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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2008.1
- 수록면
- 596 - 606 (11page)
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Heat shock protein 70 (HSP70), which evidences important
functions as a molecular chaperone and anti-
apoptotic molecule, is substantially induced in cells
exposed to a variety of stresses, including hypertonic
stress, heavy metals, heat shock, and oxidative stress,
and prevents cellular damage under these conditions.
However, the molecular mechanism underlying the induction
of HSP70 in response to hypertonicity has
been characterized to a far lesser extent. In this study,
we have investigated the cellular signaling pathway of
HSP70 induction under hypertonic conditions. Initially,
we applied a variety of kinase inhibitors to NIH3T3
cells that had been exposed to hypertonicity. The induction
of HSP70 was suppressed specifically by treatment
with protein kinase C (PKC) inhibitors (G̈ö6976
and GF109203X). As hypertonicity dramatically increased
the phosphorylation of PKCμ, we then evaluated
the role of PKCμ in hypertonicity-induced HSP70
expression and cell viability. The depletion of PKCμ
with siRNA or the inhibition of PKCμ activity with inhibitors
resulted in a reduction in HSP70 induction and
cell viability. Tonicity-responsive enhancer binding protein (TonEBP), a transcription factor for hypertonicity-
induced HSP70 expression, was translocated rapidly into the nucleus and was modified gradually in
the nucleus under hypertonic conditions. When we administered
treatment with PKC inhibitors, the mobility
shift of TonEBP was affected in the nucleus. However,
PKCμ evidenced no subcellular co-localization with
TonEBP during hypertonic exposure. From our results,
we have concluded that PKCμ performs a critical
function in hypertonicity-induced HSP70 induction,
and finally cellular protection, via the indirect regulation
of TonEBP modification.
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등록된 정보가 없습니다.
참고문헌 (22)
참고문헌 신청
Abe K / 1995 / Rapid and semiquantitative analysis of HSP72 and HSC73 heat shock mRNAs by mimic RT-PCR Brain / Res 683 : 251 ~ 3
Abravaya K / 1991 / Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in gr
Beere HM / 2000 / Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome / Nat Cell Biol 2 : 469 ~ 75
Dahl SC / 2001 / Hypertonicity-induced phosphorylation and nuclear localization of the transcription factor TonEBP / Am J Physiol Cell Physiol 280 : C248 ~ 53
Ferraris JD / 2002 / cAMP-independent role of PKA in tonicity-induced transactivation of tonicity-responsive enhancer/ osmotic response element-binding protein / Proc Natl Ac
Abravaya K / 1991 / Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in gr
Beere HM / 2000 / Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome / Nat Cell Biol 2 : 469 ~ 75
Dahl SC / 2001 / Hypertonicity-induced phosphorylation and nuclear localization of the transcription factor TonEBP / Am J Physiol Cell Physiol 280 : C248 ~ 53
Ferraris JD / 2002 / cAMP-independent role of PKA in tonicity-induced transactivation of tonicity-responsive enhancer/ osmotic response element-binding protein / Proc Natl Ac
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