TY - JOUR
T1 - Nuclear localization of propiece IL-1α in HeLa cells
AU - Kudo, Yoshihiro
AU - Tamagawa, Takaaki
AU - Nishio, Kensuke
AU - Kaneko, Tadayoshi
AU - Yonehara, Yoshiyuki
AU - Tsunoda, Mariko
N1 - Publisher Copyright:
© 2022, Nihon University, School of Dentistry. All rights reserved.
PY - 2022
Y1 - 2022
N2 - Purpose: The study aimed to examine the nuclear localization of propiece interleukin (IL)-1α (ppIL-1α) and extracellular release rates of ppIL-1α, pIL-1α, and mIL-1α. Methods: The subcellular localization of IL-1α molecules was observed in HeLa cells transfected with green fluorescent protein (GFP)-tagged IL-1α. Extracellular release efficiency was examined using N-terminal HiBiT-tagged IL-1α. The nuclear localization status of ppIL-1α was examined by incubating ppIL-1α transfectants with 0.1% Triton X-100 solution or with complete medium on ice. Results: The results indicated the diffuse cytoplasmic and nuclear localization for m and p and ppIL-1, respectively. All IL-1α forms were released from the cells even in the steady state, and the release efficiency was 25%, 13%, and 8% for mIL-1α, pIL-1α, and ppIL-1α, respectively. Under oxidative stress condition, GFP-mIL-1α was totally diminished, but weak staining of GFP-pIL-1α and GFP-ppIL-1α was detected; nuclear localization of GFP-ppIL-1α was completely abolished by 0.1% Triton X-100 treatment, however, it remained in the nucleus after culture in complete medium on ice. Conclusion: The results of this study showed that ppIL-1α was localized in the nucleus and released extracellularly even in the steady state. More-over, its cellular localization is not firm, and it is presumed to be floating in the nucleoplasm.
AB - Purpose: The study aimed to examine the nuclear localization of propiece interleukin (IL)-1α (ppIL-1α) and extracellular release rates of ppIL-1α, pIL-1α, and mIL-1α. Methods: The subcellular localization of IL-1α molecules was observed in HeLa cells transfected with green fluorescent protein (GFP)-tagged IL-1α. Extracellular release efficiency was examined using N-terminal HiBiT-tagged IL-1α. The nuclear localization status of ppIL-1α was examined by incubating ppIL-1α transfectants with 0.1% Triton X-100 solution or with complete medium on ice. Results: The results indicated the diffuse cytoplasmic and nuclear localization for m and p and ppIL-1, respectively. All IL-1α forms were released from the cells even in the steady state, and the release efficiency was 25%, 13%, and 8% for mIL-1α, pIL-1α, and ppIL-1α, respectively. Under oxidative stress condition, GFP-mIL-1α was totally diminished, but weak staining of GFP-pIL-1α and GFP-ppIL-1α was detected; nuclear localization of GFP-ppIL-1α was completely abolished by 0.1% Triton X-100 treatment, however, it remained in the nucleus after culture in complete medium on ice. Conclusion: The results of this study showed that ppIL-1α was localized in the nucleus and released extracellularly even in the steady state. More-over, its cellular localization is not firm, and it is presumed to be floating in the nucleoplasm.
KW - alarmin
KW - mature IL-1α (mIL-1α)
KW - nuclear localizing sequence (NLS)
KW - precursor IL-1α (pIL-1α)
KW - propiece IL-1α (ppIL-1α)
UR - http://www.scopus.com/inward/record.url?scp=85128161239&partnerID=8YFLogxK
U2 - 10.2334/josnusd.21-0540
DO - 10.2334/josnusd.21-0540
M3 - Article
C2 - 35236814
AN - SCOPUS:85128161239
SN - 1343-4934
VL - 64
SP - 151
EP - 155
JO - Journal of Oral Science
JF - Journal of Oral Science
IS - 2
ER -