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CONCISE REVIEW |
1 UFR d’Odontologie, Service de Parodontologie, 1 Place Alexis Ricordeau, BP 84215, 44 042 Nantes, Cedex 1, France;
2 INSERM U26 - Université Paris VII, Service de Réanimation Médicale et Toxicologique, Hôpital Lariboisière, 2 rue Ambroise Paré, 75010, Paris, France; and
3 Periodontal Research Group, Birmingham University Dental School, St Chads Queensway, Birmingham B4 6NN, UK;
* corresponding author, bruno-megarbane{at}wanadoo.fr
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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2-macroglobulin to bind Tumor Necrosis Factor-alpha, IL-2, and IL-6, and facilitates the release of various growth factors. TauCl inhibits the production of inflammatory mediators, prostaglandins, and nitric oxide. HOCl activates tyrosine kinase signaling cascades, generating an increase in the production of extracellular matrix components, growth factors, and inflammatory mediators. Thus, HOCl and TauCl appear to play a crucial role in the periodontal inflammatory process. Taken together, these findings may offer opportunities for the development of novel host-modulating therapies for the treatment of periodontitis.
KEY WORDS: periodontitis • hypochlorous acid (HOCl) • taurine-N-monochloramine (TauCl) • cytokine • inflammation • healing
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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In some individuals, susceptibility to periodontitis results from altered neutrophilic polymorphonuclear leukocyte (PMN) function or recruitment. One aspect of altered PMN function is that of the production and release of reactive oxygen species (ROS), such as hypochlorous acid (HOCl). HOCl and taurine-N-monochloramine (TauCl) are end-products of the PMN myeloperoxidase-H2O2-Cl2 system. To date, therapeutic use of NaOCl (HOCl sodium salt) and TauCl solutions in periodontitis has not been considered. However, low concentrations of both molecules are associated with compromises in anti-infection defenses, antigen neutralization, and regulation of the inflammatory reaction (Marcinkiewicz et al., 2000; Kontny et al., 2003a; Reeves et al., 2003). Experimental studies suggest that HOCl and TauCl influence redox-regulated cell processes, including modulation of receptors, signaling pathways, and gene transcription (Gopalakrishna and Jaken, 2000; Midwinter et al., 2001; Schieven et al., 2002; Kontny et al., 2003a). Thus, although never previously recognized, HOCl and TauCl may be of potential benefit as adjunctive therapies for periodontitis patients. The objectives of this review are to discuss in detail the possible roles of HOCl and TauCl as novel therapeutic agents, and their likely involvement in the pathogenesis of periodontal diseases.
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CHLORINATION AND OXIDATION PROPERTIES OF HOCl AND TAURINE CHLORAMINE |
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TOPABSTRACTINTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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EFFECTS ON ANTIGENS AND HOST-DERIVED MEDIATORS IN THE EXTRACELLULAR ENVIRONMENT |
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TOPABSTRACTINTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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Within physiological concentration ranges, HOCl has, in vitro, an immediate and highly effective microbicidal activity. HOCl induces irreversible oxidation of various bacterial respiratory electron transporters (Prütz et al., 2001). TauCl mainly generates time-dependent and extended bactericidal properties, which are significantly enhanced within an acidic environment (pH 
5) (Marcinkiewicz et al., 2000). Moreover, HOCl and TauCl may repulse some motile bacteria, especially those with flagella and gliding properties; however, the mechanism of this repulsive activity remains unclear (Liu and Fridovich, 1996). HOCl and TauCl-chlorination of proteins, or the proteinaceous part of antigens, increases their immunogeneity, which promotes the presentation of these proteins by antigen-presenting cells (APC), such as monocytes, macrophages, or dendritic cells (Kontny et al., 2003a). HOCl and TauCl-mediated PMN chlorinating activity also plays a role in PMN-macrophage interactions. Chlorination of antigens selectively promotes the non-specific immune response against Gram-negative periodontal pathogens, and reduces the response induced by Gram-positive bacteria. This affects antigen-phagocytosis-activated production of inflammatory mediators by macrophages, but the mechanisms involved remain unclear. Thus, chlorination of endotoxins (such as LPS) released from Gram-negative pathogens does not affect the secretory activity of the macrophage, whereas chlorination of Gram-positive bacteria-released antigens does significantly affect macrophage secretory activity. The release of nitric oxide and Tumor Necrosis Factor-alpha (TNF-) is decreased, while phagocytosis and Interleukin-6 (IL-6) production are preserved (Marcinkiewicz et al., 1994), but underlying mechanisms are still to be elucidated.
In addition, some harmful exotoxins may undergo oxidative-neutralization. Thus, HOCl-induced oxidation of a crucial cysteine residue of the active site of the gingipains Rgp and Kgp (2 cysteine proteases of Porphyromonas gingivalis) may reduce their potentially harmful activity on the periodontal tissues (Curtis et al., 2001).
However, most of these biochemical activities generate, in vivo, a loss of HOCl and TauCl antibacterial properties, which results in a spontaneous neutralization of their oxidative activities by the enormous amount of proteins present inside and outside phagocytic vacuoles (Reeves et al., 2003). How effective the oxidation properties of HOCl and TauCl are in vivo remains unresolved; nevertheless, such products of the neutrophil respiratory burst induce ideal conditions for microbicidal destruction by proteases rather than their oxidative killing.
Inflammatory Response Modulation
The innate inflammatory response is initiated by a release of histamine from mast cells, leading to a local increase in both capillary pressure and endothelial permeability. Simultaneously, the bacterial LPS both activates acquired immune response and stimulates epithelial cells, fibroblasts, and APCs to produce pro-inflammatory mediators (such as chemokines, IL-1, IL-6, TNF, GM-CSF, matrix metalloproteinases [MMPs], and prostaglandin PGE2), that stimulate (Teng, 2003):
(MIP-1), receptor activator of NF-
B ligand (RANK-L), superoxide anions, eicosanoids (PGE2 and leukotrienes), IL-6, TNF, and/or IL-1ß-mediated osteoclast activation.
HOCl and TauCl possess both pro- and anti-inflammatory properties that may modulate the inflammatory response within the periodontal tissues (Fig. 1
). Anti-inflammatory effects appear to predominate and are summarized below:
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, IL-1ß, IL-2, and IL-6), regulate metalloproteinases, and release activated growth factors. This activity is related to either a direct oxidation of crucial thiol or thioether residue(s) in these molecules or to an indirect modulating effect on the capacity of 2-macroglobulins to bind them: 2-macroglobulins are plasma molecules that bind and neutralize proteases, cytokines (including TNF-, IL-1ß, IL-2, IL-6, and IL-8), and growth factors including TGF-ß, basic fibroblast growth factor (bFGF, also called FGF-2), ß-nerve growth factor (ß-NGF), and platelet-derived growth factor (PDGF). In plasma, 2-macroglobulin binding affinity is higher to growth factors (with Kd values in a nanomolar range) than to cytokines (with Kd values in a micromolar range). Consequently, 85–90% of TGF-ß and PDGF molecules are inactive, bound to 2-macroglobulins. HOCl-associated 2-macroglobulin oxidation induces: (1) a decrease of protease binding, (2) an important increase of 2-macroglobulin affinity for TNF-, IL-2, and IL-6 (Kd values in the nanomolar range with a five-fold increase of their binding rate), and (3) a greater decrease of affinity to ß-NGF, PDGF-BB, TGF-ß1, and TGF-ß2 (with a nine- or 13-fold decrease of the binding rate to PDGF-BB and TGF-ß2, respectively). In addition, 2-macroglobulin reacts with methylamine, a nucleophilic primary amine, forming an 2-macroglobulin-methylamine complex, which can be oxidized by HOCl, leading to a decrease in the binding of various growth factors, without any modification of its affinity to the inflammatory cytokines (Wu et al., 1998). By contrast, HOCl and TauCl may, in certain conditions, exert a deleterious stimulation of inflammatory processes. In the defense reaction against bacteria, numerous enzymes are released by leukocytes into the extracellular environment, a mechanism that appears to be essential in periodontitis. Metalloproteinases—including sulfur, magnesium, iron, zinc, or calcium-dependent endopeptidases, such as collagenases—are involved in such tissue damage.
2-macroglobulin-related neutralization of cell proteases, whereas both HOCl and TauCl inactivate the 1-proteinase inhibitor (Evans and Pryor, 1994; Wu et al., 1998). In summary, both HOCl and TauCl modulate the inflammatory response, often in a concentration-dependent manner. The anti-inflammatory effects would appear to predominate, but the outcome of these multiple affects in vivo requires further exploration. To date, no clinical trials have investigated the effects of a HOCl and TauCl combination in human or animal periodontal therapy.
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EFFECTS ON MEDIATOR PRODUCTION AND INTRACELLULAR SIGNAL TRANSDUCTION PATHWAYS |
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TOPABSTRACTINTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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, IL-6, IL-2, and INF-
production, and (ii) a defective synthesis of IL-4 and IL-10 (Górska et al., 2003). IL-1 and TNF- release results in an intensive recruitment of inflammatory cells with: (1) chemokine production, including MCP-1 and the MIP family; (2) activation of endothelial cell leukocyte adhesion molecules; and (3) stimulation of both adherent and non-adherent leukocytes. The result is a stimulation of PMN degranulation, ROS production, and MMP synthesis. Moreover, PGE2 production is activated. All these inflammatory molecules generate potentially harmful activity, resulting in connective tissue damage, alveolar bone resorption, and periodontal clinical attachment loss (Górska et al., 2003; Teng, 2003). Consequently, neutralization of this inflammatory cascade appears crucial to periodontal healing.
TauCl and HOCl inhibit in vitro the cell production of various inflammatory mediators and ROS (Table). TauCl significantly reduces the production of IL-1ß, IL-6, and IL-8 in LPS-stimulated human adherent monocytes, and also inhibits lymphocyte proliferation (Park et al., 2002). In LPS-stimulated murine peritoneal macrophages, TauCl may interfere with the transduction signals which generate MMP-9 expression (Park et al., 2000). TauCl-related inhibition of MCP-1, MIP-2, IL-1ß, IL-2, IL-6, IL-8, TNF-, nitric oxide (NO), and PGE2 production involves the nuclear factor kappa B (NF-B) and activator protein 1 (AP-1) transcriptional pathways (Fig. 2), leading to partial or complete inhibition (Kontny et al., 2003a; Liu et al., 2003).
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B and AP-1 are redox-sensitive transcription factors, whose control has been proposed as a potentially important host-modulation strategy in periodontitis (Chapple et al., 2002). The NF-B proteins are comprised of homo- and hetero-dimers belonging to the Re1 protein family. They are responsible for the transcription of many genes, including those regulating inflammation, acquired immunity, cell-to-cell interactions, cell apoptosis, and proliferation. The NF-B dimer is associated with an IB inhibitory protein, which masks its nuclear location signal site and maintains NF-B in its latent form within the cytoplasm. AP-1 is a two-gene-dependent transcription factor (Jun and Fos). The monomers (c-Jun, c-Fos, v-Jun, v-Fos, Fos, Fra-1, Fra-2, Jun-D, Jun-B, and ATF) can generate a homodimeric complex (Jun/Jun) or a heterodimeric complex (Jun/Fos). This transcription factor family is critical to the early genetic regulation of immune responses.
NF-B and AP-1 are stimulated by a specific mitogen-activated protein kinase (MAP-kinase) pathway. Cell receptors contain an extracellular binding site, a transmembrane domain, and a cytoplasmic domain, which exerts a catalytic kinase activity. Receptor-linked protein-tyrosine kinase activation induces a cascade of transduction signals, involving MAP-kinases. Briefly, the tyrosine residue phosphorylation of the membrane receptor indirectly induces the recruitment and activation of MAP-kinase-kinase kinases (MAPKK-kinases), mainly through tumor-necrosis-factor receptor-associated factor (TRAF) proteins. MAPKK-kinases are serine-threonine kinases. Their activation leads to phosphorylation and activation of MAPK-kinases, which in turn may phosphorylate critical threonine and tyrosine residues in MAP-kinases. MAP-kinases have the potential to phosphorylate other cytoplasmic proteins, which may activate transcription factors (like AP-1, NF-B, Stat3, Gadd153/CHOP, and the Smad family), inducing their translocation from the cytoplasm to the nucleus (Gopalakrishna and Jaken, 2000).
NF-B and AP-1 are activated by specific MAP-kinases, called, respectively, IB kinases (IKK) and c-Jun N-terminal kinase (JNK). Two IKK homologues can be distinguished: IKK- and IKK-ß. This inducible serine phosphorylation leads to a polyubiquitination of adjacent lysines, followed by a 26S proteasome-dependent degradation of IB, thus releasing NF-B, which translocates to the nucleus and binds to DNA. Similarly, for example, JNK phosphorylates c-Jun, following TNF--receptor stimulation, thereby inducing AP-1 activation (Appendix 3).
NF-B is known to regulate the production of numerous inflammatory mediators (such as IL-1, IL-1ß, IL-2, IL-6, TNF-, NO, PGE2, TGF-ß, and adhesion molecules) and an inhibitor of apoptosis proteins (IAP), whereas AP-1 regulates the production of some cytokines (e.g., IL-8) and MMPs. All these mediators and proteins are involved in periodontal diseases, and their physiological inhibition seems to be crucial to periodontal tissue turn-over, and to triggering the processes of regeneration (Górska et al., 2003; Teng, 2003). TauCl inhibited the NF-B-related transcription of inducible nitric oxide synthase (iNOS) and TNF- genes in a rat model of broncho-alveolar macrophages (Barua et al., 2001), and iNOS, cyclo-oxygenase-2 (COX2), TNF-, MCP-1, and MIP-2 genes in rat cortical astrocytes (Liu et al., 2003). TauCl reduced both the translocation and NF-B DNA-binding activities, and maintained cytoplasmic levels of unphosphorylated IB-, probably as a complex with NF-B (Quinn et al., 2003). The TauCl-induced inhibition of IB kinase (IKK) activity is suspected on an upstream key kinase or thioredoxin-dependent redox protein. By contrast, in human Jurkat T-cells, the TNF--stimulated luciferase gene expression is NF-B-controlled. TauCl reduces IKK activation at a downstream rather than an upstream level, in the kinase cascade. This TauCl-generated inhibition does not occur on serine 32/36 phosphorylation, but results from an oxidation of IB- methionine 45, yielding a sulfoxide residue. This oxidation is likely to induce a spatial structure change that masks serine 32/36, preventing phosphorylation, or avoids phosphorylated IB- recognition by F-box protein and subsequent lysine 21/22 ubiquitination (Kanayama et al., 2002).
The level of TauCl-inhibition for each above-mentioned mediator depends on NF-B involvement in its production. Furthermore, these data do not hide the existence of other TauCl-mediated inhibitory mechanisms. Thus, in HFLS, the inhibition of COX2 gene NF-B-transcription (IC50 ~ 400 µM) is less sensitive than post-transcriptional events (IC50 ~ 300 µM), suggesting that the main inhibition occurs at the post-transcriptional level (Kontny et al., 2003b). In the same way, TauCl essentially suppresses the translation of TNF- mRNA (Park et al., 2002). Therefore, TauCl has the ability to inhibit the production of the principal inflammatory mediators involved in the pathogenesis of periodontitis. These inhibitions may involve activity at the level of gene transcription, at the post-transcriptional stage, and/or at mRNA translation. Consequently, TauCl not only protects tissues against excess HOCl (an anti-oxidant effect), but also possesses anti-inflammatory properties.
Tissue-regenerative Activity
Cessation of tissue destruction, both by direct neutralization and by cell inhibition of pro-inflammatory mediators, could promote healing (Appendix 4). The induction of periodontal tissue regeneration is known to require an adequate production of cellular growth factors, such as insulin-like growth factor (IGF), epidermal growth factor (EGF), keratinocyte growth factor (KGF, also called FGF-7), FGF-1 and -2, TGF-ß, PDGF, vascular endothelium growth factor (VEGF), connective tissue growth factor (CTGF), and/or cementum-derived growth factor (CGF) (Grzesik and Narayanan, 2002). Protein tyrosine kinases and protein tyrosine phosphatases (PTPs) form complexes involving membrane receptors for certain growth factors, and receptors that regulate the synthesis of many inflammatory and regenerative molecules, including IGF-1, bFGF (FGF-2), EGF, NGF, and/or PDGF. In these complexes, PTPs negatively control phosphotyrosine protein kinases through a tyrosine phosphorylation inhibition. PTP activation involves the reduction of one specific thiol residue within the active site. All PTPs share a CXXXXXR active site motif (where C is a cysteine, R an arginine, and X any amino acid). In the low-molecular-weight phosphotyrosine-protein phosphatases (LMW-PTP), present in many mammalian tissues, cysteine-12 and cysteine-17 are conserved residues in the catalytic site. Oxidative stress induces the production of intracellular H2O2. H2O2-mediated oxidation inhibits LMW-PTP by producing a disulfide bond between cysteine-12 and cysteine-17 (Chiarugi et al., 2001). Similarly to H2O2, an oxidative action of other non-specific lipophilic oxidants, such as HOCl or NH2Cl, on these strategic thiol residues may be hypothesized (Fig. 2
). To date, there is no definitive demonstration of a HOCl-induced direct activation of receptor-tyrosine-kinases, although recent experimental results suggest its existence. In human B- and T-lymphocytes, HOCl induces (similarly to H2O2) a protein tyrosine phosphorylation and activates the zeta-associated protein-70 (ZAP-70) tyrosine kinase, generating a tyrosine-kinase-dependent calcium signaling. Furthermore, HOCl may bypass cell membrane receptors to stimulate intracellular protein tyrosine kinases and calcium signaling directly. In this case, cell receptor activation may prolong the HOCl-generated calcium signal. Activation of these directs intracellular transduction pathways and stimulates TNF- gene transcription in human peripheral blood mononuclear cells (Schieven et al., 2002). HOCl-mediated effects on calcium signaling pathways may, in turn, induce intracellular modifications, including HOCl calcium-dependent production (Blackburn and Chatham, 1994).
As mentioned above, the production of pro-inflammatory cytokines, growth factors, and extracellular matrix components requires the MAP-kinase-mediated activation of transcription factors, such as AP-1, NF-B, Stat3, Gadd153/CHOP, and the Smad family. Moreover, most of these factors bind to their specific membrane receptors and activate signal transduction pathways, which may involve MAP kinase activation (such as VEGF or PDGF). In contrast to H2O2, HOCl does not significantly activate JNK, except at a lethal dose (50 µM). The extremely low doses of HOCl required for MAP kinase activation (20–50 µM), compared with H2O2 (400–1000 µM), may result from the high reactivity of HOCl with thiol groups and not physiological enzymatic degradation. HOCl-induced MAP kinase activation may be due to a direct thiol residue substitution into sulfenic/disulfide and/or an intracellular redox-status change. These hypotheses require further investigation (Midwinter et al., 2001). Protein-kinase C may also activate MAP kinases. It possesses cysteine-rich regulation and catalytic domains. More precisely, the regulation domain possesses 4 crucial zinc fingers that allow for binding to membrane lipids. Each zinc finger contains 6 regulatory spaced cysteine residues that may generate a fold structure, leading to coordination between 2 zinc atoms. The zinc-thiolate structure is positively charged and is highly susceptible to negatively charged lipophilic oxidants, like hypochlorite. These oxidants induce the loss of zinc finger conformation, thereby activating protein-kinases-C through calcium- and phospholipid-independent pathways (Gopalakrishna and Jaken, 2000). However, since protein-kinases C are partially located inside the cell membrane, other negatively charged but hydrophilic agents, such as TauCl, are not active. Although not yet described, a synergistic effect between protein-kinase-C phosphorylation and oxidation has been suggested. Interestingly, the zinc finger structure is a crucial part of various other signaling proteins, including TRAF proteins, c-myc, Raf, some DNA-repair enzymes, transcription factors of the steroid-binding superfamily, and the transcription factor protein 53 (p53). This may explain their potential sensitivity to negatively charged oxidants.
HOCl is a non-specific lipophilic oxidant, has a rapid rate of cell-uptake, and preferentially oxidizes thiol residues. This redox activity is more powerful than H2O2. At toxic concentrations, HOCl generates a rapid and irreversible loss of intracellular protein-thiol groups, including glutathione, glutaredoxin, and thioredoxin, through an irreversible oxidative cross-linking and aggregation process (Pullar et al., 2001). Low HOCl levels oxidize preferentially accessible thiol residues and, more specifically, cysteine residues of vital cellular anti-oxidants, such as reduced glutathione, thioredoxin, and glutaredoxin. Thioredoxin expression modulates NF-B activity at 3 levels. In the nucleus, it helps NF-B to bind to DNA (Harper et al., 2001). In the cytosol, it activates NF-B at a downstream level of NIK (Hirota et al., 2000), while, near the cell membrane, it inhibits NF-B-mediated cytokine production, at an upstream level of NIK and at a downstream level of TRAFs (Takeuchi et al., 2000). In contrast, glutaredoxin expression increases NF-B activation and, as well as thioredoxin, increases AP-1 activation. HOCl may oxidize cytoplasmic anti-oxidants close to the cell membrane, and thus indirectly regulates these transcription factors. Moreover, non-specific oxidants, like H2O2 and HOCl, may modulate IB kinase activities, with the generation of an inducible phosphorylation on the tyrosine 42 residue instead of the serine 32/36 residues of IB-, resulting in an IB- dissociation from NF-B, without its degradation by the 26S proteasome (Janssen-Heininger et al., 2000).
Thus, although HOCl has the ability to inhibit the redox-sensitive transcription factors, similarly to TauCl, anti-oxidant-mediated HOCl neutralization prevents this activity in vivo. In fact, an HOCl-induced moderate depletion of anti-oxidants may favor the HOCl-mediated non-specific activation of protein tyrosine kinases, MAP kinases, and/or protein kinases C, which leads to non-specific pro-inflammatory gene transcription. Therefore, non-toxic HOCl concentrations induce cell proliferation and stimulate extracellular matrix component production in human fibroblasts (Hidalgo and Dominguez, 2000).
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CONCLUSION |
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TOPABSTRACTINTRODUCTIONCHLORINATION AND OXIDATION...EFFECTS ON ANTIGENS AND...EFFECTS ON MEDIATOR PRODUCTION...CONCLUSIONREFERENCES |
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2-macroglobulins; and (4) reduction of the binding of growth factors to 2-macroglobulins. However, differences exist between HOCl and TauCl activities. Extracellular HOCl stimulates membrane receptors and activates kinase cascades, leading to the production of native compounds of the extracellular matrix and/or cytokines (including growth factors and pro-inflammatory cytokines), whereas TauCl inhibits most of the production of pro-inflammatory cytokines and reactive oxygen species. The hydrogen peroxide/myeloperoxidase system generates HOCl and TauCl as end-products. Thus, a deficient production of both HOCl and TauCl may play a key role in the pathogenesis of periodontal diseases. Further investigation into the dynamic interactions of these 2 molecules—not only with each other, but also with components of the periodontal connective tissues and inflammatory-immune system—may lead to new opportunities for periodontal therapy, based upon the modulation of the host response in susceptible patients.
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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Received January 27, 2004; Last revision July 31, 2004; Accepted August 31, 2004
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