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Heat shock proteins are co-opted for cancer
Date:9/20/2007

protein synthesis and metabolism.

In mice, an HSF1 deficiency drastically limited tumor formation induced by either a chemical carcinogen or a cancer-causing genetic mutation.

Using cells from a variety of human tumors, Dai showed that depriving the cancer cells of HSF1 strongly suppressed their ability to grow and survive. We propose that HSF1 could provide a uniquely effective target for the discovery of broadly active anticancer agents, says Lindquist.

Its increasingly apparent, Whitesell comments, that many biological mechanisms can play dual rolessometimes beneficial, sometimes not.

It makes perfect sense to us that HSF1 plays this dual role, Dai says. It has been shown that HSF1 is involved in protecting against neurodegeneration, in which brain cells die slowly over time. In cancer, the opposite is true: cancer cells dont die. Ironically, cancer cells hijack and exploit this evolutionarily conserved self-protective function of HSF1.

In fact, he says, cancer cells appear much more sensitive than normal cells to the loss of HSF1 function.

It will be interesting to see how the insights gained from studies such as this one can be applied to develop useful therapeutics, Whitesell says. The next step is to look for existing compounds that induce or inhibit the heat-shock response in cells. The challenge will be to manipulate the target for therapeutic advantage without tipping the scales too much or in the wrong places.


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Contact: Eric Bender
bender@wi.mit.edu
617-258-9183
Whitehead Institute for Biomedical Research
Source:Eurekalert

Page: 1 2

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