Uvb-irradiation induces phosphorylation of the 27-kda heat shock proto in in mouse kecatinocytes

S. Kobayashi, M. Sakamoto, J. Nozaki, M. Tanaka, M. Takehana

Research output: Contribution to journalArticlepeer-review


In the mouse ketatinocytes line Pam 212, the unphosphrylated 2 7-kDa heat shock protein (HSP27) isoform (pi 6.4) is constitutively expressed. Irradiat ion with ultraviolet B (UVB) osult s in the format ion of the phosphorylated HSP27 isoforms (pT 6.0) and the isoform level increases dose-dependently. The isoform can be Eliminated by the protein phosphatase 2A treamfiit . By prêtreatment with tumor necrosis factor alpha and okadaic acid, the level of the isoform increases 3 times that with irradiation only. These pretreated ketatinocytes are resistant aqa inst act in f ragp'entat ion by UVB-irradiation and shows an increase of translocation of HSP27 f rom the cytoplasm to the nucleus. These result suqqt'St that the phosphorylation of HSP27 may be related to the regulation of microfilament dynamies or apoptosis i'ol lowi ng irradiation stress.

Original languageEnglish
Pages (from-to)A1182
JournalFASEB Journal
Issue number9
Publication statusPublished - 1997 Dec 1

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Uvb-irradiation induces phosphorylation of the 27-kda heat shock proto in in mouse kecatinocytes'. Together they form a unique fingerprint.

Cite this