α1-antitrypsin mitigates NLRP3-inflammasome activation in amyloid β1-42-stimulated murine astrocytes

J Neuroinflammation. 2018 Sep 27;15(1):282. doi: 10.1186/s12974-018-1319-x.

Abstract

Background: Neuroinflammation has an essential impact on the pathogenesis and progression of Alzheimer's disease (AD). Mostly mediated by microglia and astrocytes, inflammatory processes lead to degeneration of neuronal cells. The NLRP3-inflammasome (NOD-like receptor family, pyrin domain containing 3) is a key component of the innate immune system and its activation results in secretion of the proinflammatory effectors interleukin-1β (IL-1β) and interleukin-18 (IL-18). Under physiological conditions, cytosolic NLRP3-inflammsome is maintained in an inactive form, not able to oligomerize. Amyloid β1-42 (Aβ1-42) triggers activation of NLRP3-inflammasome in microglia and astrocytes, inducing oligomerization and thus recruitment of proinflammatory proteases. NLRP3-inflammasome was found highly expressed in human brains diagnosed with AD. Moreover, NLRP3-deficient mice carrying mutations associated with familial AD were partially protected from deficits associated with AD. The endogenous protease inhibitor α1-antitrypsin (A1AT) is known for its anti-inflammatory and anti-apoptotic properties and thus could serve as therapeutic agent for NLRP3-inhibition. A1AT protects neurons from glutamate-induced toxicity and reduces Aβ1-42-induced inflammation in microglial cells. In this study, we investigated the effect of Aβ1-42-induced NLRP3-inflammasome upregulation in primary murine astrocytes and its regulation by A1AT.

Methods: Primary cortical astrocytes from BALB/c mice were stimulated with Aβ1-42 and treated with A1AT. Regulation of NLRP3-inflammasome was examined by immunocytochemistry, PCR, western blot and ELISA. Our studies included an inhibitor of NLRP3 to elucidate direct interactions between A1AT and NLRP3-inflammasome components.

Results: Our study revealed that A1AT reduces Aβ1-42-dependent upregulation of NLRP3 at the mRNA and protein levels. Furthermore, A1AT time-dependently mitigated the expression of caspase 1 and its cleavage product IL-1β in Aβ1-42-stimulated astrocytes.

Conclusion: We conclude that Aβ1-42-stimulation results in an upregulation of NLRP3, caspase 1, and its cleavage products in astrocytes. A1AT time-dependently hampers neuroinflammation by downregulation of Aβ1-42-mediated NLRP3-inflammasome expression and thus may serve as a pharmaceutical opportunity for the treatment of Alzheimer's disease.

Keywords: Alpha 1-antitrypsin; Alzheimer’s disease; Amyloid β; Astrocytes; Inflammasome; NALP3; NLRP3; Neuroinflammation.

MeSH terms

  • Amyloid beta-Peptides / toxicity*
  • Animals
  • Animals, Newborn
  • Astrocytes / drug effects*
  • Brain / cytology
  • Calcium-Binding Proteins / metabolism*
  • Cells, Cultured
  • Cytokines / metabolism
  • Dose-Response Relationship, Drug
  • Furans
  • Glial Fibrillary Acidic Protein / metabolism
  • Heterocyclic Compounds, 4 or More Rings / pharmacology
  • Indenes
  • Inflammasomes / metabolism
  • L-Lactate Dehydrogenase / metabolism
  • Lipopolysaccharides / pharmacology
  • Mice
  • Mice, Inbred BALB C
  • Microfilament Proteins / metabolism*
  • NLR Family, Pyrin Domain-Containing 3 Protein / antagonists & inhibitors
  • NLR Family, Pyrin Domain-Containing 3 Protein / genetics
  • NLR Family, Pyrin Domain-Containing 3 Protein / metabolism*
  • Peptide Fragments / toxicity*
  • Sulfonamides
  • Sulfones / pharmacology
  • Trypsin Inhibitors / pharmacology*
  • Up-Regulation / drug effects
  • alpha 1-Antitrypsin / pharmacology*

Substances

  • Aif1 protein, mouse
  • Amyloid beta-Peptides
  • Calcium-Binding Proteins
  • Cytokines
  • Furans
  • Glial Fibrillary Acidic Protein
  • Heterocyclic Compounds, 4 or More Rings
  • Indenes
  • Inflammasomes
  • Lipopolysaccharides
  • Microfilament Proteins
  • NLR Family, Pyrin Domain-Containing 3 Protein
  • Peptide Fragments
  • Sulfonamides
  • Sulfones
  • Trypsin Inhibitors
  • alpha 1-Antitrypsin
  • amyloid beta-protein (1-42)
  • N-(1,2,3,5,6,7-hexahydro-S-indacen-4-ylcarbamoyl)-4-(2-hydroxy-2-propanyl)-2-furansulfonamide
  • L-Lactate Dehydrogenase