Coronary endothelial dysfunction induced by nucleotide oligomerization domain-like receptor protein with pyrin domain containing 3 inflammasome activation during hypercholesterolemia: beyond inflammation

Antioxid Redox Signal. 2015 May 1;22(13):1084-96. doi: 10.1089/ars.2014.5978. Epub 2015 Mar 31.

Abstract

Aims: This study hypothesized that activation of endothelial nucleotide oligomerization domain-like receptor protein with pyrin domain containing 3 (Nlrp3) inflammasomes directly produces endothelial dysfunction during hypercholesterolemia, which is distinct from its canonical roles in inflammation.

Results: Acute hypercholesterolemia in mice was induced by intraperitoneal administration of poloxamer 407 (0.5 g/kg) for 24 h. Endothelial dysfunction was assessed by evaluating endothelium-dependent vasodilation in isolated, perfused, and pressurized coronary arteries in response to bradykinin (10(-10)-10(-6) M) and acetylcholine (10(-9)-10(-5) M). Impaired endothelium-dependent vasodilation was observed in Nlrp3(+/+) mice with acute hypercholesterolemia, which was markedly ameliorated in Nlrp3(-/-) mice. Treatment of mice with inhibitors for caspase-1 or high mobility group box 1 (HMGB1) significantly restored endothelium-dependent vasodilation in Nlrp3(+/+) mice with acute hypercholesterolemia. Confocal microscopic analysis demonstrated that hypercholesterolemia markedly increased caspase-1 activity and HMGB1 expression in coronary arterial endothelium of Nlrp3(+/+) mice, which was absent in Nlrp3-deficient mice. Further, recombinant HMGB1 directly induced endothelial dysfunction in normal Nlrp3(+/+) coronary arteries. In vitro, Nlrp3 inflammasome formation and its activity were instigated in cultured endothelial cells by cholesterol crystal, a danger factor associated with hypercholesterolemia. Moreover, cholesterol crystals directly induced endothelial dysfunction in coronary arteries from Nlrp3(+/+) mice, which was attenuated in Nlrp3(-/-) arteries. Such cholesterol crystal-induced impairment was associated with enhanced superoxide production, downregulation of endothelial nitric oxide synthase activity, and pyroptosis.

Innovation and conclusion: Our data provide the first evidence that activation of endothelial Nlrp3 inflammasome directly impairs endothelial function beyond its canonical inflammatory actions. This novel non-canonical action of Nlrp3 inflammasomes may initiate or exacerbate vascular injury during hypercholesterolemia.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / adverse effects
  • Animals
  • Bradykinin / adverse effects
  • Carrier Proteins / metabolism
  • Caspase 1 / metabolism
  • Cholesterol / pharmacology
  • Coronary Vessels / drug effects
  • Coronary Vessels / metabolism
  • Coronary Vessels / pathology*
  • Cytoskeletal Proteins / metabolism
  • Disease Models, Animal
  • Endothelial Cells / drug effects
  • Endothelial Cells / metabolism*
  • Glycyrrhizic Acid / pharmacology
  • HMGB1 Protein / metabolism
  • Hypercholesterolemia / chemically induced
  • Hypercholesterolemia / metabolism*
  • Hypercholesterolemia / pathology
  • Inflammasomes / metabolism*
  • Inflammation / metabolism*
  • Male
  • Mice, Inbred C57BL
  • NLR Family, Pyrin Domain-Containing 3 Protein
  • Nitric Oxide / metabolism
  • Nucleotides / metabolism
  • Poloxamer
  • Pyrin
  • Pyroptosis / drug effects
  • Reactive Oxygen Species / metabolism
  • Receptors, Cell Surface / metabolism*
  • Serpins / pharmacology
  • Superoxides / metabolism
  • Vasodilation / drug effects
  • Viral Proteins / pharmacology

Substances

  • Carrier Proteins
  • Cytoskeletal Proteins
  • HMGB1 Protein
  • Inflammasomes
  • Mefv protein, mouse
  • NLR Family, Pyrin Domain-Containing 3 Protein
  • Nlrp3 protein, mouse
  • Nucleotides
  • Pyrin
  • Reactive Oxygen Species
  • Receptors, Cell Surface
  • Serpins
  • Viral Proteins
  • Poloxamer
  • Superoxides
  • Nitric Oxide
  • Glycyrrhizic Acid
  • interleukin-1beta-converting enzyme inhibitor
  • Cholesterol
  • Caspase 1
  • Acetylcholine
  • Bradykinin