Retinoic acid receptors and binding proteins in human skin.

Abstract

Nuclear retinoic acid receptors (RAR) are likely to mediate many of the pleiotypic cutaneous actions of retinoids by acting as ligand-dependent enhancer factors. The presence of nuclear RAR in skin was confirmed by identification of a 45-kDa nuclear RA binding activity by fast protein liquid chromatography (FPLC). Analysis of RNA extracted from skin specimens demonstrated expression of RAR-alpha and RAR-gamma transcripts, as well as expression of the homologous low-affinity receptor, RXR-alpha. Both isoforms of RAR-gamma RAR-gamma 1 and RAR-gamma 2 were detectable, with RAR-gamma 1 being the more strongly expressed. FPLC analysis also demonstrated a 15-kDa peak of specific RA binding activity, consistent with the presence of cellular retinoic acid binding protein (CRABP). Of the two known forms of CRABP, CRABP-II was much more strongly expressed than CRABP-I at the level of steady-state mRNA. CRABP-II was also expressed in keratinocytes and fibroblasts in vitro. CRABP-II was up-regulated by agents that induce keratinocyte differentiation, and inhibited by prolonged exposure to high concentrations of RA. In contrast, CRABP-II was consistently induced by RA in dermal, but not in lung fibroblasts. CRABP-I was expressed at low to undetectable levels under all these conditions. The presence of tissue-specific and differentiation-related regulation of CRABP-II suggests that it may be an important regulator of RA action in human skin.

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@article{Elder1992RetinoicAR, title={Retinoic acid receptors and binding proteins in human skin.}, author={James T. Elder and Anders {\AA}str{\"{o}m and Ulf Pettersson and A Tavakkol and Andre Krust and Philippe Kastner and Pierre Chambon and John J . Voorhees}, journal={The Journal of investigative dermatology}, year={1992}, volume={98 6 Suppl}, pages={36S-41S} }