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- Title
Epidermal FABP (FABP5) Regulates Keratinocyte Differentiation by 13(S)-HODE-Mediated Activation of the NF-κB Signaling Pathway.
- Authors
Ogawa, Eisaku; Owada, Yuji; Ikawa, Shuntaro; Adachi, Yasuhiro; Egawa, Teie; Nemoto, Kei; Suzuki, Kaori; Hishinuma, Takanori; Kawashima, Hiroshi; Kondo, Hisatake; Muto, Masahiko; Aiba, Setsuya; Okuyama, Ryuhei
- Abstract
Fatty acid-binding proteins (FABPs) are postulated to serve as lipid shuttles that solubilize hydrophobic fatty acids and deliver them to appropriate intracellular sites. Epidermal FABP (E-FABP/FABP5) is predominantly expressed in keratinocytes and is overexpressed in the actively proliferating tissue characteristic of psoriasis and wound healing. In this study, we found decreased expression of the differentiation-specific proteins keratin 1, involucrin, and loricrin in E-FABP−/− keratinocytes relative to E-FABP+/+ keratinocytes. We also determined that incorporation of linoleic acid was significantly reduced in E-FABP−/− keratinocytes. Although linoleic acid did not directly affect keratinocyte differentiation, keratin 1 expression was induced by the linoleic acid derivative 13(S)-hydroxyoctadecadienoic acid (13(S)-HODE), and this induction was concomitant with increased NF-κB activity. In E-FABP−/− keratinocytes, the expression of 13(S)-HODE and the subsequent induction of NF-κB activity was lower than in wild-type keratinocytes. The reduction of linoleic acid in E-FABP−/− keratinocytes led to decreased cellular 13(S)-HODE content, resulting in decreased keratin 1 expression through downregulation of NF-κB activity. The regulation of fatty acid metabolism by E-FABP during keratinocyte differentiation suggests that E-FABP may have a role in the pathogenesis of psoriasis.
- Subjects
FATTY acid-binding proteins; KERATINOCYTES; ESSENTIAL fatty acids; LINOLEIC acid; MICROBIAL differentiation; PSORIASIS &; genetics
- Publication
Journal of Investigative Dermatology, 2011, Vol 131, Issue 3, p604
- ISSN
0022-202X
- Publication type
Article
- DOI
10.1038/jid.2010.342