HSF1

Official Full Name

heat shock transcription factor 1

Organism

Homo sapiens

GeneID

3297

Background

The product of this gene is a transcription factor that is rapidly induced after temperature stress and binds heat shock promoter elements (HSE). This protein plays a role in the regulation of lifespan. Expression of this gene is repressed by phosphorylation, which promotes binding by heat shock protein 90. [provided by RefSeq, Jul 2017]

Synonyms

HSTF1;

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Detailed Information

Recent Research Progress

Heat shock factor 1 (HSF1) is a transcriptional factor that determines the efficiency of heat shock responses (HSRs) in the cell. HSF1 has been extensively considered to be a potential target for the treatment of conditions associated with protein aggregation. The activity of HSF1 is traditionally regulated at the transcriptional level, where the transactivation domain is modified by extensive post-translational modifications such as phosphorylation, SUMOylation and acetylation. Recently, it has also been reported that HSF1 is regulated at the monomer level. The monomeric HSF1 not only determines the efficiency of HSRs, but exerts a protective effect in a manner independent of trimerization. HSF1 may be an alternative strategy for amplifying HSR.

Coincidentally, increased HSF1 expression predicts a shortened disease-specific survival in prostate cancer patients after radical prostatectomy. A recent report has identified HSF1 as a potential biomarker in mRNA expression datasets on prostate cancer. This finding indicates that increased nuclear HSF1 expression is associated with disease progression and invasiveness, and is independent of established clinicopathological variables, predicting early initiation of secondary treatment and poor disease-specific survival. Wang X et al. investigated the effect of HSF1 proteins on cell proliferation, apoptosis and invasion of breast cancer. The results showed that the proliferation rate and tumor growth rate of HSF1-knockdown cells were significantly decreased, indicating that HSF1 may be involved in the proliferation of breast cancer cells. From the perspective of apoptosis, it was found that the apoptosis rate of HSF1-knockdown MCF-7(the Michigan Cancer Foundation-7) breast cancer cells was significantly higher than that of the control cells, indicating that the over-expression of HSF1 significantly reduces cell apoptosis. In addition, the invasion ability of cells reflected the features of the metastasis and infiltration of tumor cells at a particular level. It was also found that the invasion ability of HSF1-knockdown MCF-7 cells was significantly decreased, manifesting that HSF1 is related to the invasion ability of MCF-7 cells. HSF1 may promote cell proliferation, inhibit cell apoptosis and increase cell invasion so as to promote disease progression by acting on its downstream signaling molecules, and it is expected to be used as a target for the treatment of tumors.

A recent research suggested that heat-shock transcription factor 1 (HSF1) is a novel repressor of ischaemia-induced cardiac hypertrophy, the main cause of death from myocardial infarction (MI). Ligation of left anterior descending coronary was used to produce MI in HSF1-deficient heterozygote (KO), HSF1 transgenic (TG) mice and their wild-type (WT) littermates, respectively. Neonatal rat cardiomyocytes (NRCMs) were treated by hypoxia to mimic MI in vitro. The HSF1 phosphorylation was significantly reduced in the infarct border zone of mouse left ventricles (LVs) 1 week after MI and in the hypoxia-treated NRCMs. HSF1 KO mice showed more significant maladaptive cardiac hypertrophy and deteriorated cardiac dysfunction 1 week after MI compared to WT MI mice. Deficiency of HSF1 by siRNA transfection notably increased the hypoxia-induced myocardial hypertrophy in NRCMs. Mechanistically, the data collectively demonstrated that HSF1 is critically involved in the pathological cardiac hypertrophy after MI via modulating JAK2/STAT3 signaling and may constitute a potential therapeutic target for MI patients.

References:

Björk JK, et al. Increased HSF1 expression predicts shorter disease-specific survival of prostate cancer patients following radical prostatectomy. Oncotarget, 2018, 9(58): 31200-31213.
WANG X, et al. A study on the biological function of heat shock factor 1 proteins in breast cancer. Oncology Letters, 2018, 16(3): 3821-3825.
Yuan L, et al. Heat-shock transcription factor 1 is critically involved in the ischaemia-induced cardiac hypertrophy via JAK2/STAT3 pathway. Journal of Cellular & Molecular Medicine, 2018.

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