Inflammasomes and their regulation in periodontal disease: a review

Kübra Aral, Michael Milward, Yvonne Kapila, Afig Berdeli, Paul Cooper

Research output: Contribution to journalReview articlepeer-review

13 Citations (Scopus)
286 Downloads (Pure)


Interleukin‐1β (IL‐1β), which is secreted by host tissues leading to periodontal tissue inflammation, is a major pro‐inflammatory cytokine in the pathogenesis of periodontal disease. The conversion of pro‐IL‐1β into its biologically active form is controlled by multiprotein complexes named as inflammasomes, which are key regulator of host defense mechanisms and inflammasome involved diseases, including the periodontal diseases. Inflammasomes are regulated by different proteins and processes, including pyrin domain (PYD)‐only proteins (POPs), CARD‐only proteins (COPs), tripartite motif family proteins (TRIMs), autophagy, and interferons. A review of in vitro, in vivo, and clinical data from these publications revealed that several inflammasomes including (NOD)‐like receptor (NLR) pyrin domain‐containing 3 (NLRP3) and absent in melanoma 2 (AIM2) have been found to be involved in periodontal disease pathogenesis. To the best of our knowledge, the current article provides the first review of the literature focusing on studies that evaluated both inflammasomes and their regulators in periodontal disease. An upregulation for inflammasomes and a downregulation of inflammasome regulator proteins including POPs, COPs, and TRIMs have been reported in periodontal disease. Although interferons (types I and II) and autophagy have been found to be involved in periodontal disease, their possible role in inflammasome activation has not evaluated yet. Modulating the excessive inflammatory response by the use of inflammasome regulators may have potential in the management of periodontal disease.
Original languageEnglish
Pages (from-to)473-487
JournalJournal of Periodontal Research
Issue number4
Early online date20 Jan 2020
Publication statusE-pub ahead of print - 20 Jan 2020


  • autophagy
  • caspase activation and recruitment domains
  • inflammasomes
  • interferons
  • periodontal disease
  • pyrin domain
  • tripartite motif proteins


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