[CANCER RESEARCH 52, 2854-2861, May 15, 1992|
Thermotolerance in the Absence of Induced Heat Shock Proteins in a Murine
Lymphoma1
Barbara Fisher,2 Peggy Kraft, George M. Hahn, and Robin L. Anderson3
Department of Radiation Oncology, Stanford University, Stanford, California 94305 [B. F., P. K., G. M. ff.J, and Peter MacCallum Cancer Institute, 4SI Lt. Lonsdale
St., Melbourne, yictoria 3000, Australia [R. L. A.]
ABSTRACT
Three murine lymphoma cell lines, CHI, a B-cell lymphoma, and VL3
and RDM4, both T-cell lymphomas, were tested for their ability to induce
heat shock protein synthesis and thermotolerance after heat shock. All
three lines could develop thermotolerance, but the persistence of tolerance
was less than can be measured in nonlymphoid cell lines. Analysis of
protein synthesis patterns by one-dimensional gel electrophoresis sug
gested that only the VL3 cells were capable of the induction of heat
shock proteins. After two-dimensional gel analysis, however, the induc
tion of one heat shock protein was evident in RDM4 cells. No induced
heat shock proteins could be detected in the CHI cells. These data
provide strong evidence that, while the induction of heat shock proteins
may be sufficient for development of thermotolerance, they are not
necessary and that another mechanism is available to cells.
INTRODUCTION
The development of thermotolerance, a transient resistance
to heat induced by prior heating or by other inducers of the
heat shock response (1), is nearly always accompanied by the
induction of a class of proteins known as the HSP4 or stress
proteins (2). The good temporal correlation between the ap
pearance and turnover of the HSP and the development and
decay of thermotolerance (3-5) is strong circumstantial evi
dence that the HSP protect cells from subsequent damage from
heat or other stress-inducing agents such as ethanol, arsenite,
transition metals, release from hypoxia, and various inhibitors
of oxidative phosphorylation.
Further evidence for the involvement of HSP in heat protec
tion comes from the characterization of heat-resistant lines
selected from rodent cell lines. Heat-resistant cells derived from
Chinese hamster ovary cells contain elevated levels of HSP73
(6), those from a transformed subclone of Chinese hamster lung
fibroblasts contain elevated levels of HSP27 (7), and those from
the murine RIF-1 tumor contain elevated levels of several major
HSP (8). Landry et al. (9) have gone on to show that transfec-
tion of the human gene for HSP27 into the Chinese hamster
lung cells confers resistance to heat shock. Other experiments
have shown that microinjection of antibodies against HSP73/
72 (10) or introduction of a large number of copies of the heat
shock element (11) results in increased heat sensitivity, provid
ing further evidence for the involvement of this family of
proteins in heat protection. (There are two major HSP in
murine cells with subunit molecular weights of approximately
70,000: HSP73, which is constitutively expressed; and HSP72,
which is induced after stress.)
On the other hand, several studies have shown that HSP are
Received 3/26/90; accepted 3/10/92.
The costs of publication of this article were defrayed in part by the payment
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1Supported by Grant CA4466S from the National Cancer Institute and by the
Anti-Cancer Council of Victoria, Australia.
2 Present address: London Regional Cancer Centre, 790 Commissioners Rd.
E., London, Ontario N6A 4L6, Canada.
3 To whom requests for reprints should be addressed.
4 The abbreviations used are: HSP, heat shock protein(s); CHO, Chinese
hamster ovary.
not essential for the expression of thermotolerance. For exam
ple, under certain circumstances, cells treated with cyclohex-
imide can still express thermotolerance despite the lack of de
novo protein synthesis (12-15). However, these experiments
are confounded by the fact that cycloheximide itself can confer
heat protection (16, 17). Other research suggests that cyclohex
imide does inhibit thermotolerance (18).
There are other examples of thermotolerance in the absence
of HSP induction that do not involve the use of protein synthe
sis inhibitors. CHO cells heated slowly to 42°Cover a 3-h
period show tolerance to 42°Cheating without an increase in
the amount of HSP, but tolerance to 45°Cis minimal (19).
Exposure of cells to hydrocortisone for 12 to 24 h also induces
thermotolerance without the induction of HSP (20). Other
examples include thermal adaptation of CHO cells at 40°C
(21), exposure of pollen tubes from Tradescantia to gradually
increasing temperatures (22), and mild heat exposure in snail
larvae (23). Taken together, these studies suggest that, while
HSP are sufficient for expression of thermotolerance, they are
not necessary and that another mechanism(s) can also confer
heat protection. Data from our laboratory (19), from Hallberg
(14), and from Lee and Dewey (24) suggest that the tolerance
that develops in the absence of increased HSP synthesis does
not confer the same degree of heat protection, especially at
higher temperatures, as can be achieved in the presence of
elevated HSP.
One approach to investigating the importance of induced
HSP in the development of thermotolerance is to study cells
with a defective heat shock response. Aujame (25) has shown
that some murine plasmacytomas of both B- and T-cell origin
and some murine erythroleukemia cell lines (26) fail to show
induction of HSP 72, but induction of the other HSP is normal.
Aujame and Furko (27) went on to show that the plasmacyto
mas do express thermotolerance. Early embryonic cells also fail
to show induction of HSP until the embryo reaches the blasto-
cyst stage (28) and, in parallel with these observations, Müller
e/ al. (29) have demonstrated that these cells fail to express
thermotolerance. Some embryonal carcinoma cell lines (28, 30)
and a murine erythroleukemic line, MEL (31), are also deficient
in expression of HSP, but the response of these cells to heat
has not been tested. Some species of Hydra, but not all, also
fail to exhibit thermotolerance and induction of HSP (32).
A cell line with an inability to synthesize any heat-induced
HSP was discovered in our laboratory during a study of the
effect of hyperthermia on the lateral diffusion of H-2Kk (33).
The CHI cells are from an early murine B-cell lymphoma
isolated by Lanier et al. (34) by inoculation of BlO-H-FH-Sp/
Wts mice with spleen cells or sera from syngeneic donors
hyperimmunized with sheep erythrocytes. The cells lack the T-
cell-specific antigen (Thy-1) but express cell surface immunog-
lobin and the H-2K, H-2D, and la specificities determined by
the H-2°haplotype. We have now analyzed the response of
CH1 cells to heat shock in more detail and compared them to
two other murine lymphoma lines, VL3 and RDM4. In all
three lines, thermotolerance can be expressed, but it decays
more rapidly than in fibroblast cell lines. Analysis of protein
2854
Research.
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