Journal of ISSN: 2373-4345JDHODT

Dental Health, Oral Disorders & Therapy
Mini Review
Volume 6 Issue 1 - 2017
Association of TNF-Α, IL-1β with Chronic Periodontitis and Type 2 Diabetes Mellitus
Abdullah Seckin Ertugrul*
Department of Periodontology, Izmir Katip Celebi University, Turkey
Received: December 30, 2016 | Published: January 19, 2016
*Corresponding author: Abdullah Seckin Ertugrul, Department of Periodontology, Izmir Katip Celebi University, Izmir, Turkey, Email:
Citation: Ertugrul AS (2017) Association of TNF-Α, IL-1β with Chronic Periodontitis and Type 2 Diabetes Mellitus. J Dent Health Oral Disord Ther 6(1): 00188. DOI: 10.15406/jdhodt.2017.06.00188

Abstract

The most common endocrine disease, Diabetes Mellitus (DM), a metabolic disorder characterized by hyperglycemia, occurs due to the interaction of some environmental factors such as a high-fat diet, genetic history, and obesity. DM is classified into two categories: type-1 and type-2 DM.

  1. Type-1 DM (T1DM): occurs due to a reduction in insulin production as a result of autoimmune destruction of pancreatic cells, and is observed mostly in children and young adults.
  2. Type-2 DM (T2DM): is generally observed in adults and is characterized by the reduction in insulin resistance due to the failure in pancreatic beta cells to create a sufficient amount of insulin secretion.

Mini Review

T2DM constitutes 70-95% of DM patients [1,2]. IL-1β levels in GCF are lower in T2DM patients with gingivitis or slight periodontitis than in patients with moderate or severe periodontitis. Also, the levels of IL-1β in GCF in T2DM patients were higher than in systemically healthy patients [3]. Clinically healthy DM patients with pocket depth of not more than 3 mm have a more common form of periodontitis and have higher levels of prostaglandin E2 and TNF-α than systemically healthy patients [4]. Microorganism toxins are known to stimulate connection epithelium cells to secrete various inflammatory mediators in IL-1β, IL-6, TNF-α, and matrix metalloproteinases (MMPs). All of these mediators may pass over the connection of epithelium and reach the GCF. The normal flora of the body blocks the development of microorganisms and may act as an effective buffer against infections [5]. Cytokines that pioneer inflammation, such as IL-1β, IL-6, and TNF-α, play a very significant role in the initiation, regulation, and prolongation of natural immune response [6]. These cytokines cause vascular changes and the migration of cells such as from neutrophilia to periodontium. It is revealed that IL-1β, IL-6, and TNF-α have various activities that may cause tissue destruction, including chronic inflammation such as periodontitis [7]. IL-1β, IL-6, and TNF-α are the basic mediators of chronic inflammatory disease, and have the potential to destroy tissue and initiate bone loss [7,8]. It is revealed that IL-1β, IL-6, and TNF-α stimulate fibroblasts in cultures to produce collagenase [7-9]. Moreover, osteoblasts suppress alkaline phosphatase expression and matrix synthesis, and inhibit bone construction [10]. IL-1, which is the most powerful inducer of bone demineralization, exhibits a synergistic impact with TNF-a in stimulating bone resorption, as well as significant changes in collagen tissue matrix [11,12]. According to bone resorption trials, IL-1β is 100-fold more potent than TNF-α [13]. TNF-α molecules induce multiplication and differentiation of osteoclast pioneer cells and stimulate bone resorption by indirectly activating matured osteoclasts [14]. TNF-a also induces IL-6 production, which stimulates osteoclast formation, direct osteoclastic bone resorption, and T-cell differentiation [8].

The duty of the host defense system is to protect against infectious agents. Skin and mucous membranes create physical barriers against microorganism attacks and toxins and enable host defense. The flushing impact of liquids such as saliva and GCF is removed from organisms that invade in mucosal surfaces, and enables protection with bactericidal agents. The strict epithelial barrier of gingival sulcular epithelium and connection epithelium is known to block the invasion of microorganisms and products in periodontal tissues. Besides being complements to GCF, saliva and serum act as elements of host defense [15,16]. As a result of an immuno-inflammatory response developed in periodontal tissue that coincides to periodontal pathogen microorganisms, an increase occurs in the construction of inflammatory cytokines (IL-1β and TNF-α), chemotactic cytokines (IL-6), and tissue-destructive enzymes (MMPs). These proinflammatory mediators and enzymes are responsible for a great part of the destruction observed in periodontal disease [17]. The balance between inflammatory-anti-inflammatory cytokines and enzymes is more significant than the level of each inflammatory mediator found in periodontal tissues. The imbalance between cytokines and their inhibitors is the greatest factor responsible for the destruction of periodontal tissues [18]. Periodontal diseases may be defined as the inflammatory response of periodontal tissues against oral bacterial changes. Bacterial biofilm is very significant in gingival inflammation in periodontal tissues and periodontal tissue destruction. IL-1β and TNF-α are known to be cytokines that play a rather significant role in alveolar bone destruction [19]. Cytokines that play a significant role in periodontal diseases play a significant role in the initiation, regulation, and prolongation of natural immune response [20]. IL-1β and TNF-α cause vascular changes and also the migration of effector cells such as neutrophilia to periodontium. Thus, periodontal pathogens are suppressed and diminished. However, when the persistent nature of subgingival plaque combines with non-compliant cytokine response, the combination may cause inflammation and tissue destruction. The induction of primary mediators such as IL-1β and TNF-α stimulates the release of secondary mediators such as cyclooxygenase that cause the production of prostaglandins or chemokine acting as chemotactic cytokines. This enables inflammatory response in two routes, including the release of enzymes that cause collagen tissue destruction, and the resorption of osteoclastic bone resorption. Gelatinases (MMP-2 and MMP-9) act by destroying type IV collagen, laminin, and other basal membrane components. MMP-9 is an enzyme that allows insulin degradation. High levels of glucose contribute to the activation of latent MMP-9. Also, MMP-9 cells are considered to increase T-cell proliferation [21]. MMP-1, MMP-8, MMP-13, and MMP-18 are included in the collagenase group of enzymes. The basic property of these enzymes is the ability to destroy type I, II, and III collagens from a special region [22].

References

  1. Wu JT (1993) Review of diabetes: identification of markers for early detection, glycemic control, and monitoring clinical complications. J Clin Lab Anal 7(5): 293-300.
  2. American Diabetes Association (2006) Diagnosis and classification of diabetes mellitus. Diabetes care 29: S43-S48.
  3. Salvi GE, Beck JD, Offenbacher S (1998) PGE2, IL-1 beta, and TNF-alpha responses in diabetics as modifiers of periodontal disease expression. Ann Periodontol 3(1): 40-50.
  4. Offenbacher S, Collins JG, Heasman PA (1993) Diagnostic potential of host response mediators. Adv Dent Res 7(2): 175-181.
  5. Mathur A, Yang C, Wolff L (1996) Cytokines in gingival crevicular fluid of periodontally disseased and healthy sites. J Periodontal Res 31: 489-95.
  6. Okada H, Murakami S (1998) Cytokine expression in periodontal health and disease. Crit Rev Oral Biol Med 9(3): 248-266.
  7. Meikle MC, Atkinson SJ, Ward RV, Murphy G, Reynolds JJ (1989) Gingival fibroblasts degrade type I collagen films when stimulated with tumor necrosis factor and interleukin 1: evidence that breakdown is mediated by metalloproteinases. J PeriodontalRes 24(3): 207-213.
  8. Birkedal-Hansen H (1993) Role of cytokines and inflammatory mediators in tissue destruction. J Periodontal Res 28(6 Pt 2): 500-510.
  9. Richards D, Rutherford RB (1988) The effects of interleukin 1 on collagenolytic activity and prostaglandin-E secretion by human periodontal-ligament and gingival fibroblast. Archives of Oral Biology 33(4): 237-243.
  10. Gamonal J, Acevedo A, Bascones A, Jorge O, Silva A (2000) Levels of interleukin-1β, -8 and -10 and RANTES in gingival crevicular fluid and cell populations in adult periodontitis patients and the effect of periodontal treatment. J Periodontol 71: 1535-1545.
  11. Gowen M, Wood DD, Ihrie EJ, Mc Guire MK, Russell RG (1983) An interleukin 1 like factor stimulates bone resorption in vitro. Nature 306(5941): 378-380.
  12. Qwarnström EE, Mac Farlane SA, Page RC (1989) Effects of interleukin-1 on fibroblast extracellular matrix, using a 3-dimensional culture system. J Cell Physiol 139(3): 501-508.
  13. Stashenko P, Dewhirst FE, Rooney ML, Desjardins LA, Heeley JD (1987) Interleukin-1 beta is a potent inhibitor of bone formation in vitro. J Bone Miner Res 2(6): 595-565.
  14. Yoneda T, Alsina, Chavez, Bonewald, Nishimura, et al. (1991) Evidence that tumor necrosis factor plays a pathogenetic role in the paraneoplastic syndromes of cachexia, hypercalcemia, and leukocytosis in a human tumor in nude mice. J Clin Invest87(3): 977-985.
  15. Lamster IB, DePaola DP, Oppermann RV, Papapanou PN, Wilder RS (2000) The relationship of periodontal disease to diseases and disorders at distant sites: communication to health care professionals and patients. J Am Dent Assoc 139(10): 1389-1397.
  16. Kinane DF (2000) Periodontal diagnostics. Ann R Australas Coll Dent Surg 15: 34-41.
  17. Preshaw PM (2008) Host response modulation in periodontics. Periodontol48: 92-110.
  18. Van Dyke TE, Tohme ZN (2000) Periodontal diagnosis: evaluation of current concepts and future needs. J Int Acad Periodontol 2(3): 71-78.
  19. Graves DT, Cochran D (2003) The contribution of interleukin-1 and tumor necrosis factor to periodontal tissue destruction. J Periodontol 74(3): 391-401.
  20. Mathur A, Michalowicz B, Castillo M, Aeppli D (1996) Interleukin-1 alpha, interleukin-8 and interferon-alpha levels in gingival crevicular fluid. J Periodontal Res 31(7): 489-495.
  21. Greenwald RA, Golub LM, Ramamurthy NS, ChowdhuryM, Moak Sa, et al. (1998) In vitro sensitivity of the three mammalian collagenases to tetracycline inhibition: relationship to bone and cartilage degradation. Bone 22(1): 33-38.
  22. Allan JA, Docherty AJ, Barker PJ, Huskisson NS, Reynolds JJ, et al. (1995) Binding of gelatinases A and B to type collagen and other matrix components. Biochem J 309(Pt 1): 299-306.
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