2018
DOI: 10.1111/jre.12561
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Peptidylarginine deiminase is involved in maintaining the cornified oral mucosa of rats

Abstract: Citrullination is likely a protein modification that plays an important role in maintaining the structure and function of oral cornified mucosa in a way that is distinctly different from that of the skin.

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Cited by 4 publications
(4 citation statements)
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“…Massive deimination of filaggrin is favorable to its complete proteolytic breakdown, leading to the production of free amino acid derivatives, a key process for the maintenance of tissue hydration [33]. We also identified a chemical activator of PADs, aceffyline, a xanthine derived from caffeine that promotes the deimination of filaggrin and consequently cornified epithelium hydration [100,101], as also observed by others [102]. Filaggrin is a basic protein that interacts with keratin IF in the upper epidermis to promote their aggregation [103].…”
Section: Deimination Of Ifap Impact On Their Proteolysissupporting
confidence: 63%
“…Massive deimination of filaggrin is favorable to its complete proteolytic breakdown, leading to the production of free amino acid derivatives, a key process for the maintenance of tissue hydration [33]. We also identified a chemical activator of PADs, aceffyline, a xanthine derived from caffeine that promotes the deimination of filaggrin and consequently cornified epithelium hydration [100,101], as also observed by others [102]. Filaggrin is a basic protein that interacts with keratin IF in the upper epidermis to promote their aggregation [103].…”
Section: Deimination Of Ifap Impact On Their Proteolysissupporting
confidence: 63%
“…With respect to the role of citrullination in the oral mucosa, Arita et al reported that PAD contributes to the integrity of the stratum corneum of the oral mucosa by citrullinating filaggrin and profilaggrin in the rat palate [ 32 ]. In addition to filaggrin, other citrullinated peptides with physiological roles include the glial cell fibrillary acidic protein [ 33 ], myelin basic protein [ 34 ], and histones [ 35 ].…”
Section: Discussionmentioning
confidence: 99%
“…Fifty percent inhibition of PADs using chloro-amidine, a pan-PAD inhibitor non-toxic for keratinocytes, partly reversed this consequence of dryness on keratinocyte metabolism [42]. Similarly, inhibition of PADs in an organotypic model, derived from rat palate keratinocytes reduced the breakdown of FLG and increased its association with keratins [43]. In this experimental model, activation of PADs with acefylline, a PAD1 and PAD3 activator [44], had the opposite effects.…”
Section: Pads and Deiminated Proteins In The Epidermismentioning
confidence: 92%