Variability of Enzyme Markers during Clinical Regression of Atopic Dermatitis

Tarroux, R.; Assalit, M.F.; Licu, D.; Périé, Jacques; Redoulès, Daniel

doi:10.1159/000049389

Cited by 19 publications

(17 citation statements)

References 17 publications

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“…This is associated with a disturbed skin-barrier function induced by several biological changes (1). These include the decrease in the size of corneocytes (2,3) alterations in stratum corneum ceramide content, the maturation of lipid-containing Odland bodies (4-9), perforin hyper-releasability (10) and the activity of proteases (11)(12)(13). The epidermal calcium ion gradient is also disturbed in AD (14), and in certain cases, alterations in the levels of Filaggrin; a key calcium-dependent protein in skin-barrier formation which may predispose subjects to the disease (15).…”

Section: Introductionmentioning

confidence: 99%

Calmodulin‐like skin protein level increases in the differentiated epidermal layers in atopic dermatitis

Donovan

Ambach

Thomas-Collignon

et al. 2013

Experimental Dermatology

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In atopic dermatitis (AD), the skin barrier is disturbed, and the expression of calcium-dependent S100 proteins and the calcium gradient is also altered in the epidermis. The calmodulinlike skin protein (CLSP), which is expressed in the differentiated epidermis, is believed to modulate the function of calciumdependent proteins involved in barrier formation and is significantly increased in the epidermis of psoriatic patients. We, therefore, investigated the CLSP level in skin biopsies taken from patients with acute exacerbated and non-exacerbated AD as well as from healthy control subjects. Immunohistochemical, Western blot and ELISA analyses showed significant increases (P < 0.03) in CLSP level in the epidermis from patients with acute exacerbated AD as compared to that from patients with non-exacerbated AD and from control subjects. Such increased expression of CLSP may help re-establish a functional epidermal barrier in acute AD.Abbreviations: AD, atopic dermatitis; CLSP, calmodulin-like skin protein; AEAD, acute exacerbated AD; NEAD, non-exacerbated AD.

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Section: Introductionmentioning

confidence: 99%

Calmodulin‐like skin protein level increases in the differentiated epidermal layers in atopic dermatitis

Donovan

Ambach

Thomas-Collignon

et al. 2013

Experimental Dermatology

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“…And the PTD group compared with the PSD group showed more irregular granular keratin in granular cells and immature keratin formation. It is well documented that ACP activity is increased in damaged tissues, [44][45][46] and ACP activity in PTD group was significantly higher than that of PSD group. Therefore, these results suggest that PPD skin toxicity in a tungstate supplemented diet is enhanced.…”

Section: Discussionmentioning

confidence: 83%

The Effects of Tungstate on Skin Lesions Caused by PPD in Rats

Lee¹,

Cho

S³

2008

Biological & Pharmaceutical Bulletin

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Red brownish p-phenylenediamine (PPD) has been widely used as one of the ingredients in hair dyes. The use by consumers of hair dye results in exposure of the hair, scalp skin, eyes, nail, and hands to PPD. PPD studies have found that women using dye with a formulation that included PPD suffered acute sensitive responses such as headaches, dizziness, and systemic anaphylaxis for the long time after using the product.1) And in patch tests, PPD caused erythema, rash, and a burning sensation on human skin. Furthermore, workers occupationally exposed to PPD in the field suffered from the bladder cancer.2,3) Previous studies have shown that PPD application induces injury to rat skin. 4,5) It is reported that PPD is metabolized to N-acetylated adducts as the major metabolites by N-acetyltransferase in human skin and liver, 6) and rats. 7) Moreover, it is reported that N-oxidation of arylamines like PPD occurs in the liver and is generally considered to involve cytochrome P450. 8) Furthermore, N-acetylated PPD metabolites are less toxic and they are excreted in urine.9) And, lipid peroxidation was increased while glutathione was decreased in skin by PPD application.5,10) In addition, PPD toxicity is increased by MnSOD polymorphism 11) while PPD toxicity is alleviated by thiol antioxidants.12) These reports suggest that production of ROS can be related to PPD skin toxicity. However, there are ongoing controversies whether PPD induced organ toxicity or whether it is safe in animal and clinical experiment. 13,14) It is well known that xenobiotic-induced tissue damage is related to reactive metabolites as well as produced reactive oxygen species (ROS) such as superoxide, hydroxyl radical, single oxygen and hydrogen peroxide under the metabolism. 15,16) Many studies have reported an imbalance between ROS generating systems and scavenging systems such as the increasing of ROS generating enzymes and/or decreasing of scavenging enzymes and nonenzymatic antioxidants. 17,18) It is accepted that xanthine oxidase (XO), one of the ROS generating systems, is increased in the injured cells.19) It has been revealed that inhibition of XO activity by allopurinol 20) or tungstate 21) alleviates experimental tissue damage. This indicates therefore a relationship of XO to skin cell injury, which suggests that the XO plays a role in the toxicity by the exposure of xenobiotics such as cosmetics and chemicals due to relatively higher XO activity in skin tissue compared with other tissues except liver and intestine. 19,22) It is reported that oxidized PPD, imine derivatives by hydrogen peroxide 23) could induce malignant and benign tumors in the mammary gland, uterus, and soft tissues of rats.24) Moreover, it is reported that XO could generate ROS such as superoxide and hydrogen peroxide.25,26) So, we hypothesized hydrogen peroxide derived from the XO system in skin involved with PPD oxidation and produced oxidized PPD is associated with dermal tissue damage.It is well established that sodium tungstate has relatively lower toxicity than that o...

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“…In AD patients, the levels and activities of epidermal proteases in samples of stratum corneum are elevated [26,27]. The balance between expression and activity of proteases and protease inhibitors determines the thickness of the barrier [28,29].…”

Section: Discussionmentioning

confidence: 99%