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KMID : 0670719970020010077
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Journal of the Korean Society Hyperthermia Oncology
1997 Volume.2 No. 1 p.77 ~ p.94
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Heat Shock Proteins, Thermotolerance, and Their Relevance to Hyperthermic Oncology
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Young-Mee Park
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Abstract
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Introduction
During the last decade, much progress has been made in understanding the molecular,
biochemical and cellular consequences of thermal stress. Results from cell culture
experiments, animal studies and clinical trials have provided significant evidence that
hyperthermia has a useful role in cancer therapy, such as radiotherapy and
chemotherapy. Nonetheless, the mechanistic description of how cells are killed by
hyperthermia is far from clear. Evidence suggests that protein denaturation is involved
in this process, while direct damage to DNA is not. Acute and chronic heating induce a
variety of intracellular changes such as alteration in nuclear and cytoskeletal structures,
cellular metabolism and macromolecular synthesis. Intracellular signal transduction or
hormone-receptor interactions to are affected by heat shock.
On the transcriptional and transitional level, heat shock induces the expression of a
unique set of genes, the heat shock genes, which encode for the synthesis of number of
proteins, called heat shock proteins (HSPs). Some of the HSPs are highly conserved in
nature, for example the 70kD protein (HSP 70). Recently, significant discoveries have
been nape about the possible functions of some of the HSPs. For example, members of
the HSP70 multigene family in eukaryotes have been shown to participate in protein
transport into cellular organelle, such as mitochondria or endoplasmic reticulum. HSP60
is found to be involved in the assembly of imported proteins into mitochondria. In more
general term, it is suggested that HSPs participate in the formation and disaggregation
of macromolecular stucture.
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