2014
DOI: 10.1080/09168451.2014.905190
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Thiol modification by bioactivated polyphenols and its potential role in skin inflammation

Abstract: In the present study, we evaluated the modifying behavior of simple phenolic compounds on the sulfhydryl groups of glutathione and proteins. The catechol-type polyphenols, including protocatechuic acid, but neither the monophenols nor O-methylated catechol, can modify the sulfhydryl groups in a phenol oxidase-dependent manner. The possible involvement of polyphenol bioactivation in the enhancement of skin inflammation was also suggested.

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Cited by 6 publications
(9 citation statements)
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“…Bioactivation to chemically reactive species is usually dependent on oxidative phase II biotransformation which is performed principally by cytochrome P-450 (CYP) enzymes. However, a non-specific CYP inhibitor SKF525A, even up to a dose of 20 mmol, did not counteract a PCA-induced modifying effect on inflammatory responses in mouse skin (Nakamura et al 2014). Drug bioactivation can also be catalyzed by non-CYP enzymes such as those found in neutrophils.…”
Section: -4 Discussionmentioning
confidence: 93%
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“…Bioactivation to chemically reactive species is usually dependent on oxidative phase II biotransformation which is performed principally by cytochrome P-450 (CYP) enzymes. However, a non-specific CYP inhibitor SKF525A, even up to a dose of 20 mmol, did not counteract a PCA-induced modifying effect on inflammatory responses in mouse skin (Nakamura et al 2014). Drug bioactivation can also be catalyzed by non-CYP enzymes such as those found in neutrophils.…”
Section: -4 Discussionmentioning
confidence: 93%
“…Addition of tyrosinase to PCA-treated cells also reduced GSH level to 72% of control (P < 0.001). In addition, PCA alone did not directly react with GSH whereas addition of tyrosinase resulted in formation a PCA-GSH adduct (Nakamura et al 2014).…”
Section: -3e Cytotoxic Effect Of Pca In Cultured Cells De-mentioning
confidence: 99%
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“…It is plausible that tyrosine is a mediator in the tyrosinase‐catalysed oxidation of sulphydryl groups in cysteine and glutathione. Bioactive phenols, which are substrates for tyrosinase diphenolase activity, were also suggested to cause glutathione oxidation in the presence of tyrosinase (Nakamura et al , ). This was supported by the observed reduction in glutathione levels.…”
Section: Resultsmentioning
confidence: 99%
“…All these formations are primarily associated with the induction of multiple biological responses associated with the activation of nuclear transcription factor kappa B (NF‐kappaB) and AP‐1 transcription factors, which regulate secretion of pro‐inflammatory cytokines, tumour necrosis factor alpha (TNF‐α), interleukin (IL‐1, IL‐6, IL‐8), thereby inducing skin inflammation. One of the main functions of polyphenols in the skin is the ability to inhibit pro‐inflammatory cytokines and enzymes activity, mainly iNOS (inducible nitric oxide synthase), NADPH oxidase (nicotinamide adenine dinucleotide phosphate‐oxidase) , COX‐1 (cyclooxygenase‐1), COX‐2 (cyclooxygenase‐2), 5‐LOX (arachidonate 5‐lipoxygenase) , 12‐LOX (12‐lipoxygenase), 15‐LOX (15‐lipoxygenase), phospholipase A2 (Yoon and Baek, ; Pastore et al , ; McClain and Watson, ; Nakamura et al ., ).…”
Section: Introductionmentioning
confidence: 99%