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(Received for publication, March 14, 1997, and in revised form, April 17, 1997)
From the ABSTRACT Harmful conditions including heat shock,
oxidative stress, UV, and so forth cause programmed cell death, whose
triggering requires activation of the Jun N-terminal kinase, JNK. High
levels of Hsp72, a heat-inducible member of Hsp70 family, protect cells against a variety of stresses by a mechanism that is unclear at present. Here we report that elevated levels of Hsp72 inhibit a signal
transduction pathway leading to programmed cell death by preventing
stress-induced activation of JNK. Stress-induced activation of another
stress-kinase, p38 (HOG1), is also blocked when the level of Hsp72 is
increased. Similarly, addition of a purified recombinant Hsp72 to a
crude cell lysate reduced p38 kinase activation, while depletion of the
whole family of Hsp70 proteins with a monoclonal antibody enhanced such
activation. In addition, we have found that accumulation of abnormal
proteins in cells upon incubation with amino acid analogs causes
activation of JNK and p38 kinases, which can be prevented by
overproduction of Hsp72. Taken together, these data suggest that, in
regulation of JNK and p38 kinases, Hsp70 serves as a "sensor" of
the build-up of abnormal proteins after heat shock and other stresses.
The inhibitory effect of an increased level of Hsp70 on JNK appears to
be a major contributor to acquired thermotolerance in mammalian cells.
INTRODUCTION Exposure of mammalian cells to severe heat shock, strong oxidants,
UV irradiation, and other stressful conditions causes activation of a
family of homologous stress-activated protein kinases including JNK1 and p38 (1-3). This activation
proceeds through a signal transduction pathway that involves the small
GTP-binding proteins, MEK kinase, MEKK1, and dual-specificity kinases
MKK3, MKK4 (SEK1), and MKK6, which in turn phosphorylate and activate
JNK and p38 (4-8). JNK was recently shown to be an essential component
of a signal transduction pathway which leads to programmed cell death
in response to certain stimuli, including stressful conditions (9-12).
In fact, overproduction of a dominant negative mutant of JNK activating
kinase, SEK1, inhibits programmed cell death in response to heat shock,
UV irradiation, oxidative stress (9), and certain other inducers of
apoptosis (10-12).
Another protein, which when overproduced enhances cell survival
following exposure to a variety of stressful conditions, is Hsp72, a
heat-inducible member of Hsp70 family. Indeed, overproduction of Hsp72
either by expression under the regulation of a strong promoter on a
plasmid, or physiologically, by exposure of cells to a mild heat shock,
leads to a dramatic protection against severe heat shock, UV
irradiation, H2O2, and other harmful conditions and factors (13-16).
Members of the Hsp70 protein family function as molecular chaperones in
refolding of denatured polypeptides (17, 18). In fact, overproduction
of Hsp72 was shown to reduce stress-induced denaturation and
aggregation of certain proteins (19, 20) that has led to the common
assumption that refolding and antiaggregating activities of Hsp72
determine its role in cellular protection against stresses (21, 22).
However, under some conditions the protective action of Hsp72 appears
to be unrelated to its chaperoning activity. For example, tumor
necrosis factor (TNF) causes cell death by the activation of a signal
transduction pathway leading to apoptosis (23). This apoptotic process
can be prevented by overproduction of Hsp72 (24), which therefore seems
to interfere with the apoptotic program. Similarly TNF, exposure to
high temperatures, and some other stresses cause activation of the
apoptosis-triggering signal transduction pathways that include
activation of JNK (9-12). The protective action of Hsp72 in these
circumstances may also involve direct interference with the apoptotic
program. It should be noted, however, that upon exposure to extremely
high temperatures, when cell death is not due to apoptosis, but to
necrosis, the antiaggregating and protein refolding activities of Hsp72
may become critical for cell protection (20).
At what step can Hsp72 interfere with the apoptotic program? We
hypothesized that overproduction of Hsp72 inhibits activation of JNK by
harmful conditions. This idea was tested on the U937 leukemia cell
line, in which JNK activation appeared to be essential for the
activation of apoptosis by heat shock, UV, and oxidative stress (9),
and on the PEER lymphoid cell line, in which we overproduced Hsp72
under the control of tetracycline-regulated promotor.
EXPERIMENTAL PROCEDURES U937 and PEER human lymphoid tumor cells were
grown in RPMI 1640 medium with 10% (U937) or 20% (PEER) fetal bovine
serum and were used for experiments while in the mid-log phase
(3-7 × 105 cells/ml). PEER cells were stably
transfected with plasmids encoding Hsp72 under the control of a
tetracycline-regulated transactivator. Hsp72 was inserted as a first
cistron in a dicistronic expression vector that contains the green
fluorescent protein (GFP) gene. In this construct synthesis of Hsp72 is
repressed when grown in the presence of tetracycline, but removal of
this antibiotic leads to rapid and efficient induction of Hsp72. Cells
were incubated in the absence of tetracycline for 48 h in order to
induce expression of Hsp72 and GFP. Cells that express GFP were
selected with a cell sorter. These cells were viable and continued to
grow normally when tetracycline was added to repress Hsp72
synthesis.
2 × 107 PEER
cells were collected by centrifugation and washed once with
phosphate-buffered saline. Cells were resuspended in 0.4 ml of a
hypotonic buffer that contained 10 mM Hepes, 10 mM KCl, 1 mM dithiothreitol, 1 mM
phenylmethylsulfonyl fluoride, 0.2 mM EDTA (pH 7.4). After
15 min of swelling on ice, cells were disrupted on ice by 60 strokes in
Dounce homogenizer, and a 0.2 volume of a buffer containing 50 mM Hepes and 250 mM KCl (pH 7.4) was added.
Nuclei and cell debris were removed by centrifugation at 500 × g for 5 min at 4 °C, and the lysate was returned to ice. Typically cell lysates prepared by this procedure contained 4-7 mg/ml
protein.
For determination of cell viability, 0.5 mg/ml of MTT (Sigma) was added to 100 ml of cell suspension (0.5 × 106 cells/ml in 96-well plates) for 4 h, and the
formazan formed was dissolved in acidic 2-propanol; optical density was
measured using an enzyme-linked immunosorbent assay reader at 590 nm.
The OD of formazan formed by control (untreated) cells was taken as 100%. PARP degradation was determined by Western blotting with anti-PARP polyclonal antibodies.
JNK was assayed using glutathione
S-transferase-c-Jun protein as a substrate either in an
in-gel assay or after immunoprecipitation with anti-JNK antibodies
(Santa Cruz Biotechnology) as described previously (25). p38 kinase
activity was determined by Western blotting with polyclonal antibodies
(New England Biolabs) specifically reacting with the phosphorylated
(active) form of p38.
RESULTS AND DISCUSSION We first investigated the effect of enhanced levels of Hsp72 on
activation of stress kinase and apoptosis in U937 cells. To raise the
level of Hsp72, U937 cells were subjected to a mild heat shock (20 min
at 43 °C), followed by a 6-h recovery. Such mild heat shock caused
only a weak transient activation of JNK and did not activate an
apoptotic program (not shown). The second, severe, heat shock (60 min
at 43 °C) was applied, and it caused death of about 70% of the cell
population (Fig. 1A), as measured by the MTT
assay (ability of cells' mitochondria to reduce tetrazolium salts) or
by counting the number of surviving cells (not shown). Pretreatment
with the mild heat shock (preheating) reduced cell death after the
second heat shock by more than 90% (Fig. 1A). Cell death
was preceded by an extensive cleavage of PARP (Fig. 1B) and
nuclear condensation (not shown), thus indicating that it was of an
apoptotic, rather than of a necrotic, nature. Both the PARP cleavage
(Fig. 1B) and the nuclear condensation were strongly
inhibited in the preheated cells.
Preheating of cells also led to almost complete inhibition of
activation of JNK in response to the second challenge with heat shock
(Fig. 1C). While JNK became activated 30 min following the heat shock and maintained its activity for 4 h, in preheated cells JNK activity was practically undetectable at any point during this time
period (not shown). It is noteworthy that activation of another
stress-activated kinase, p38, was also inhibited under these conditions
by more than 70% (Fig. 1D). This kinase was shown to
participate in induction of IL-6, activation of phospholipase A2, regulation of phosphorylation of Hsp27, and other
processes (26-30). Preheating of cells also strongly reduced
activation of JNK and p38 kinases in response to another stress, a
challenge with 9% ethanol (Fig. 1, C and D), and
inhibited ethanol-induced apoptosis (Fig. 1, A and
B). Since inactivation of JNK by overexpression of a
dominant negative mutant of the upstream kinase was previously shown to
protect cells against heat shock and some other stresses (9), we
conclude that the protective action of the mild heat shock is
associated with an suppression of the JNK activation. Thus, prevention
of activation of JNK in preheated cells may be a significant factor in
the phenomenon of acquired thermotolerance and tolerance to ethanol.
These data complement the recent observation that JNK activation in
response to mild heat shock is strongly reduced in a stable
thermoresistant cell line (31) that overproduced the whole set of heat
shock proteins including Hsp72 (32).
Since the protective effects of the mild heat shock may be associated
not only with Hsp72 but also with some other heat-inducible polypeptides, we also studied the effects of stresses on a stably transfected PEER cell line that overexpresses Hsp72 under control of a
tetracycline-regulated transactivator. We first reproduced the effects
of mild heat shock on this cell line, i.e. demonstrated that
preheating of the cells in the presence of tetracycline (without expression of Hsp72 from a plasmid) protects against heat shock and
ethanol treatments and reduces activation of JNK and p38 (Fig. 1,
C and D). To study the effect of Hsp72 produced
from the plasmid under normal conditions, without mild heat shock (Fig.
2A), cells were incubated in the absence of
tetracycline for 24 h, followed by selection of cells containing
elevated levels of Hsp72 (see "Experimental Procedures"). In these
cells the level of Hsp72 was about 3-4 times higher than that of PEER
cells after the mild heat shock (not shown) and was similar to the
level of Hsp72 in U937 cells following the mild heat shock. The
selected cells with elevated levels of Hsp72 were challenged with a
severe heat shock (60 min at 43 °C) or 9% ethanol. Activation of
both JNK and p38 kinases was strongly inhibited in these cells compared
with the cells with the normal level of Hsp72 grown in the presence of tetracycline (Fig. 2, B and C). A strong
protection against apoptosis upon heat shock and ethanol treatments was
also observed in the Hsp72 overproducing cells (Fig.
2D).
These results support the hypothesis that Hsp72, when overproduced,
inhibits activation of JNK and p38 kinases and thus suppresses cell
suicide. It should be mentioned that, in the stably transfected cells
that chronically overexpress Hsp72 (13), we observed protection from
apoptosis without inhibition of JNK
activity.2,3 Therefore, it
is possible that another mechanism of prevention of apoptosis that does
not involve inhibition of JNK operates in cell lines that chronically
overexpress Hsp72. On the other hand, the effect described here of the
regulated acute overexpression of Hsp72 from the plasmid is identical
to that of elevated levels of Hsp72 induced by the mild heat shock,
indicating the physiological relevance of the observed phenomenon.
It is noteworthy that the regulated overexpression of Hsp72 in the PEER
cell line not only suppressed the responses to heat shock and ethanol
but also strongly inhibited activation of both JNK (not shown) and p38
(Fig. 2E) kinases caused by some other stresses, for
example, osmotic shock, H2O2, and UV
irradiation. Therefore, an elevated level of Hsp72 appears to interfere
with transduction of signals from a variety of stressful conditions. Moreover, accumulation of Hsp72 strongly reduced activation of stress-induced kinases in response to TNF and
IL-1,4 which is consistent with recent
findings that the response of JNK (and potentially of p38 kinase) to UV
and osmotic shock is mediated by the activation of TNF, IL-1, and
epidermal growth factor receptors (33).
Does a high level of Hsp72 directly affect activation of JNK and p38
kinases or does it through induction or repression of synthesis of some
other proteins? To address this question, effects of addition of a
purified recombinant Hsp72 on the activation of p38 kinase in cell
lysate were studied. In a crude lysate p38 kinase becomes activated
upon incubation at 20 °C for 15 min (Fig. 3A). Under exposure of the lysate to
43 °C, p38 kinase was activated even further (Fig. 3B).
No additional p38 activation was observed in the lysates subjected to
UV irradiation (Fig. 3B). Addition of purified Hsp72 (but
not bovine serum albumin, not shown) repressed the activation by about
40-70% (Fig. 3A). Importantly, the addition of a
monoclonal anti-Hsp70 antibody (MA3-007, Affinity Bioreagents) raised
against the conserved ATPase domain, which cross-reacts with all major
species of Hsp70, had an effect opposite to that triggered by the
addition of Hsp72. It led to a 1.5-3-fold stimulation of p38 kinase
activity (Fig. 3B). Addition of control monoclonal anti-
Experiments with activation of p38 kinase in a cell lysate by addition
of anti-Hsp70 antibody suggested that depletion or just capturing of
Hsp70 may result in activation of stress kinases in cells. Members of
the Hsp70 family bind misfolded polypeptides and therefore could be
captured upon a build-up of abnormal misfolded proteins in the cytosol.
Therefore, to test whether accumulation of abnormal proteins cause
activation of stress kinases, cells were incubated with amino acid
analogs, which incorporate into newly synthesized polypeptides and
prevent their proper folding. In fact, incubation of cells with the
proline analog, L-azetidine carboxylate, as well as with
the arginine analog, canavanine, stimulated both JNK and p38 kinases,
and the overproduction of Hsp72 strongly reduced such activation (Fig.
4, A and B). A similar stimulation
of stress-activated kinases was observed upon incubation of the cells
with puromycin, which causes an accumulation of truncated and therefore
improperly folded N-terminal fragments of proteins (not shown).
Therefore, build-up of abnormal proteins activates stress kinase, while
Hsp72 and probably other members of Hsp70 family suppress such
activation.
These data suggest a mechanism of activation of stress kinases by heat
shock and some other stressful conditions. Such stresses may cause
protein damage and denaturation and may lead to a build-up of abnormal
proteins. In turn these abnormal proteins deplete free Hsp70, which
leads to activation of stress-activated kinases (Fig.
5). The role of Hsp70 in the activation of stress
kinases may be analogous to its role in activation of heat shock gene transcription (34, 35). Accordingly, we suggest that in unstressed cells Hsp70 associates with an upstream component of the kinase cascade
and keeps it in an inactive form. Depletion of a free cellular Hsp70 by
accumulated abnormal proteins after heat shock (21, 22) would cause
dissociation of the bound Hsp70 from the upstream component of the
kinase cascade, thus leading to activation of downstream kinases.
Therefore, Hsp70 may function as a "stress sensor" that triggers
not only transcription of the heat shock genes but also activation of
stress kinases.
The results described in this report may also explain why
overproduction of Hsp72 prevents activation of the phospholipase A2 by TNF (36) and prevents induction of synthesis of IL-6
by IL-1 (15). Indeed, Hsp72 may simply prevent activation by TNF or
IL-1 of the p38 kinase, which was shown to activate the phospholipase A2 (27) and which is responsible for IL-6 induction (26). In summary, Hsp70 seems to play a very general role in signal transduction pathways, which lead to adaptation of cells and organisms to stressful conditions.
FOOTNOTES ACKNOWLEDGEMENTS We thank Dr. Vladimir Volloch and Dr. Alfred
Goldberg for helpful discussion.
REFERENCES
Volume 272, Number 29,
Issue of July 18, 1997
pp. 18033-18037
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A NOVEL PATHWAY OF CELLULAR THERMOTOLERANCE*
§¶,¶,
,,,
Boston Biomedical Research Institute,
Boston, Massachusetts 02114, the § Medical Radiology
Research Center, 249020 Obninsk, Russia, 
Biotechnology Research
Institute, Montreal H4P 2R2, Quebec, Canada, and the ** Dana Farber
Cancer Institute, Boston, Massachusetts 02115
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS AND DISCUSSION
FOOTNOTES
ACKNOWLEDGEMENTS
REFERENCES
Fig. 1.
Preexposure of cells to a mild heat shock
protects them from apoptosis and inhibits activation of JNK and p38
kinase by high temperature or ethanol treatments. A, effects
of preexposure to mild heat shock on cell viability. U937 and PEER
cells were exposed for 20 min at 43 °C followed by 6 h of
recovery (a time period that allows an accumulation of Hsp72, not
shown). Then the cells were subjected to a severe heat shock
(HS, 30 or 60 min at 43 °C) or to 9% ethanol
(ET) for 60 min. Cell were allowed to undergo apoptosis at
37 °C for the next 14 h, and their viability was measured by
the MTT assay. B, effects of preexposure to mild heat shock
on PARP cleavage. Cells were treated as in A, but instead of
measuring mitochondrial respiration by the MTT assay, PARP cleavage was
tested by Western blot with the anti-PARP antibody. C,
control; HS, heat shock 60 min; ET, ethanol 9%,
60 min. C, effects of preexposure to mild heat shock on the
activation of JNK by the second challenging stress. Cells were treated
as in A, but after 60 min of the second challenging stress
samples were taken, and JNK activity was tested by an in-gel assay.
D, effects of preexposure to mild heat shock on the
activation of p38 kinase by the second challenging stress. Cells were
treated as in A, but after 60 min of the second challenging
stress, samples were taken, and the amount of active p38 kinase was
measured as described under "Experimental Procedures."
[View Larger Version of this Image (29K GIF file)]
Fig. 2.
Overexpression of Hsp72 in PEER cells
inhibits activation of JNK and p38 kinase by a number of stressful
stimuli. A, the level of Hsp72 in the cells incubated
without tetracycline for 48 h was measured by a Western blot with
anti-Hsp72 antibody. B, JNK activity in cells overexpressing
Hsp72 and control cells after heat shock (43 °C). JNK activity was
measured after immunoprecipitation with anti-JNK antibodies. Cells that
express tetracycline-regulated transactivator (tTA) were
used as a control. C, activity p38 kinase in Hsp72
overexpressing cells after treatments with different stressful stimuli
(heat shock, 43 °C; 9% ethanol; 0.4 M sorbitol; 1 mM H2O2; UV-C, 500 J/m2). D and E, effects of Hsp72
overexpression on apoptosis after treatments with heat shock (43 °C)
or 9% ethanol measured by the MTT assay (D) and PARP
cleavage (E).
[View Larger Version of this Image (17K GIF file)]
-galactosidase antibody did not cause activation of p38 (not
shown). These data indicate that the level of Hsp70 in a cell may
directly regulate stress-activated kinases. The observed variability in
the extent of stimulation of p38 by MA3-007 antibody may be due to the
presence of endogenous ADP. Indeed, addition of ADP strongly reduced
the stimulatory effect of the anti-Hsp70 antibody (not shown).
Fig. 3.
Effects of Hsp72 on activation of p38 kinase
in cell lysate. A, effect of purified Hsp72 on the
activation of p38 kinase in cell lysate. Ten µl of lysate were placed
in the test tubes and incubated at 23 °C for 15 min in the presence
or absence of purified Hsp72 (added at amounts of 5% of total
protein). An ATP-regenerating system (20 mM creatine
phosphate, 2 mM ATP, 5 IU of creatine phosphate kinase) was
present in all samples. The reaction was stopped by addition of
Laemmli sample buffer. 0, no incubation at
23 °C, i.e. Laemmli buffer was added to lysate kept on
ice. B, effects of anti-Hsp72 antibody, incubation at high
temperature, and under UV irradiation on the activation of p38 kinase
in cell lysate. C0, no incubation at 23 °C;
AB, lysate was preincubated for 10 min on ice with
monoclonal anti-Hsp70 antibody that cross-reacts with all major species
of the Hsp70 family (Affinity Bioreagents no. MA3-007) and then, after
addition of the ATP-regenerating system, was transferred to 23 °C
for 15 min; HS, lysate was incubated for 15 min at 43 °C;
UV, lysate was irradiated with 500 J/m2 of UV-C
and then was incubated at 23 °C for 15 min; C1, lysate was incubated at 23 °C for 15 min without any treatments.
[View Larger Version of this Image (28K GIF file)]
Fig. 4.
Amino acid analogs cause an activation of JNK
and p38 kinases. A, PEER control cells and cells that
overexpress Hsp72 were transferred to the media without either arginine
or proline, and 10 mM of canavanine (Can) or
L-azetidine carboxylate (Azc) were added. The
activity of p38 kinase was tested after 2 h of incubation.
B, U937 control and preheated cells (as in Fig. 1) were
treated with 10 mM of Azc or heat-shocked (HS,
30 min), and JNK activity was tested after immunoprecipitation with
anti-JNK antibodies.
[View Larger Version of this Image (24K GIF file)]
Fig. 5.
Proposed role of Hsp70 in modulation of
stress kinase activity. Various proteotoxic conditions cause
depletion of free Hsp70 that leads to activation of stress kinase. In
thermotolerant cells (with high level of Hsp70) such activation is
prevented, thus blocking apoptosis and other
kinase-dependent events.
[View Larger Version of this Image (17K GIF file)]
¶
Contributed equally to this study.
To whom correspondence should be addressed: Boston Biomedical
Research Institute, 20 Stanford St., Boston, MA 02114. Tel.: 617-742-2010 (ext. 312); Fax: 617-523-6649; E-mail:
sherman{at}bbri.harvard.edu.
1
The abbreviations used are: JNK, Jun N-terminal
kinase; MTT, 3-[4,5-dimethylthiasol-2-yl]-2,5-diphenyltetrasolium
bromide; PARP, poly(ADP-ribose) polymerase; TNF, tumor necrosis factor; GFP, green fluorescent protein; IL, interleukin.
2
D. D. Mosser, submitted for publication.
3
S. Rits, unpublished data.
4
V. L. Gabai, manuscript in preparation.
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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R. Steel, J. P. Doherty, K. Buzzard, N. Clemons, C. J. Hawkins, and R. L. Anderson Hsp72 Inhibits Apoptosis Upstream of the Mitochondria and Not through Interactions with Apaf-1 J. Biol. Chem., December 3, 2004; 279(49): 51490 - 51499. [Abstract] [Full Text] [PDF]
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M. Zhao, A. Wimmer, K. Trieu, R. G. DiScipio, and I. U. Schraufstatter Arrestin Regulates MAPK Activation and Prevents NADPH Oxidase-dependent Death of Cells Expressing CXCR2 J. Biol. Chem., November 19, 2004; 279(47): 49259 - 49267. [Abstract] [Full Text] [PDF]
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 H. M. Beere `The stress of dying': the role of heat shock proteins in the regulation of apoptosis J. Cell Sci., June 1, 2004; 117(13): 2641 - 2651. [Abstract] [Full Text] [PDF]
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 K. Kojima, M. W. Musch, M. J. Ropeleski, D. L. Boone, A. Ma, and E. B. Chang Escherichia coli LPS induces heat shock protein 25 in intestinal epithelial cells through MAP kinase activation Am J Physiol Gastrointest Liver Physiol, April 1, 2004; 286(4): G645 - G652. [Abstract] [Full Text] [PDF]
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L. Doerwald, C. Onnekink, S. T. van Genesen, W. W. de Jong, and N. H. Lubsen Translational Thermotolerance Provided by Small Heat Shock Proteins Is Limited to Cap-dependent Initiation and Inhibited by 2-Aminopurine J. Biol. Chem., December 12, 2003; 278(50): 49743 - 49750. [Abstract] [Full Text] [PDF]
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 K. Ruchalski, H. Mao, S. K. Singh, Y. Wang, D. D. Mosser, F. Li, J. H. Schwartz, and S. C. Borkan HSP72 inhibits apoptosis-inducing factor release in ATP-depleted renal epithelial cells Am J Physiol Cell Physiol, December 1, 2003; 285(6): C1483 - C1493. [Abstract] [Full Text] [PDF]
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 Z. Batulan, G. A. Shinder, S. Minotti, B. P. He, M. M. Doroudchi, J. Nalbantoglu, M. J. Strong, and H. D. Durham High Threshold for Induction of the Stress Response in Motor Neurons Is Associated with Failure to Activate HSF1 J. Neurosci., July 2, 2003; 23(13): 5789 - 5798. [Abstract] [Full Text] [PDF]
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J. Yaglom, C. O'Callaghan-Sunol, V. Gabai, and M. Y. Sherman Inactivation of Dual-Specificity Phosphatases Is Involved in the Regulation of Extracellular Signal-Regulated Kinases by Heat Shock and Hsp72 Mol. Cell. Biol., June 1, 2003; 23(11): 3813 - 3824. [Abstract] [Full Text] [PDF]
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K. Merienne, D. Helmlinger, G. R. Perkin, D. Devys, and Y. Trottier Polyglutamine Expansion Induces a Protein-damaging Stress Connecting Heat Shock Protein 70 to the JNK Pathway J. Biol. Chem., May 2, 2003; 278(19): 16957 - 16967. [Abstract] [Full Text] [PDF]
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 L. D. Kaplan, C. R. Chu, J. P. Bradley, F. H. Fu, and R. K. Studer Recovery of Chondrocyte Metabolic Activity after Thermal Exposure Am. J. Sports Med., May 1, 2003; 31(3): 392 - 398. [Abstract] [Full Text] [PDF]
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 B. C. Santos, J. M. Pullman, A. Chevaile, W. J. Welch, and S. R. Gullans Chronic hyperosmolarity mediates constitutive expression of molecular chaperones and resistance to injury Am J Physiol Renal Physiol, March 1, 2003; 284(3): F564 - F574. [Abstract] [Full Text] [PDF]
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M.-K. Kwak, N. Wakabayashi, K. Itoh, H. Motohashi, M. Yamamoto, and T. W. Kensler Modulation of Gene Expression by Cancer Chemopreventive Dithiolethiones through the Keap1-Nrf2 Pathway. IDENTIFICATION OF NOVEL GENE CLUSTERS FOR CELL SURVIVAL J. Biol. Chem., February 28, 2003; 278(10): 8135 - 8145. [Abstract] [Full Text] [PDF]
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 C. Kitamura, Y. Ogawa, T. Nishihara, T. Morotomi, and M. Terashita Transient Co-localization of c-Jun N-terminal Kinase and c-Jun with Heat Shock Protein 70 in Pulp Cells during Apoptosis Journal of Dental Research, February 1, 2003; 82(2): 91 - 95. [Abstract] [Full Text] [PDF]
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 D. N. Lerman, P. Michalak, A. B. Helin, B. R. Bettencourt, and M. E. Feder Modification of Heat-Shock Gene Expression in Drosophila melanogaster Populations via Transposable Elements Mol. Biol. Evol., January 1, 2003; 20(1): 135 - 144. [Abstract] [Full Text] [PDF]
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H.-S. Park, S.-G. Cho, C. K. Kim, H. S. Hwang, K. T. Noh, M.-S. Kim, S.-H. Huh, M. J. Kim, K. Ryoo, E. K. Kim, et al. Heat Shock Protein Hsp72 Is a Negative Regulator of Apoptosis Signal-Regulating Kinase 1 Mol. Cell. Biol., November 15, 2002; 22(22): 7721 - 7730. [Abstract] [Full Text] [PDF]
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F. Li, H. P. Mao, K. L. Ruchalski, Y. H. Wang, W. Choy, J. H. Schwartz, and S. C. Borkan Heat stress prevents mitochondrial injury in ATP-depleted renal epithelial cells Am J Physiol Cell Physiol, September 1, 2002; 283(3): C917 - C926. [Abstract] [Full Text] [PDF]
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 D. E. Muscarella and S. E. Bloom Differential Activation of the c-Jun N-Terminal Kinase Pathway in Arsenite-Induced Apoptosis and Sensitization of Chemically Resistant Compared to Susceptible B-Lymphoma Cell Lines Toxicol. Sci., July 1, 2002; 68(1): 82 - 92. [Abstract] [Full Text] [PDF]
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V. L. Gabai, K. Mabuchi, D. D. Mosser, and M. Y. Sherman Hsp72 and Stress Kinase c-jun N-Terminal Kinase Regulate the Bid-Dependent Pathway in Tumor Necrosis Factor-Induced Apoptosis Mol. Cell. Biol., May 15, 2002; 22(10): 3415 - 3424. [Abstract] [Full Text] [PDF]
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V. L. Gabai and M. Y. Sherman Molecular Biology of Thermoregulation: Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock J Appl Physiol, April 1, 2002; 92(4): 1743 - 1748. [Abstract] [Full Text] [PDF]
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M. Yu, K. E. Pinkerton, and H. Witschi Short-Term Exposure to Aged and Diluted Sidestream Cigarette Smoke Enhances Ozone-Induced Lung Injury in B6C3F1 Mice Toxicol. Sci., January 1, 2002; 65(1): 99 - 106. [Abstract] [Full Text] [PDF]
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Y.-H. Wang, F. Li, J. H. Schwartz, P. J. Flint, and S. C. Borkan c-Src and HSP72 interact in ATP-depleted renal epithelial cells Am J Physiol Cell Physiol, November 1, 2001; 281(5): C1667 - C1675. [Abstract] [Full Text] [PDF]
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 T. Ooie, N. Takahashi, T. Saikawa, T. Nawata, M. Arikawa, K. Yamanaka, M. Hara, T. Shimada, and T. Sakata Single Oral Dose of Geranylgeranylacetone Induces Heat-Shock Protein 72 and Renders Protection Against Ischemia/Reperfusion Injury in Rat Heart Circulation, October 9, 2001; 104(15): 1837 - 1843. [Abstract] [Full Text] [PDF]
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 L. H. E. H. Snoeckx, R. N. Cornelussen, F. A. Van Nieuwenhoven, R. S. Reneman, and G. J. Van der Vusse Heat Shock Proteins and Cardiovascular Pathophysiology Physiol Rev, October 1, 2001; 81(4): 1461 - 1497. [Abstract] [Full Text] [PDF]
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B. C. Berk Vascular Smooth Muscle Growth: Autocrine Growth Mechanisms Physiol Rev, July 1, 2001; 81(3): 999 - 1030. [Abstract] [Full Text] [PDF]
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 K. K. Meldrum, D. R. Meldrum, S. F. Sezen, J. K. Crone, and A. L. Burnett Heat shock prevents simulated ischemia-induced apoptosis in renal tubular cells via a PKC-dependent mechanism Am J Physiol Regulatory Integrative Comp Physiol, July 1, 2001; 281(1): R359 - R364. [Abstract] [Full Text] [PDF]
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 P. Lane, G. Hao, and S. S. Gross S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation Sci. Signal., June 12, 2001; 2001(86): re1 - re1. [Abstract] [Full Text] [PDF]
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 A. Wenzel, C. Grimm, M. W. Seeliger, G. Jaissle, F. Hafezi, R. Kretschmer, E. Zrenner, and C. E. Remé Prevention of Photoreceptor Apoptosis by Activation of the Glucocorticoid Receptor Invest. Ophthalmol. Vis. Sci., June 1, 2001; 42(7): 1653 - 1659. [Abstract] [Full Text]
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J. B. Wijeweera, A. J. Gandolfi, A. Parrish, and R. C. Lantz Sodium Arsenite Enhances AP-1 and NF{{kappa}} B DNA Binding and Induces Stress Protein Expression in Precision-Cut Rat Lung Slices Toxicol. Sci., June 1, 2001; 61(2): 283 - 294. [Abstract] [Full Text] [PDF]
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 M. Koishi, S.'i. Yokota, T. Mae, Y. Nishimura, S. Kanamori, N. Horii, K. Shibuya, K. Sasai, and M. Hiraoka The Effects of KNK437, a Novel Inhibitor of Heat Shock Protein Synthesis, on the Acquisition of Thermotolerance in a Murine Transplantable Tumor in Vivo Clin. Cancer Res., January 1, 2001; 7(1): 215 - 219. [Abstract] [Full Text]
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 C. Jolly and R. I. Morimoto Role of the Heat Shock Response and Molecular Chaperones in Oncogenesis and Cell Death J Natl Cancer Inst, October 4, 2000; 92(19): 1564 - 1572. [Abstract] [Full Text] [PDF]
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D. D. Mosser, A. W. Caron, L. Bourget, A. B. Meriin, M. Y. Sherman, R. I. Morimoto, and B. Massie The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis Mol. Cell. Biol., October 1, 2000; 20(19): 7146 - 7159. [Abstract] [Full Text]
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V. L. Gabai, J. A. Yaglom, V. Volloch, A. B. Meriin, T. Force, M. Koutroumanis, B. Massie, D. D. Mosser, and M. Y. Sherman Hsp72-Mediated Suppression of c-Jun N-Terminal Kinase Is Implicated in Development of Tolerance to Caspase-Independent Cell Death Mol. Cell. Biol., September 15, 2000; 20(18): 6826 - 6836. [Abstract] [Full Text]
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 M. V. Gonzalez, B. Jimenez, M. T. Berciano, J. M. Gonzalez-Sancho, C. Caelles, M. Lafarga, and A. Munoz Glucocorticoids Antagonize AP-1 by Inhibiting the Activation/Phosphorylation of JNK Without Affecting its Subcellular Distribution J. Cell Biol., September 5, 2000; 150(5): 1199 - 1208. [Abstract] [Full Text] [PDF]
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 G. Huszar, K. Stone, D. Dix, and L. Vigue Putative Creatine Kinase M-Isoform in Human Sperm Is Identifiedas the 70-Kilodalton Heat Shock Protein HspA2 Biol Reprod, September 1, 2000; 63(3): 925 - 932. [Abstract] [Full Text]
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F.-X. Beck, W. Neuhofer, and E. Muller Molecular chaperones in the kidney: distribution, putative roles, and regulation Am J Physiol Renal Physiol, August 1, 2000; 279(2): F203 - F215. [Abstract] [Full Text] [PDF]
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S.-i. Yokota, M. Kitahara, and K. Nagata Benzylidene Lactam Compound, KNK437, a Novel Inhibitor of Acquisition of Thermotolerance and Heat Shock Protein Induction in Human Colon Carcinoma Cells Cancer Res., June 1, 2000; 60(11): 2942 - 2948. [Abstract] [Full Text] [PDF]
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T. Kondo, T. Matsuda, M. Tashima, H. Umehara, N. Domae, K. Yokoyama, T. Uchiyama, and T. Okazaki Suppression of Heat Shock Protein-70 by Ceramide in Heat Shock-induced HL-60 Cell Apoptosis J. Biol. Chem., March 17, 2000; 275(12): 8872 - 8879. [Abstract] [Full Text] [PDF]
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T. Kondo, T. Matsuda, T. Kitano, A. Takahashi, M. Tashima, H. Ishikura, H. Umehara, N. Domae, T. Uchiyama, and T. Okazaki Role of c-jun Expression Increased by Heat Shock- and Ceramide-activated Caspase-3 in HL-60 Cell Apoptosis. POSSIBLE INVOLVEMENT OF CERAMIDE IN HEAT SHOCK-INDUCED APOPTOSIS J. Biol. Chem., March 10, 2000; 275(11): 7668 - 7676. [Abstract] [Full Text] [PDF]
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D.-F. Liao, Z.-G. Jin, A. S. Baas, G. Daum, S. P. Gygi, R. Aebersold, and B. C. Berk Purification and Identification of Secreted Oxidative Stress-induced Factors from Vascular Smooth Muscle Cells J. Biol. Chem., January 7, 2000; 275(1): 189 - 196. [Abstract] [Full Text] [PDF]
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S. Dorion, J. Berube, J. Huot, and J. Landry A Short Lived Protein Involved in the Heat Shock Sensing Mechanism Responsible for Stress-activated Protein Kinase 2 (SAPK2/p38) Activation J. Biol. Chem., December 31, 1999; 274(53): 37591 - 37597. [Abstract] [Full Text] [PDF]
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J. Nanduri, S. Mitra, C. Andrei, Y. Liu, Y. Yu, M. Hitomi, and A. M. Tartakoff An Unexpected Link between the Secretory Path and the Organization of the Nucleus J. Biol. Chem., November 19, 1999; 274(47): 33785 - 33789. [Abstract] [Full Text] [PDF]
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S. Uma, V. Thulasiraman, and R. L. Matts Dual Role for Hsc70 in the Biogenesis and Regulation of the Heme-Regulated Kinase of the alpha Subunit of Eukaryotic Translation Initiation Factor 2 Mol. Cell. Biol., September 1, 1999; 19(9): 5861 - 5871. [Abstract] [Full Text] [PDF]
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S. H. Kim, D. Kim, J. S. Han, C. S. Jeong, B. S. Chung, C. D. Kang, and G. C. Li Ku Autoantigen Affects the Susceptibility to Anticancer Drugs Cancer Res., August 1, 1999; 59(16): 4012 - 4017. [Abstract] [Full Text] [PDF]
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J. A. Yaglom, V. L. Gabai, A. B. Meriin, D. D. Mosser, and M. Y. Sherman The Function of HSP72 in Suppression of c-Jun N-terminal Kinase Activation Can Be Dissociated from Its Role in Prevention of Protein Damage J. Biol. Chem., July 16, 1999; 274(29): 20223 - 20228. [Abstract] [Full Text] [PDF]
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V. I. Shifrin and P. Anderson Trichothecene Mycotoxins Trigger a Ribotoxic Stress Response That Activates c-Jun N-terminal Kinase and p38 Mitogen-activated Protein Kinase and Induces Apoptosis J. Biol. Chem., May 14, 1999; 274(20): 13985 - 13992. [Abstract] [Full Text] [PDF]
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 G. SCHETT, C.-W. STEINER, M. GRÖGER, S. WINKLER, W. GRANINGER, J. SMOLEN, Q. XU, and G. STEINER Activation of Fas inhibits heat-induced activation of HSF1 and up-regulation of hsp70 FASEB J, May 1, 1999; 13(8): 833 - 842. [Abstract] [Full Text]
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A. B. Meriin, J. A. Yaglom, V. L. Gabai, D. D. Mosser, L. Zon, and M. Y. Sherman Protein-Damaging Stresses Activate c-Jun N-Terminal Kinase via Inhibition of Its Dephosphorylation: a Novel Pathway Controlled by HSP72 Mol. Cell. Biol., April 1, 1999; 19(4): 2547 - 2555. [Abstract] [Full Text] [PDF]
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 M.-J. Champagne, P. Dumas, S. N. Orlov, M. R. Bennett, P. Hamet, and J. Tremblay Protection Against Necrosis but Not Apoptosis by Heat-Stress Proteins in Vascular Smooth Muscle Cells : Evidence for Distinct Modes of Cell Death Hypertension, March 1, 1999; 33(3): 906 - 913. [Abstract] [Full Text] [PDF]
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D. A. Raynes and V. Guerriero Jr. Inhibition of Hsp70 ATPase Activity and Protein Renaturation by a Novel Hsp70-binding Protein J. Biol. Chem., December 4, 1998; 273(49): 32883 - 32888. [Abstract] [Full Text] [PDF]
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S. A. Lee, A. Dritschilo, and M. Jung Impaired Ionizing Radiation-induced Activation of a Nuclear Signal Essential for Phosphorylation of c-Jun by Dually Phosphorylated c-Jun Amino-terminal Kinases in Ataxia Telangiectasia Fibroblasts J. Biol. Chem., December 4, 1998; 273(49): 32889 - 32894. [Abstract] [Full Text] [PDF]
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 A. L. Scarim, M. R. Heitmeier, and J. A. Corbett Heat Shock Inhibits Cytokine-Induced Nitric Oxide Synthase Expression by Rat and Human Islets Endocrinology, December 1, 1998; 139(12): 5050 - 5057. [Abstract] [Full Text] [PDF]
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Y. J. Lee and P. M. Corry Metabolic Oxidative Stress-induced HSP70 Gene Expression Is Mediated through SAPK Pathway. ROLE OF Bcl-2 AND c-Jun NH2-TERMINAL KINASE J. Biol. Chem., November 6, 1998; 273(45): 29857 - 29863. [Abstract] [Full Text] [PDF]
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 I. J. Benjamin and D. R. McMillan Stress (Heat Shock) Proteins : Molecular Chaperones in Cardiovascular Biology and Disease Circ. Res., July 27, 1998; 83(2): 117 - 132. [Abstract] [Full Text] [PDF]
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K. A. Buzzard, A. J. Giaccia, M. Killender, and R. L. Anderson Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis J. Biol. Chem., July 3, 1998; 273(27): 17147 - 17153. [Abstract] [Full Text] [PDF]
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B. C. Santos, A. Chevaile, M.-J. Hebert, J. Zagajeski, and S. R. Gullans A combination of NaCl and urea enhances survival of IMCD cells to hyperosmolality Am J Physiol Renal Physiol, June 1, 1998; 274(6): F1167 - F1173. [Abstract] [Full Text] [PDF]
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A. B. Meriin, V. L. Gabai, J. Yaglom, V. I. Shifrin, and M. Y. Sherman Proteasome Inhibitors Activate Stress Kinases and Induce Hsp72. DIVERSE EFFECTS ON APOPTOSIS J. Biol. Chem., March 13, 1998; 273(11): 6373 - 6379. [Abstract] [Full Text] [PDF]
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R Patel, B Bartosch, and J. Blank p21WAF1 is dynamically associated with JNK in human T-lymphocytes during cell cycle progression J. Cell Sci., January 8, 1998; 111(15): 2247 - 2255. [Abstract] [PDF]
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K. Bellmann, V. Burkart, J. Bruckhoff, H. Kolb, and J. Landry p38-dependent Enhancement of Cytokine-induced Nitric-oxide Synthase Gene Expression by Heat Shock Protein 70 J. Biol. Chem., June 9, 2000; 275(24): 18172 - 18179. [Abstract] [Full Text] [PDF]
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M. A. Miller, S. E. McGowan, K. R. Gantt, M. Champion, S. L. Novick, K. A. Andersen, C. J. Bacchi, N. Yarlett, B. E. Britigan, and M. E. Wilson Inducible Resistance to Oxidant Stress in the Protozoan Leishmania chagasi J. Biol. Chem., October 20, 2000; 275(43): 33883 - 33889. [Abstract] [Full Text] [PDF]
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D. C. H. Ng and M. A. Bogoyevitch The Mechanism of Heat Shock Activation of ERK Mitogen-activated Protein Kinases in the Interleukin 3-dependent ProB Cell Line BaF3 J. Biol. Chem., December 22, 2000; 275(52): 40856 - 40866. [Abstract] [Full Text] [PDF]
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V. L. Gabai, A. B. Meriin, J. A. Yaglom, J. Y. Wei, D. D. Mosser, and M. Y. Sherman Suppression of Stress Kinase JNK Is Involved in HSP72-mediated Protection of Myogenic Cells from Transient Energy Deprivation. HSP72 ALLEVIATES THE STRESS-INDUCED INHIBITION OF JNK DEPHOSPHORYLATION J. Biol. Chem., November 22, 2000; 275(48): 38088 - 38094. [Abstract] [Full Text] [PDF]
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N. R. Madamanchi, S. Li, C. Patterson, and M. S. Runge Thrombin Regulates Vascular Smooth Muscle Cell Growth and Heat Shock Proteins via the JAK-STAT Pathway J. Biol. Chem., May 25, 2001; 276(22): 18915 - 18924. [Abstract] [Full Text] [PDF]
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G. A. Shinder, M.-C. Lacourse, S. Minotti, and H. D. Durham Mutant Cu/Zn-Superoxide Dismutase Proteins Have Altered Solubility and Interact with Heat Shock/Stress Proteins in Models of Amyotrophic Lateral Sclerosis J. Biol. Chem., April 13, 2001; 276(16): 12791 - 12796. [Abstract] [Full Text] [PDF]
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K. F. Winklhofer, A. Reintjes, M. C. Hoener, R. Voellmy, and J. Tatzelt Geldanamycin Restores a Defective Heat Shock Response in Vivo J. Biol. Chem., November 21, 2001; 276(48): 45160 - 45167. [Abstract] [Full Text] [PDF]
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C.-Y. Li, J.-S. Lee, Y.-G. Ko, J.-I. Kim, and J.-S. Seo Heat Shock Protein 70 Inhibits Apoptosis Downstream of Cytochrome c Release and Upstream of Caspase-3 Activation J. Biol. Chem., August 11, 2000; 275(33): 25665 - 25671. [Abstract] [Full Text] [PDF]
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J. G. Kiang, S. C. Kiang, Y.-T. Juang, and G. C. Tsokos Nomega -nitro-L-arginine inhibits inducible HSP-70 via Ca2+, PKC, and PKA in human intestinal epithelial T84 cells Am J Physiol Gastrointest Liver Physiol, March 1, 2002; 282(3): G415 - G423. [Abstract] [Full Text] [PDF]
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