Inverse regulation of the nuclear factor-kappaB binding to the p53 and interleukin-8 kappaB response elements in lesional psoriatic skin

J Invest Dermatol. 2005 Jun;124(6):1284-92. doi: 10.1111/j.0022-202X.2005.23749.x.

Abstract

Nuclear factor-kappaB (NF-kappaB) is an inducible nuclear transcription factor regulating a range of cellular processes. An imbalance of the DNA binding activity of NF-kappaB may, therefore, be part of the pathophysiological mechanisms in psoriasis. The purpose of this study was to determine the NF-kappaB DNA binding activity in psoriatic skin using three different kappaB sites and to determine how DNA binding activity was modulated by the anti-psoriatic drug calcipotriol. By electrophoretic mobility shift assay, we demonstrated that the NF-kappaB DNA binding to the p53 kappaB site was decreased, whereas the NF-kappaB DNA binding to the interleukin-8 (IL-8) kappaB site was increased in lesional psoriatic skin compared with non-lesional psoriatic skin. No regulation was seen on the NF-kappaB DNA binding to the major histocompatibility complex class I kappaB site. These changes were paralleled by a similar decrease in p53 expression and an increase in IL-8 expression in involved psoriatic skin compared with uninvolved skin as determined by quantitative RT-PCR. The alteration in NF-kappaB DNA binding activity was neither accompanied by any change in the expression of the inhibitor kappaB (IkappaB) kinases, IKKalpha, IKKbeta, and IKKgamma nor in the expression of the NF-kappaB inhibitor proteins, IkappaBalpha and IkappaBbeta. Immunofluorescence analysis revealed that p65 was sequestered in the cytoplasm of keratinocytes, whereas p50 exhibited a cytoplasmic as well as a nuclear localization. Interestingly, this distribution of p50 and p65 was similar in lesional and non-lesional psoriatic skin. Topical application of calcipotriol to lesional psoriatic skin for 4 d resulted in increased NF-kappaB binding to the p53 kappaB site and decreased NF-kappaB binding to the IL-8 kappaB site. Taken together, our data demonstrate that the NF-kappaB DNA binding activity is regulated in a specific manner in psoriatic skin depending on the kappaB sites investigated, and that topical treatment of psoriatic skin normalizes the abnormal NF-kappaB binding activity seen in lesional psoriatic skin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Administration, Cutaneous
  • Adult
  • Blotting, Western
  • Calcitriol / administration & dosage
  • Calcitriol / analogs & derivatives*
  • Calcitriol / pharmacology*
  • Cells, Cultured
  • DNA / metabolism
  • Dermatologic Agents / administration & dosage
  • Dermatologic Agents / pharmacology*
  • Electrophoretic Mobility Shift Assay
  • Fluorescent Antibody Technique
  • Gene Expression Regulation / drug effects
  • Humans
  • I-kappa B Kinase
  • I-kappa B Proteins / metabolism
  • Interleukin-8 / genetics
  • Interleukin-8 / metabolism*
  • Keratinocytes / drug effects
  • Keratinocytes / metabolism
  • NF-kappa B / genetics
  • NF-kappa B / metabolism*
  • Protein Isoforms / metabolism
  • Protein Serine-Threonine Kinases / metabolism
  • Psoriasis / drug therapy
  • Psoriasis / metabolism*
  • Psoriasis / pathology
  • RNA, Messenger / metabolism
  • Response Elements
  • Reverse Transcriptase Polymerase Chain Reaction
  • Skin / metabolism*
  • Skin / pathology
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Dermatologic Agents
  • I-kappa B Proteins
  • Interleukin-8
  • NF-kappa B
  • Protein Isoforms
  • RNA, Messenger
  • Tumor Suppressor Protein p53
  • calcipotriene
  • DNA
  • Protein Serine-Threonine Kinases
  • CHUK protein, human
  • I-kappa B Kinase
  • IKBKB protein, human
  • IKBKE protein, human
  • Calcitriol