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.
|Publication status||Published - 1997 Dec 1|
ASJC Scopus subject areas
- Molecular Biology