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FEBS Lett. 2012 Jul 30;586(16):2300-5. doi: 10.1016/j.febslet.2012.06.022. Epub 2012 Jun 23.

Dermokine-β impairs ERK signaling through direct binding to GRP78.

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1
Environmental Health Science Laboratory, Sumitomo Chemical Co., Ltd., Osaka 554-8558, Japan. higashik2@sc.sumitomo-chem.co.jp

Abstract

Dermokine-β is abundant in stratified epithelia and in differentiating cultured keratinocytes. In this study, we investigated the role of dermokine-β in differentiation of keratinocytes. Treatment of keratinocytes or skin tumor cells with dermokine-β attenuated phosphorylation of extracellular-signal-regulated kinase (ERK). Exposure of cells to dermokine-β, 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-β-associated protein. Blockage of GRP78 expression by a specific siRNA abrogated actions of dermokine-β. These findings provide novel insights into the physiological significance of dermokine-β in the epidermis.

PMID:
22735594
DOI:
10.1016/j.febslet.2012.06.022
[Indexed for MEDLINE]
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