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1 Citations 4 Q&As
1 Citations 5 Q&As
Facts about Heat shock factor protein 1.
Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Activation is reversible, and throughout the attenuation and recovery period period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218).
Human | |
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Gene Name: | HSF1 |
Uniprot: | Q00613 |
Entrez: | 3297 |
Belongs to: |
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HSF family |
heat shock factor protein 1; heat shock transcription factor 1HSTF1HSF 1; HSF1; HSTF 1; HSTF1
Mass (kDA):
57.26 kDA
Human | |
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Location: | 8q24.3 |
Sequence: | 8; NC_000008.11 (144291603..144314720) |
Nucleus. Cytoplasm. Nucleus, nucleoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624, PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683, PubMed:10359787). Translocates in the nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic shuttling protein (PubMed:26159920). Colocalizes with IER5 in the nucleus (PubMed:27354066). Colocalizes w
HSF1 stands for heat shock element transcription factor. It binds to certain genes and inhibits their expression. This biomarker can help to target cancer cells. This article explains what HSF does.
HSF1 does not cause cancer in humans, but overexpression of this protein inhibits the transformation of immortalized mice embryonic fibroblasts. HSF1-deficient MEFs are insensitive to the oncogenic adenovirus RASV12D. Moreover, they exhibit reduced proliferation and increased cell death after transduction. Hence, HSF1 could offer cancer cells relief.
It has been demonstrated that insulin resistance can be linked to changes in HSF1 expression and other heat shock response effectsors. HSPA1A expression in mice is sufficient to prevent the development of type-2 diabetes. HSPA1A exclusion in obese mice prevented insulin resistance. BGP-15 treatment improved insulin sensitivity in mice. HSF1 regulates the expression and function of insulin-responsive genes. Therefore, manipulation of their expression may increase insulin sensitivity and skeletal muscular oxidation.
The binding of HSF1 to specific DNA sequences regulates gene expression. HSF1 regulates ATG7, a gene well-known as having a resistance to chemotherapy. Knockdown ATG7 decreases autophagy. However, HSF1-stable cell were more sensitive and responsive to carboplatin than those that were unstable. HSF1 is bound to DNA only through the promoter region. This increases histone H3 and acetylation.
The trans-conformation of HSF1 enhances its DNA-binding activity. This could explain the many roles it plays in transcriptional regulation. PIN1 has been identified in the HSF1-DNA relationship as a key mediator. More research is needed to confirm these findings. HSF1 DNA association in mice is still controversial. It is a reversible process. Despite its multiple roles in cancer development, HSF1-DNA association in mice does appear to be a positive determinant.
The heat shock factor (HSF) binds to a protein in the nucleus that is responsible for regulating heat shock response. The five subunits that make up the HSF proteins in humans are all structurally distinct. HSF homodimers will become unstable if they are subject to heat shock. HSF-related heterodimers will form inhibitory complexes when they are exposed to heat stress. The HSF hexamer binds HSE with high affinity, promoting transcription of heat shock-related genes.
The human HSF gene has been mapped to chromosome 56A. It has low activity at 25°C due to its low translation efficacy. DNA competition experiments further confirm the specific binding of HSF to DNA in vitro. Without heat shock, HSF translation in vitro requires activating substances to be present in the cells' cytosol.
Boster Bio HSF1 is able to bind directly to the ATF-1 gene, which encodes heat shock-resistant A. fumigatus Protein ATF-1. This gene is essential to the survival and growth this species. HSF1 is responsible for controlling translation, osmoregulation and cell division in A. fumigatus. The gene encodes a nudC orlog that functions as a transcription factor and exhibits chaperone activity.
Despite these positive results, there is no direct evidence that HSF1 switches between states. HSF1 switches from one state to another through a dynamic dissociation and re-association with chaperones. Although the mechanism of HSF1 switching is still unknown, it could be related to other factors. This research will shed new light on the role of chaperones in the heat shock response.
Boster Bio's HSF1 marker gene inhibits the transcriptions of genes that are involved the the heat-shock (HSR) response. It is not known how HSF binds with ecdysone inducible genes. HSF and Ecdysone interact but this causes chromatin change that allows HSF bind to ecdysone. This interaction also involves active transcribing, which mediates HSE access. Activator protein 1 is believed to be a key component in HSF binding. This allows the Glucocorticoid to bind with cognate elements in ecdysone induced genes.
HSF's rapid recovery from injury indicates that it is active for transcription of target gene targets. HSF is stable in binding to DNA in vivo, indicating that the HSF/hsp70 interaction does not depend on turnover. In living cells, transcription activators display dynamic behaviours. HSF markers are useful in studying the dynamics of transcription genes and native heat shock genes.
The HSF1 gene marker is a powerful tool for studying the regulation of heat shock-related genes. This marker inhibits heat shock-related genes expression in a variety of tissues. The HSF1 gene marker binds with spermatogonias as well as spermatids. This is a highly-specific heat-shock reaction marker. The marker binds to genes within the head and testes.
Boster Bio’s HSF1 gene-marker detects polymerases in the elongation phases. Functional HSF is essential for heat shock genes. Activator dependent reinitiation of transcription prevents formation of a slow TFIID/TFIIA compound on the promoter. This is especially important for genes that are heat-shock-related.
Researchers have identified PAR4's role as a breast cancer marker and are investigating its pro-apoptotic effects. Previous studies have shown that PAR4 can prevent breast cancer cells from growing. This study investigated the expression of PAR4 in breast cancer tissues, and its effects on in vitro and in vivo breast cancer cell growth. We discuss the mechanisms. We discuss the effects of this model on the growth and spread of breast cancer cells.
Researchers from the University of Rochester Medical Center discovered a new mechanism that suppresses tumor growth. These findings could lead to new anticancer drugs. They discovered that a specific type of STAT5A protein was capable of stabilizing the form of chromosomal genetic DNA called heterochromatin. This inhibits the growth and spread of cancer cells.
A study published in Journal of Neuroscience recently suggests that Boster Bio HSF1 antagonists can inhibit the production of amyloid beta42 proteini. While the exact mechanism is still unknown, it is possible that the inhibitors interfere with g–secretase which is a negative feedback enzyme that can contribute towards amyloid deposition.
APP is an evolutionary conserved large transmembrane protein that is processed by b and g-secretases. Familial AD can be caused by mutations within the APP genes. The non-toxic fragments that result are thought to inhibit the production of Abs. The inhibitors can also block another amyloidogenic pathway, making them a good choice to treat patients with this disease.
PMID: 1871105 by Rabindran S.K., et al. Molecular cloning and expression of a human heat shock factor, HSF1.
PMID: 1871106 by Schuetz T.J., et al. Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans.
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