Altered expression of dermokine in skin disorders

Hasegawa, Minoru; Higashi, Kei; Yokoyama, Chikako; Yamamoto, Fernanda Paula; Tachibana, Taro; Matsushita, T.; Hamaguchi, Yasuhito; Saito, Koichi; Fujimoto, Manabu; Takehara, Kazuhiko

doi:10.1111/j.1468-3083.2012.04598.x

Cited by 20 publications

(30 citation statements)

References 26 publications

(64 reference statements)

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“…In a recent work, Hasegawa et al reported that Dmkn b and c are induced during early stages of wound healing in mice (Hasegawa et al, 2013b). We confirmed the induced expression of these Dmkn at day 3 post-wounding.…”

Section: Discussionsupporting

confidence: 77%

“…In the epidermis, DMKN b and c are secreted by the lamellar bodies and detected in the intercellular space between the granular and the cornified layers of normal human epidermis (Toulza et al, 2006). There is little data about DMKN expression in human diseases; DMKN b and c are overexpressed in inflammatory skin diseases, downregulated in skin cancers and, although hardly detected in normal colon epithelium, overexpressed in colorectal tumors (Hasegawa et al, 2013b;Tagi et al, 2010;Toulza et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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Mice deficient for the epidermal Dermokine β and γ display transient cornification defects

Leclerc

Huchenq

Kežić

et al. 2014

Journal of Cell Science

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Expression of the human dermokine gene (DMKN) leads to the production of four dermokine isoform families. The secreted a, b and c isoforms have an epidermis-restricted expression pattern, with Dmkn b and c being specifically expressed by the granular keratinocytes. The d isoforms are intracellular and ubiquitous. Here, we performed an in-depth characterization of Dmkn expression in mouse skin and found an expression pattern that was less complex than in humans. In particular, mRNA coding for the d family were absent. Homozygous mice null for the Dmkn b and c isoforms had no obvious phenotype but only a temporary scaly skin during the first week of life. The pups null for the Dmkn b and c isoforms had smaller keratohyalin granules and their cornified envelopes were more sensitive to mechanical stress. At the molecular level, amounts of profilaggrin and filaggrin monomers were reduced whereas amino acid components of the natural moisturizing factor were increased. In addition, the electrophoretic mobility of involucrin was modified, suggesting post-translational modifications. Finally, the mice null for the Dmkn b and c isoforms strongly overexpressed Dmkn a. These data are evocative of compensatory mechanisms relevant to the temporary phenotype. Overall, we improved the knowledge of Dmkn expression in mouse and highlighted a role for Dmkn b and c in cornification.

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Section: Discussionsupporting

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Mice deficient for the epidermal Dermokine β and γ display transient cornification defects

Leclerc

Huchenq

Kežić

et al. 2014

Journal of Cell Science

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“…Proinflammatory cytokines such as interleukin-1b, interleukin-12, and tumor necrosis factor-a augmented dermokine expression in cultured human keratinocytes. In contrast, growth factors including epidermal growth factor, insulin-like growth factor-I, keratinocyte growth factor, and transforming growth factor-a significantly reduced dermokine expression [9]. The present study was conducted to reveal the physiological significance of dermokine-b in the epidermis.…”

Section: Introductionmentioning

confidence: 99%

“…We have recently shown that the expression levels of dermokineb were increased in inflammatory skin disorders, while decreased in skin cancers [9]. Proinflammatory cytokines such as interleukin-1b, interleukin-12, and tumor necrosis factor-a augmented dermokine expression in cultured human keratinocytes.…”

Section: Introductionmentioning

confidence: 99%

Dermokine‐β impairs ERK signaling through direct binding to GRP78

et al. 2012

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a b s t r a c tDermokine-b is abundant in stratified epithelia and in differentiating cultured keratinocytes. In this study, we investigated the role of dermokine-b in differentiation of keratinocytes. Treatment of keratinocytes or skin tumor cells with dermokine-b attenuated phosphorylation of extracellularsignal-regulated kinase (ERK). Exposure of cells to dermokine-b, as well as its carboxyl-terminus domain peptide, interrupted phosphorylation of ERK and stimulated dermokine gene expression. Inhibition of ERK signaling by its specific inhibitor also increased dermokine expression level. A combination of chemical cross-linking and immunoprecipitation, followed by proteomics analyses, identified glucose-regulated protein 78 (GRP78) as a dermokine-b-associated protein. Blockage of GRP78 expression by a specific siRNA abrogated actions of dermokine-b. These findings provide novel insights into the physiological significance of dermokine-b in the epidermis.

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“…MMP10-dependent processing of DMKN is of particular interest, because DMKN expression in skin wounds spatially and temporally overlaps with increased levels of MMP10 in wound edge keratinocytes (4,(73)(74)(75). Moreover, recombinant DMKN inhibited ERK phosphorylation in cultured keratinocytes and delayed wound closure in mice (75,76).…”

Section: Discussionmentioning

confidence: 99%

Matrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates With Pleiotropic Functions*

Schlage

Kockmann

Sabino

et al. 2015

Molecular & Cellular Proteomics

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Altered expression of dermokine in skin disorders

Abstract: These results provide novel insights into the physiological and pathological significance of dermokine in the epidermis.

Cited by 20 publications

References 26 publications

Mice deficient for the epidermal Dermokine β and γ display transient cornification defects

Mice deficient for the epidermal Dermokine β and γ display transient cornification defects

Dermokine‐β impairs ERK signaling through direct binding to GRP78

Matrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates With Pleiotropic Functions*

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