Brief communication (Original). Trefoil factor expression by immunohistochemistry in patients with oral lichen planus

Chaiyarit, Ponlatham; Klanrit, Poramate; Phothipakdee, Pensri; Subarnbhesaj, Ajiravudh; Thongprasom, Kobkan; Giraud, Andrew S.

doi:10.5372/1905-7415.0806.352

Cited by 5 publications

(5 citation statements)

References 29 publications

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“…The procedure of immunostaining was modified from previous studies by the present authors [28,29]. Briefly, all biopsy specimens were fixed in 10% neutral buffered formalin upon collection, embedded in paraffin wax, sectioned at 5-mm thicknesses and incubated in a hot-air oven at 60 8 C for 24 h. Deparaffinization of tissue specimens was performed.…”

Section: Immunohistochemical Methodsmentioning

confidence: 99%

New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus

Thi

Phoomak

Champattanachai

et al. 2018

Clinical and Experimental Immunology

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Oral lichen planus (OLP) is considered a chronic inflammatory immune-mediated disease of the oral mucosa. Immunopathogenesis of OLP is thought to be associated with cell-mediated immune dysregulation. O-GlcNAcylation is a form of reversible glycosylation. It has been demonstrated that O-GlcNAcylation promoted nuclear factor kappa B (NF-κB) signalling. Activation of NF-кB can induce expression of nucleotide-binding domain-like receptor family pyrin domain containing 3 (NLRP3) inflammasome, which is a large intracellular multi-protein complex involving an immune response. Dysregulated expression of the NLRP3 inflammasome was reported to be associated with autoinflammatory diseases. No integrative studies between O-GlcNAcylation and NLRP3 inflammasome in OLP patients have been reported. The present study aimed to determine the immunohistochemical expression of O-GlcNAcylation, NF-κB signalling molecules and NLRP3 inflammasome in oral mucosae of OLP patients. Oral tissue samples were collected from 30 OLP patients and 30 healthy individuals. Immunohistochemical staining and analyses of immunostaining scores were performed to evaluate expression of O-GlcNAcylation, NF-κB signalling molecules and NLRP3 inflammasome. According to observations in this study, significantly higher levels of O-GlcNAcylation, NF-κB signalling molecules and NLRP3 inflammasome were demonstrated in OLP patients compared with control subjects (P < 0·001). Positive correlations among O-GlcNAcylation, NF-κB signalling molecules and NLRP3 inflammasome were also observed in OLP samples (P < 0·01). In conclusion, the present study provides supportive evidence that increased O-GlcNAcylation is associated with increased expression of NLRP3 inflammasome via the NF-κB signalling pathway. These findings provide a new perspective on immunopathogenesis of OLP in relation to autoinflammation.

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Section: Immunohistochemical Methodsmentioning

confidence: 99%

New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus

Thi

Phoomak

Champattanachai

et al. 2018

Clinical and Experimental Immunology

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“…Furthermore, TFF3 (and also little TFF1 and TFF2) is synthesized in the oral mucosal epithelium [16,21]. Expression of TFF2 and TFF3 in oral mucosal tissue is downregulated in patients with oral squamous cell carcinoma and oral lichen planus [21,22]. Decreased salivary TFF3 levels were also observed in patients with obstructive sleep apnea and rhonchopathy [23].…”

Section: Trefoil Factor Family (Tff) Peptidesmentioning

confidence: 99%

Salivary Trefoil Factor Family (TFF) Peptides and Their Roles in Oral and Esophageal Protection: Therapeutic Potential

Hoffmann

2021

IJMS

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Human saliva is a complex body fluid with more than 3000 different identified proteins. Besides rheological and lubricating properties, saliva supports wound healing and acts as an antimicrobial barrier. TFF peptides are secreted from the mucous acini of the major and minor salivary glands and are typical constituents of normal saliva; TFF3 being the predominant peptide compared with TFF1 and TFF2. Only TFF3 is easily detectable by Western blotting. It occurs in two forms, a disulfide-linked homodimer (Mr: 13k) and a high-molecular-mass heterodimer with IgG Fc binding protein (FCGBP). TFF peptides are secretory lectins known for their protective effects in mucous epithelia; the TFF3 dimer probably has wound-healing properties due to its weak motogenic effect. There are multiple indications that FCGBP and TFF3-FCGBP play a key role in the innate immune defense of mucous epithelia. In addition, homodimeric TFF3 interacts in vitro with the salivary agglutinin DMBT1gp340. Here, the protective roles of TFF peptides, FCGBP, and DMBT1gp340 in saliva are discussed. TFF peptides are also used to reduce radiotherapy- or chemotherapy-induced oral mucositis. Thus, TFF peptides, FCGBP, and DMBT1gp340 are promising candidates for better formulations of artificial saliva, particularly improving wound healing and antimicrobial effects even in the esophagus.

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“…TFF3 is also detectable in parotid ducts [15]. Furthermore, TFF3 is expressed in the oral epithelium and the gingiva [13,16,17,18]. Of note, TFF3 is decreased in patients with chronic periodontitis, oral lichen planus, obstructive sleep apnea, and rhonchopathy [17,18,19].…”

Section: Introductionmentioning

confidence: 99%

Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)

Houben

Harder

Schlüter

et al. 2019

IJMS

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The peptide TFF3 is a member of a family of secretory lectins, and is typically synthesized by mucous epithelia together with mucins. It is mainly released from intestinal goblet cells as a high-molecular mass heterodimer with IgG Fc binding protein (FCGBP). Herein, we investigated human saliva by fast protein liquid chromatography (FPLC) and proteomics and identified high- and low-molecular-mass forms of TFF3. Whereas the high-molecular-mass forms represent a heterodimer with FCGBP, the low-molecular-mass forms represent homodimeric TFF3 forms. Proteomic analysis also revealed a C-terminally truncated form of TFF3. We hypothesize that salivary TFF3-FCGBP might play a role in the innate immune defense of the oral cavity and that TFF3 might also bind to microbial glycans. The known interaction of TFF3 with the agglutinin DMBT-1, a typical constituent of human saliva, further supports this protective role.

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Brief communication (Original). Trefoil factor expression by immunohistochemistry in patients with oral lichen planus

Cited by 5 publications

References 29 publications

New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus

New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus

Salivary Trefoil Factor Family (TFF) Peptides and Their Roles in Oral and Esophageal Protection: Therapeutic Potential

Different Forms of TFF3 in the Human Saliva: Heterodimerization with IgG Fc Binding Protein (FCGBP)

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