title: Lysophospholipids improve skin moisturization by modulating of calcium-dependent cell differentiation pathway.
abstract: Recent studies have demonstrated that lysophospholipids (LPL) play critical roles in several biological signal transduction pathways to maintain the homoeostasis of cells, tissues and organs. Among them, lysophosphatidic acid (LPA) has been identified as a lipid mediator that induces morphological improvement in the epidermis in mice. In this study, we examined the effects of LPL (soybean-derived phospholipids modified with phospholipase A2 and C) compared with LPA. We initially examined the effects of LPA on normal human epidermal keratinocytes (NHEK) focusing on the expression of profilaggrin and serine palmitoyltransferase (SPT) mRNAs. LPA enhanced the expression of profilaggrin and SPT mRNAs via the modulation of Ca(2+) influx. Based on those results, the influence of LPL on NHEK was examined and was expanded to analyse the expression of two tight junction-related proteins, occludin and claudin-1. LPL had similar effects to increase profilaggrin and SPT mRNA expression and also stimulated the expression of occludin and claudin-1 at the mRNA and protein levels. In accordance with these results, LPL elicited significant improvements in surface water content in human skin. These findings indicate that LPL has the potential to strengthen the skin moisturizing capability by up-regulating the expression of mRNAs encoding components important to skin barrier function and skin hydration.
authors.affiliation: Nikkol Group Cosmos Technical Center Co, Ltd, 3-24-3 Hasune, Itabashi-ku, Tokyo 174-0046, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Yahagi
authors.forename: M
authors.initials: M
authors.lastname: Koike
authors.forename: Y
authors.initials: Y
authors.lastname: Okano
authors.forename: H
authors.initials: H
authors.lastname: Masaki
mesh_terms: D000328:Adult; D015153:Blotting, Western; D002118:Calcium / Q000378:metabolism*; D002454:Cell Differentiation / Q000187:drug effects* / Q000502:physiology; D062445:Claudin-1; D004311:Double-Blind Method; D000078404:Epidermal Cells; D004817:Epidermis / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D015603:Keratinocytes / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D008246:Lysophospholipids / Q000008:administration & dosage / Q000494:pharmacology*; D008297:Male; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics; D008858:Microscopy, Phase-Contrast; D008875:Middle Aged; D062793:Occludin; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D051102:Serine C-Palmitoyltransferase / Q000096:biosynthesis / Q000235:genetics; D012867:Skin / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism*; D015854:Up-Regulation
chemical_list: C568108:CLDN1 protein, human; D062445:Claudin-1; C568113:Cldn1 protein, mouse; D008246:Lysophospholipids; D008565:Membrane Proteins; C568985:OCLN protein, human; D062793:Occludin; C568986:Ocln protein, mouse; D012333:RNA, Messenger; D051102:Serine C-Palmitoyltransferase; D002118:Calcium