Ligand‐specific and non‐specific in vivo modulation of human epidermal cellular retinoic acid binding protein (CRABP)

Ligand‐specific and non‐specific in vivo modulation of human epidermal cellular retinoic acid... Abstract. Retinoic acid (RA) is bound intracellularly by a specific, low molecular weight protein (CRABP), that is unrelated to its nuclear receptor and whose function and regulation are still unknown. In the present study we were able to obtain an in vivo modulation of CRABP by different stimuli in one of the major target organs of RA: the human skin. We found increased CRABP after daily application during 4 days of natural or synthetic retinoids (RA, acitretin, isotretinoin, Ro137410, retinol), that have either a high affinity to CRABP or can be transformed into RA. Only Ro150778 with no affinity and no reported transformation had no effect. No macro‐ or microscopical changes could be observed with any of the tested compounds. Induction of inflammatory and hyperproliferative changes in the skin by topical dithranol treatment, UVB irradiation or scotch tape stripping also induced a significant increase of CRABP 3 days after exposure. Topical diflucortolone showed not only a tendancy to decrease intrinsic CRABP levels, but significantly reduced the retinoid stimulated rise of CRABP. Thus we conclude that the increase of CRABP in a fully differentiated adult tissue seems to be a biological phenomenon following processes of inflammation and proliferation with a lag of several days, while retinoids seem to be able to induce such a rise independently of, or before, the appearance of such processes. Corticosteroids seem to be inhibitors of this reaction. We discuss the hypothesis that CRABP might function as an intracellular ‘buffer’ in the case of RA overload. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png European Journal of Clinical Investigation Wiley

Ligand‐specific and non‐specific in vivo modulation of human epidermal cellular retinoic acid binding protein (CRABP)

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Publisher
Wiley
Copyright
Copyright © 1989 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0014-2972
eISSN
1365-2362
DOI
10.1111/j.1365-2362.1989.tb00221.x
Publisher site
See Article on Publisher Site

Abstract

Abstract. Retinoic acid (RA) is bound intracellularly by a specific, low molecular weight protein (CRABP), that is unrelated to its nuclear receptor and whose function and regulation are still unknown. In the present study we were able to obtain an in vivo modulation of CRABP by different stimuli in one of the major target organs of RA: the human skin. We found increased CRABP after daily application during 4 days of natural or synthetic retinoids (RA, acitretin, isotretinoin, Ro137410, retinol), that have either a high affinity to CRABP or can be transformed into RA. Only Ro150778 with no affinity and no reported transformation had no effect. No macro‐ or microscopical changes could be observed with any of the tested compounds. Induction of inflammatory and hyperproliferative changes in the skin by topical dithranol treatment, UVB irradiation or scotch tape stripping also induced a significant increase of CRABP 3 days after exposure. Topical diflucortolone showed not only a tendancy to decrease intrinsic CRABP levels, but significantly reduced the retinoid stimulated rise of CRABP. Thus we conclude that the increase of CRABP in a fully differentiated adult tissue seems to be a biological phenomenon following processes of inflammation and proliferation with a lag of several days, while retinoids seem to be able to induce such a rise independently of, or before, the appearance of such processes. Corticosteroids seem to be inhibitors of this reaction. We discuss the hypothesis that CRABP might function as an intracellular ‘buffer’ in the case of RA overload.

Journal

European Journal of Clinical InvestigationWiley

Published: Apr 1, 1989

References

  • Effect of vitamin A status on retinoid‐binding protein levels in rat tissues
  • Interaction of the retinol/cellular retinol‐binding protein complex with isolated nuclei and nuclear components
    Liau, Liau; Ong, Ong; Chytil, Chytil
  • Quantitation and tissue localization of the cellular retinoic acid‐binding protein
    Eriksson, Eriksson; Hansson, Hansson; Nordlinder, Nordlinder; Busch, Busch; Sundelin, Sundelin; Peterson, Peterson
  • Basic questions on toxicology and pharmacology of anthralin
    Ippen, Ippen
  • Pharmacological studies of anthralin erythema
    Misch, Misch; Davies, Davies; Greaves, Greaves; Coutts, Coutts
  • Analyses of the interactions between retinoid‐binding proteins and embryonal carcinoma cells
    Barkai, Barkai; Sherman, Sherman

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