Ultraviolet B-mediated phosphorylation of the small heat shock protein HSP27 in human keratinocytes

Jon W. Wong, Biao Shi, Behnom Farboud, Marla McClaren, Takayuki Shibamoto, Carroll E Cross, Roslyn Rivkah Isseroff

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

Exposure of human keratinocytes to environmental stress is known to induce changes in the expression, phosphorylation, and subcellular relocalization of the 27 kDa heat shock protein. This study demonstrates that ultraviolet B (280-320 nM) irradiation with physiologic doses induces a dose-dependent phosphorylation of 27kDa heat shock protein, generating the more acidic 27 kDa heat shock protein B, C, and D isoforms. Ultraviolet B also induces perinuclear cytoplasmic relocation and nuclear translocation of 27 kDa heat shock protein and caused aggregation of cytoplasmic actin filaments into a broad perinuclear distribution. The ultraviolet B-induced phosphorylation is reversible, returning to baseline levels 4 h after exposure, and this coincides with the reversal of ultraviolet B-induced actin reorganization. The ultraviolet B-induced phosphorylation is not affected by the protein kinase C inhibitor, GF 109203X, is partially inhibited by epidermal growth factor receptor tyrosine kinase inhibitor. PD 153035, and is substantially inhibited by the specific p38 mitogen-activated protein kinase inhibitor, SB 203580. In addition, pretreatment of cells with the anti-oxidant N-acetyl cysteine partially inhibits ultraviolet B-and oxidant-induced 27 kDa heat shock protein phosphorylation. The p38 mitogen-activated protein kinase cascade is thus the major transduction pathway for ultraviolet B-induced 27 kDa heat shock protein phosphorylation, and reactive oxygen species generated in response to ultraviolet B also contribute to this phosphorylation. As 27 kDa heat shock protein phosphorylation and relocalization has been associated with increased cell survival after environmental insult, our data suggest that ultraviolet B, in addition to initiating recognized cytotoxic events in keratinocytes, also initiates a signaling pathway that may provide cellular protection against this ubiquitous environmental insult.

Original languageEnglish (US)
Pages (from-to)427-434
Number of pages8
JournalJournal of Investigative Dermatology
Volume115
Issue number3
DOIs
StatePublished - 2000

Fingerprint

Small Heat-Shock Proteins
Phosphorylation
Keratinocytes
Heat-Shock Proteins
HSP27 Heat-Shock Proteins
p38 Mitogen-Activated Protein Kinases
Protein Kinase Inhibitors
Oxidants
Dosimetry
Actins
Acetylcysteine
Cells
Relocation
Protein C Inhibitor
Protein C
Cytoskeleton
Actin Cytoskeleton
Epidermal Growth Factor Receptor
Protein-Tyrosine Kinases
Protein Kinase C

Keywords

  • 27kDa heat shock protein translocation
  • Actin filaments
  • Oxidative stress
  • P38 MAP kinase
  • Signal transduction

ASJC Scopus subject areas

  • Dermatology

Cite this

Ultraviolet B-mediated phosphorylation of the small heat shock protein HSP27 in human keratinocytes. / Wong, Jon W.; Shi, Biao; Farboud, Behnom; McClaren, Marla; Shibamoto, Takayuki; Cross, Carroll E; Isseroff, Roslyn Rivkah.

In: Journal of Investigative Dermatology, Vol. 115, No. 3, 2000, p. 427-434.

Research output: Contribution to journalArticle

Wong, Jon W. ; Shi, Biao ; Farboud, Behnom ; McClaren, Marla ; Shibamoto, Takayuki ; Cross, Carroll E ; Isseroff, Roslyn Rivkah. / Ultraviolet B-mediated phosphorylation of the small heat shock protein HSP27 in human keratinocytes. In: Journal of Investigative Dermatology. 2000 ; Vol. 115, No. 3. pp. 427-434.
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