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Heat shock proteins in cancer
Heat shock proteins in cancer:
chaperones of tumorigenesis
Stuart K. Calderwood1,3, Md Abdul Khaleque1, Douglas B. Sawyer3
and Daniel R. Ciocca2
1Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA
2Institute of experimental Medicine and Biology of Cuyo (CRICYT-CONICET) and Argentine Foundation for Cancer Research (FAIC),
Mendoza 5500, Argentina
3Boston University School of Medicine, Boston, MA 02118, USAThe heat shock proteins (HSPs) induced by cell stress are
expressed at high levels in a wide range of tumors and
are closely associated with a poor prognosis and
resistance to therapy. The increased transcription of
HSPs in tumor cells is due to loss of p53 function and to
higher expression of the proto-oncogenes HER2 and
c-Myc, and is crucial to tumorigenesis. The HSP family
members play overlapping, essential roles in tumor
growth both by promoting autonomous cell prolifer-
ation and by inhibiting death pathways. The HSPs have
thus become targets for rational anti-cancer drug
design: HSP90 inhibitors are currently showing much
promise in clinical trials, whereas the increased
expression of HSPs in tumors is forming the basis of
chaperone-based immunotherapy.Introduction
Heat shock proteins (HSPs) are the products of several
distinct gene families that are required for cell survival
during stress and are named according to the approximate
relative molecular mass (Mr) of their encoded proteins,
including HSP10, HSP27, HSP40, HSP60, HSP70, HSP90
and HSP110 [1–4] (Table 1). The cytoprotective properties
of the HSPs are closely linked to their primary functions
as molecular chaperones [1,5,6]. The intracellular
reactions catalyzed by the HSPs, which led to their
designation as molecular chaperones, are divided into
two main categories described as ‘protein holding’ and
‘protein folding’ [7,8].
The principal holding proteins belong to the HSP70 and
HSP90 families, which bind to unfolded sequences in
polypeptide substrates and show prefere
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