From: Subject: Tumorigenesis: A shocking enabler of tumour growth : Article : Nature Reviews Cancer Date: Thu, 8 May 2008 13:10:34 +0200 MIME-Version: 1.0 Content-Type: multipart/related; type="text/html"; boundary="----=_NextPart_000_009F_01C8B10C.E65D3090" X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.5512 This is a multi-part message in MIME format. ------=_NextPart_000_009F_01C8B10C.E65D3090 Content-Type: text/html; charset="iso-8859-1" Content-Transfer-Encoding: quoted-printable Content-Location: http://www.nature.com/nrc/journal/v7/n11/full/nrc2262.html Tumorigenesis: A = shocking enabler of tumour growth : Article : Nature Reviews = Cancer

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Nature Reviews Cancer = 7, 817 = (November 2007) | = doi:10.1038/nrc2262

Tumorigenesis: A shocking = enabler of tumour=20 growth

Sarah Seton-Rogers

The conserved heat-shock response, mediated largely by = the=20 transcription factor heat-shock factor 1 (HSF1),=20 allows cells to adapt to stress. Although this response is crucial to = protect=20 against some diseases of ageing, including ischaemia and = neurodegenerative=20 disorders, Susan Lindquist and colleagues now show that HSF1 has an = opposite=20 role in cancer, in which it promotes tumorigenesis.

The authors first showed that Hsf1-/- mice were less susceptible to skin = tumours=20 induced by the chemical carcinogens dimethylbenzanthracene (DMBA) and = 12-O-tetradecanoylphorbol-13-acetate (TPA) than were = wild-type mice=20 =97 tumour latency and survival were increased and tumour incidence and = burden=20 were reduced in Hsf1-/- mice. The = authors also=20 examined the effects of HSF1 on tumours arising in mice heterozygous for = the Trp53 mutation Trp53R172H. As=20 in the skin carcinogenesis model, tumour-free survival was increased in = Hsf1-/- mice carrying this allele.

A random sampling of chemically induced skin tumours = that=20 developed in Hsf1-/- and wild-type = mice showed=20 that all had activating mutations in Hras. To further examine the effects of HSF1 on=20 transformation by HRAS, the authors expressed an activated form of HRAS, = encoded=20 by HRASV12D, in Hsf1-/- and wild-type mouse embryonic = fibroblasts=20 (MEFs) and found that a lack of HSF1 made the MEFs resistant to=20 HRASV12D-induced focus formation. Similar results were = observed using=20 wild-type MEFs expressing short hairpin RNAs (shRNAs) directed against = Hsf1.

How does HSF1 promote tumorigenesis? The differential = effects of=20 HRASV12D on Hsf1-/- versus = wild-type=20 mice were a result of increased proliferation of the wild-type cells, = rather=20 than increased death of Hsf1-/- cells. = However,=20 expression of MYC or SV40 large T antigen enhanced death in Hsf1-/- MEFs, so depending on the oncogenic = insult=20 HSF1 seems able to promote either proliferation or survival. HSF1 might = also=20 affect signalling pathways. The authors found blunted activation of=20 extracellular signal-regulated kinase (ERK) downstream of Ras in the = absence of=20 HSF1. Activation of protein kinase A (PKA) downstream of = G-protein-coupled=20 receptor activation was also reduced, suggesting that HSF1 can modulate = at least=20 two oncogenic signalling pathways.

Yet another effect of HSF1 on tumorigenesis might result = from its=20 role in translation. Ribosomal biogenesis normally depends on growth = factors,=20 but cancer cells can circumvent this requirement. The expression of = ribosomal=20 subunits was reduced in serum-starved Hsf1-/- or=20 Hsf1 shRNA-expressing MEFs compared with = wild-type cells,=20 indicating that HSF1 deficiency promotes the dependency of the = translational=20 machinery on growth factors. HSF1 might also affect translation through = its=20 effects on the mammalian target of rapamycin (mTOR)=20 pathway. Inhibition of mTOR or loss of its downstream effector p70S6K=20 (ribosomal protein S6 kinase, 70 kDa) impairs protein translation and = reduces=20 cell size, and MEFs from Hsf1-/- mice = had=20 reduced p70S6K phosphorylation and a smaller size.

Finally, HSF1 can promote glycolysis, which occurs in = most cancer=20 cells and is beneficial for tumour growth and survival. Glucose uptake = was=20 decreased in Hsf1-/- compared with = wild-type=20 MEFs, and Hsf1-/- cells were less = dependent on=20 glucose for survival.

Is HSF1 relevant in human cancers? The authors examined = human cell=20 lines of varying malignant potential that were either transformed in the = laboratory or derived from human tumours with diverse histological = origins and=20 various genetic abnormalities. In all cases, they found that the growth = of=20 tumorigenic cells was decreased by shRNA knockdown of HSF1.

HSF1 seems to act not as a classic oncogene, but as a = modulator of=20 tumorigenesis, affecting multiple pathways that allow cells with = oncogenic=20 defects to adapt and survive. Activation of HSF1 is being explored for = treating=20 ischaemic injury and some neurodegenerative diseases, and it needs to be = determined whether such therapies might enhance tumorigenesis if used in = the=20 long term. Furthermore, any potential cancer therapeutics that inhibit = HSF1=20 could possibly affect neurodegeneration and ageing. Hopefully a greater=20 understanding of HSF1 will lead to the development of more effective=20 therapeutics for several diseases.

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