Heat Shock Transcription Factor 2 Is Significantly Involved in Neurodegenerative Diseases, Inflammatory Bowel Disease, Cancer, Male Infertility, and Fetal Alcohol Spectrum Disorder: The Novel Mechanisms of Several Severe Diseases.

HSF (heat shock transcription factor or heat shock factor) was discovered as a transcription factor indispensable for heat shock response. Although four classical HSFs were discovered in mammals and two major HSFs, HSF1 and HSF2, were cloned in the same year of 1991, only HSF1 was intensively studied because HSF1 can give rise to heat shock response through the induction of various HSPs' expression. On the other hand, HSF2 was not well studied for some time, which was probably due to an underestimate of HSF2 itself.

Cell Cycle Regulation by Heat Shock Transcription Factors.

Cell division and cell cycle mechanism has been studied for 70 years. This research has revealed that the cell cycle is regulated by many factors, including cyclins and cyclin-dependent kinases (CDKs). Heat shock transcription factors (HSFs) have been noted as critical proteins for cell survival against various stresses; however, recent studies suggest that HSFs also have important roles in cell cycle regulation-independent cell-protective functions.

Structural and biochemical basis of the formation of isoaspartate in the complementarity-determining region of antibody 64M-5 Fab.

The formation of the isoaspartate (isoAsp) is one of spontaneous degradation processes of proteins, affecting their stability and activity. Here, we report for the first time the crystal structures of an antibody Fab that contains isoAsp in the complementarity-determining region (CDR), along with biochemical studies to detect isoAsp. By comparing the elution profiles of cation-exchange chromatography, it was clarified that the antibody 64M-5 Fab is converted from the normal form to isoAsp form spontaneously and time-dependently under physiological conditions.

Successful hybrid management of a ruptured abdominal aortic aneurysm induced by type II and IIIB endoleaks after endovascular aortic repair.

Ruptured abdominal aortic aneurysm after endovascular abdominal aortic repair is a relatively rare condition. The management of this type of a rupture is challenging and controversial. We report here a case of ruptured abdominal aortic aneurysm 6 months after endovascular abdominal aortic repair.

A Case of Thoracic Endovascular Aortic Repair Using Carotid Access with Axillary-Carotid Bypass for Descending Aortic Aneurysm in a Patient with Aortoiliac Occlusive Disease.

The authors report a 71-year-old male with descending thoracic aortic aneurysm and multiple risk factors (aortoiliac occlusive disease, obesity, ascending aorta dilatation, and history of left ventriculoperitoneal shunt for hydrocephalus) who was treated with thoracic endovascular aortic repair (TEVAR) via left common carotid artery (LCCA) access and left axillary-carotid artery (Ax-CA) bypass; this approach shortened the LCCA clamp time during the procedure. The patient was discharged without any complications. TEVAR via LCCA access with left Ax-CA bypass is a useful and safe procedure for patients in whom conventional femoral artery access is not feasible.

Structures of the antibody 64M-5 Fab and its complex with dT(6-4)T indicate induced-fit and high-affinity mechanisms.

DNA photoproducts with (6-4) pyrimidine-pyrimidone adducts produced by ultraviolet light are mutagenic and carcinogenic. The crystal structures of the anti-(6-4) photoproduct antibody 64M-5 Fab and of its complex with dT(6-4)T were determined at 2.5 and 2.

Surgical treatment for adult congenital heart disease: consideration for indications and procedures.

The number of the adult patients with congenital heart diseases (ACHD) continues to grow owing to improvement of surgical results and medical management. Corrective surgery for complex CHD does not always mean complete cure. It is not rare that the patients will visit the cardiology institutes because of secondary lesions due to residua or sequela in adults.

Set1/MLL complex is indispensable for the transcriptional ability of heat shock transcription factor 2.

Heat shock transcription factor 2 (HSF2) is one of four mammalian HSFs, and it is essential in neurogenesis and gametogenesis. However, other aspects of this transcription factor have not been thoroughly characterized. We recently demonstrated that HSF2 suppresses the aggregation caused by polyglutamine (polyQ) protein, and that the cell protective ability of HSF2 is mediated through the induction of the small HSP alphaB-crystallin (CRYAB).

Non-Hsp genes are essential for HSF1-mediated maintenance of whole body homeostasis.

Mammalian tissues are always exposed to diverse threats from pathological conditions and aging. Therefore, the molecular systems that protect the cells from these threats are indispensable for cell survival. A variety of diseases, including neurodegenerative diseases, cause intracellular damage and disturb homeostasis.

Analysis of the heat shock factor complex in mammalian HSP70 promoter.

The heat shock response is characterized by the induction of heat shock proteins (HSPs) and is one of prominent mechanisms that regulate proteostasis capacity in the cell. In mammals, heat shock factor 1 (HSF1) regulates the expression of HSPs transcriptionally in both unstressed and stressed cells. Recent reports show that the HSF1-RPA complex constitutively gains access to nucleosomal DNA in part by recruiting a histone chaperone and a chromatin-remodeling component.

Mitochondrial SSBP1 protects cells from proteotoxic stresses by potentiating stress-induced HSF1 transcriptional activity.

Heat-shock response is an adaptive response to proteotoxic stresses including heat shock, and is regulated by heat-shock factor 1 (HSF1) in mammals. Proteotoxic stresses challenge all subcellular compartments including the mitochondria. Therefore, there must be close connections between mitochondrial signals and the activity of HSF1.

ATF1 modulates the heat shock response by regulating the stress-inducible heat shock factor 1 transcription complex.

The heat shock response is an evolutionally conserved adaptive response to high temperatures that controls proteostasis capacity and is regulated mainly by an ancient heat shock factor (HSF). However, the regulation of target genes by the stress-inducible HSF1 transcription complex has not yet been examined in detail in mammalian cells. In the present study, we demonstrated that HSF1 interacted with members of the ATF1/CREB family involved in metabolic homeostasis and recruited them on the HSP70 promoter in response to heat shock.

Heat shock factor 1 is required for migration and invasion of human melanoma in vitro and in vivo.

Heat shock factor 1 (HSF1) is a major transactivator of the heat shock response. Recent studies have demonstrated that HSF1 is involved in tumor initiation, maintenance, and progression by regulating the expression of heat shock proteins (HSPs) and other molecular targets. Furthermore, HSF1 was identified as a potent proinvasion oncogene in human melanomas.

Wound complications of the retroperitoneal approach for the abdominal aortic aneurysm repair-an evaluation of abdominal bulge formation-.

Objective: To evaluate the incidence of wound complications after the retroperitoneal approach for abdominal aortic aneurysm (AAA) repair, and to ascertain the cause of abdominal bulge (AB).

Subjects And Methods: Forty-three patients with AAA repair via the retroperitoneal space were retrospectively investigated. Wound complications and their incidence were studied by chart review.

Chicken IL-6 is a heat-shock gene.

The febrile response is elicited by pyrogenic cytokines including IL-6 in response to microorganism infections and diseases in vertebrates. Mammalian HSF1, which senses elevations in temperature, negatively regulates the response by suppressing pyrogenic cytokine expression. We here showed that HSF3, an avian ortholog of mammalian HSF1, directly binds to and activates IL-6 during heat shock in chicken cells.

Surgical angioplasty for ostial atresia of left main coronary artery in child.

Ostial atresia of the left main coronary artery (LMCA) in children without any primary disease is extremely rare. We present here a case of occlusion of the LMCA in a 9-year-old girl. Myocardial scintigraphy showed poor perfusion in both domains of the left anterior descending artery (LAD) and left circumflex artery (LCx).

RPA assists HSF1 access to nucleosomal DNA by recruiting histone chaperone FACT.

Transcription factor access to regulatory elements is prevented by the nucleosome. Heat shock factor 1 (HSF1) is a winged helix transcription factor that plays roles in control and stressed conditions by gaining access to target elements, but mechanisms of HSF1 access are not well known in mammalian cells. Here, we show the physical interaction between the wing motif of human HSF1 and replication protein A (RPA), which is involved in DNA metabolism.

Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation.

Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs.

Transcription factor cooperativity with heat shock factor 1.

The heat shock response has been characterized by the induction of major heat shock proteins that suppress protein aggregation by facilitating protein folding. Recently, we found that mammalian heat shock factor 1, a master regulator of HSP genes, regulates non-HSP genes that suppress protein aggregation by controlling protein degradation in cooperation with the transcription factor NFAT.

Silencing HSF1 by short hairpin RNA decreases cell proliferation and enhances sensitivity to hyperthermia in human melanoma cell lines.

Background: Heat shock transcription factor 1 (HSF1) is a major transactivator of genes coding for heat shock proteins (Hsps). Recent studies demonstrate that HSF1 is involved in tumor initiation, maintenance, and progression by regulating the expression of Hsps and other molecular targets. However, the role of HSF1 in melanoma is largely unknown.

Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT.

Heat shock transcription factor 1 (HSF1) is an important regulator of protein homeostasis (proteostasis) by controlling the expression of major heat shock proteins (Hsps) that facilitate protein folding. However, it is unclear whether other proteostasis pathways are mediated by HSF1. Here, we identified novel targets of HSF1 in mammalian cells, which suppress the aggregation of polyglutamine (polyQ) protein.

Heat shock transcription factor 1 inhibits expression of IL-6 through activating transcription factor 3.

The febrile response is a complex physiological reaction to disease, including a cytokine-mediated increase in body temperature and the activation of inflammatory systems. Fever has beneficial roles in terms of disease prognosis, partly by suppressing the expression of inflammatory cytokines. However, the molecular mechanisms underlining the fever-mediated suppression of inflammatory gene expression have not been clarified.

A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock.

The heat-shock response is characterized by the expression of a set of classical heat-shock genes, and is regulated by heat-shock transcription factor 1 (HSF1) in mammals. However, comprehensive analyses of gene expression have revealed very large numbers of inducible genes in cells exposed to heat shock. It is believed that HSF1 is required for the heat-inducible expression of these genes although HSF2 and HSF4 modulate some of the gene expression.

Analysis of HSF4 binding regions reveals its necessity for gene regulation during development and heat shock response in mouse lenses.

Heat shock transcription factors (HSFs) regulate gene expression in response to heat shock and in physiological conditions. In mammals, HSF1 is required for heat-mediated induction of classic heat shock genes; however, we do not know the molecular mechanisms by which HSF4 regulates gene expression or the biological consequences of its binding to chromatin. Here, we identified that HSF4 binds to various genomic regions, including the introns and distal parts of protein-coding genes in vivo in mouse lenses, and a substantial numbers of the regions were also occupied by HSF1 and HSF2.