Annexin II, a novel HSP27-interacted protein, is involved in resistance to UVC-induced cell death in human APr-1 cells.
Heat shock protein 27 (HSP27) is implicated in diverse biologic functions as a molecular chaperone. We found that HSP27 is involved in the protection of human cells against UVC lethality. To elucidate the molecular mechanisms underlying UVC resistance, we searched for HSP27-interacted proteins related to resistance in UVC-resistant human cells, APr-1. Three candidates for HSP27-interacted proteins were found from cell lysates using an affinity column coupled with GST-fused HSP27 protein. Interaction between HSP27 and two candidates, annexin II and HSP70, was confirmed by immunoprecipitation analysis. After UVC irradiation, the amount of the complex of HSP27 and annexin II decreased in the postnuclear fraction, while it increased in the nuclear fraction. Cells transfected with annexin II-siRNA were more susceptible to UVC lethality. These results suggest that annexin II is a novel HSP27-interacted protein which is involved in UVC resistance in human cells, at least those tested here.
Tong
Xiao-Bo
XB
Department of Environmental Biochemistry, Graduate School of Medicine, Chiba University, Chiba, Japan.
Kita
Kazuko
K
Karata
Kiyonobu
K
Zhu
Chang-Lin
CL
Sugaya
Shigeru
S
Ichimura
Yoshinobu
Y
Satoh
Mamoru
M
Tomonaga
Takeshi
T
Nomura
Fumio
F
Jin
Yuan-Hu
YH
Suzuki
Nobuo
N
D017306:Annexin A2 / Q000378:metabolism*; D017209:Apoptosis / Q000528:radiation effects*; D002460:Cell Line; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013379:Substrate Specificity; D014466:Ultraviolet Rays
D017306:Annexin A2; D055551:HSP27 Heat-Shock Proteins