung, and Blood Institute (T32HL091804, HL 63828, R01HL063828, R01HL096686, P01HL108806, HL-096686)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK096521, R01DK064344)
- Topics
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- adiponectin, TNF-α, caveolin-1, neutral ceramidase, AdipoR1, AdipoR2, endothelial inflammation, ICAM-1, sphingosine-1-phosphate, AMPK, leukocyte adhesion, vascular inflammation, anti-inflammatory signaling, human umbilical vein endothelial cells
- MeSH terms
- Enzyme Activation, Humans, Tumor Necrosis Factor-alpha, Vasculitis, Signal Transduction, Reactive Oxygen Species, Reactive Nitrogen Species, RNA, Small Interfering, Leukocyte Rolling, Endothelial Cells, Caveolin 1, Adiponectin, Receptors, Adiponectin, Ceramidases, Gene Knockdown Techniques, Human Umbilical Vein Endothelial Cells
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