HSP-72 synthesis is promoted by increase in [Ca2+]i or activation of G proteins but not pHi or cAMP

1994 ◽  
Vol 267 (1) ◽  
pp. C104-C114 ◽  
Author(s):  
J. G. Kiang ◽  
F. E. Carr ◽  
M. R. Burns ◽  
D. E. McClain

The family of 70-kDa heat-shock proteins (HSP-70) is evolutionarily highly conserved and has been shown to enhance cell survival from thermal injury. This study characterized HSP-72 induction in human epidermoid A-431 cells exposed to 45 degrees C for 10 min and determined the relationship between HSP-72, intracellular pH (pHi), adenosine 3',5'-cyclic monophosphate (cAMP), G proteins, and intracellular cytosolic free Ca2+ concentration ([Ca2+]i). Heat shock induced HSP-72 production, which was dependent on both temperature and the duration of heating. This HSP-72 induction was confirmed by Western blot analysis. HSP-72 levels in cells that had been heated then returned to 37 degrees C were elevated at 2 h (1.5 +/- 0.1 x control), reached a maximum at 8 h (2.7 +/- 0.1 x control), and remained above baseline for up to 4 days. Levels of HSP-72 mRNA, determined by dot-blot analysis, reached a maximum at 2 h and returned to baseline within 8 h. Both actinomycin D and cycloheximide blocked HSP-72 induction. Because heating causes intracellular acidification and increases in cAMP and [Ca2+]i, we studied the effect of pHi, cellular cAMP, and [Ca2+]i on HSP-72 induction. The reduction of pHi to 6.9 by acid loading did not affect the basal level of HSP-72 in unheated cells. Treatment with pertussis toxin, cholera toxin, or forskolin, but not 8-bromo-cAMP, 3-isobutyl-1-methylxanthine, or N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide potentiated heat-induced HSP-72 production. Inhibition of the heat-induced increase in [Ca2+]i attenuated, but failed to completely block, heat-induced HSP-72 production, mRNA synthesis, and the heat-shock transcriptional factor-heat-shock element binding complex formation, which suggests there are Ca(2+)-dependent and -independent processes involved in HSP-72 synthesis. Our results show that an increase in [Ca2+]i or activation of G proteins, but not pHi and cAMP, enhances HSP-72 induction.

2009 ◽  
Vol 1793 (11) ◽  
pp. 1738-1748 ◽  
Author(s):  
Natalia de Miguel ◽  
Nathalie Braun ◽  
Alexander Bepperling ◽  
Thomas Kriehuber ◽  
Andreas Kastenmüller ◽  
...  

Author(s):  
Arvindhan Nagarajan ◽  
Radoslav Janostiak ◽  
Narendra Wajapeyee

1994 ◽  
Vol 222 (1) ◽  
pp. 293-294 ◽  
Author(s):  
K.S. Saini ◽  
B. Bhandari

2011 ◽  
Vol 39 (12) ◽  
pp. e84-e84 ◽  
Author(s):  
M. Kimura ◽  
A. Aviv

Author(s):  
Bernadett Kalmar ◽  
Linda Greensmith

AbstractPharmacological up-regulation of heat shock proteins (hsps) rescues motoneurons from cell death in a mouse model of amyotrophic lateral sclerosis. However, the relationship between increased hsp expression and neuronal survival is not straightforward. Here we examined the effects of two pharmacological agents that induce the heat shock response via activation of HSF-1, on stressed primary motoneurons in culture. Although both arimoclomol and celastrol induced the expression of Hsp70, their effects on primary motoneurons in culture were significantly different. Whereas arimoclomol had survival-promoting effects, rescuing motoneurons from staurosporin and H2O2 induced apoptosis, celastrol not only failed to protect stressed motoneurons from apoptosis under same experimental conditions, but was neurotoxic and induced neuronal death. Immunostaining of celastrol-treated cultures for hsp70 and activated caspase-3 revealed that celastrol treatment activates both the heat shock response and the apoptotic cell death cascade. These results indicate that not all agents that activate the heat shock response will necessarily be neuroprotective.


Oncotarget ◽  
2017 ◽  
Vol 8 (35) ◽  
pp. 58553-58562 ◽  
Author(s):  
Geng Tian ◽  
Fangrong Tang ◽  
Chunhua Yang ◽  
Wenfeng Zhang ◽  
Jonas Bergquist ◽  
...  

1986 ◽  
Vol 102 (2) ◽  
pp. 353-361 ◽  
Author(s):  
J Mar ◽  
J H Lee ◽  
D Shea ◽  
C J Walsh

We have examined the nature of the requirement for RNA synthesis during the differentiation of Naegleria gruberi amebae into flagellates (Fulton, C., and C. Walsh, 1980, J. Cell Biol., 85:346-360) by looking for poly(A)+RNAs that are specific to differentiating cells. A cDNA library prepared from poly(A)+RNA extracted from cells 40 min after initiation of the differentiation (40-min RNA), the time when formation of flagella becomes insensitive to inhibitors of RNA synthesis, was cloned into pBR322. Recombinant clones were screened for sequences that were complementary to 40-min RNA but not to RNA from amebae (0-min RNA). Ten of these differentiation-specific (DS) plasmids were identified. The DS plasmids were found to represent at least four different poly(A)+RNAs based on cross-hybridization, restriction mapping, and Northern blot analysis. Dot blot analysis was used to quantify changes in DS RNA concentration. The four DS RNAs appeared coordinately during the differentiation. They were first detectable at 10-15 min after initiation, reached a peak at 70 min as flagella formed, and then declined to low levels by 120 min when flagella reached full length. The concentration of the DS RNAs was found to be at least 20-fold higher in cells at 70 min than in amebae. The changes in DS RNA concentration closely parallel changes in tubulin mRNA as measured by in vitro translation (Lai, E.Y., C. Walsh, D. Wardell, and C. Fulton, 1979, Cell, 17:867-878).


1993 ◽  
Vol 211 (2) ◽  
pp. 179-182 ◽  
Author(s):  
B. Canas ◽  
Z. Dai ◽  
H. Lackland ◽  
R. Poretz ◽  
S. Stein

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