scholarly journals A comparative analysis of Heat Shock Factor 1 in Cancer

2021 ◽  
Author(s):  
Shouhartha Choudhury
Keyword(s):  
Comparative Analysis ◽  
Heat Shock ◽  
Cancer Immunotherapy ◽  
Homo Sapiens ◽  
Current Knowledge ◽  
Analysis Data ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Bioinformatics Pipeline ◽  
Organism Growth

Abstract The heat shock factor 1 (HSF1) is a DNA-binding factor that has responses under proteotoxic stress is well-known as an HSF. Heat shock factor 1 is a unique regulator that coordinates chaperone expression to enhance organism growth. Specifically, HSF’s drive transcriptional strategy is apparent from the HSP’s and promotes cell viability. A recent study supported the HSF1 coordinated with different cancer and robust in cancer immunotherapy. In this research, I designed to genome-wide analysis of HSF1 and its family in mammals. A comparative analysis of HSF’s is mandatory to explore functions and immunogenic mechanisms involved with HSP’s in organisms. Therefore, I performed a bioinformatics pipeline and tools to the current knowledge of HSF’s in two different organisms. This application can enhance in a significant way to study particular HSF’s in discrete organisms. My finding data demonstrated the number of HSF1 and their family in Homo sapiens and Mus musculus. The conserved domain, motifs, phylogeny, chromosome location, gene network, and expression analysis documented the HSF1 associated with cancer. The analysis data concluded the HSF1 is impact in various cancers and a signature of cancer immunotherapy.

A Novel Triazole Nucleoside Suppresses Prostate Cancer Cell Growth by Inhibiting Heat Shock Factor 1 and Androgen Receptor

2015 ◽  
Vol 15 (10) ◽  
pp. 1333-1340 ◽  
Author(s):  
Yi Xia ◽  
Menghua Wang ◽  
Eliana Beraldi ◽  
Mei Cong ◽  
Amina Zoubeidi ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Androgen Receptor ◽  
Heat Shock ◽  
Cell Growth ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Cancer Cell Growth

scholarly journals Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1.

1994 ◽  
Vol 269 (51) ◽  
pp. 32272-32278
Author(s):  
T W Fawcett ◽  
S L Sylvester ◽  
K D Sarge ◽  
R I Morimoto ◽  
N J Holbrook
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

scholarly journals Phosphorylation of Serine 303 Is a Prerequisite for the Stress-Inducible SUMO Modification of Heat Shock Factor 1

2003 ◽  
Vol 23 (8) ◽  
pp. 2953-2968 ◽  
Author(s):  
Ville Hietakangas ◽  
Johanna K. Ahlskog ◽  
Annika M. Jakobsson ◽  
Maria Hellesuo ◽  
Niko M. Sahlberg ◽  
...  
Keyword(s):  
Heat Shock ◽  
Phosphorylation Site ◽  
Stress Granules ◽  
Heat Shock Factor ◽  
Transcriptional Level ◽  
Heat Shock Factor 1 ◽  
Protection Mechanism ◽  
Sumo Modification

ABSTRACT The heat shock response, which is accompanied by a rapid and robust upregulation of heat shock proteins (Hsps), is a highly conserved protection mechanism against protein-damaging stress. Hsp induction is mainly regulated at transcriptional level by stress-inducible heat shock factor 1 (HSF1). Upon activation, HSF1 trimerizes, binds to DNA, concentrates in the nuclear stress granules, and undergoes a marked multisite phosphorylation, which correlates with its transcriptional activity. In this study, we show that HSF1 is modified by SUMO-1 and SUMO-2 in a stress-inducible manner. Sumoylation is rapidly and transiently enhanced on lysine 298, located in the regulatory domain of HSF1, adjacent to several critical phosphorylation sites. Sumoylation analyses of HSF1 phosphorylation site mutants reveal that specifically the phosphorylation-deficient S303 mutant remains devoid of SUMO modification in vivo and the mutant mimicking phosphorylation of S303 promotes HSF1 sumoylation in vitro, indicating that S303 phosphorylation is required for K298 sumoylation. This finding is further supported by phosphopeptide mapping and analysis with S303/7 phosphospecific antibodies, which demonstrate that serine 303 is a target for strong heat-inducible phosphorylation, corresponding to the inducible HSF1 sumoylation. A transient phosphorylation-dependent colocalization of HSF1 and SUMO-1 in nuclear stress granules provides evidence for a strictly regulated subnuclear interplay between HSF1 and SUMO.

THE ROLE OF HEAT SHOCK FACTOR-1 IN LPS MEDIATED CARDIAC CONTRACTILE FUNCTION.

Shock ◽  
2003 ◽  
Vol 19 (Supplement) ◽  
pp. 80
Author(s):  
Jean D. White ◽  
J. W. Horton
Keyword(s):  
Heat Shock ◽  
Contractile Function ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Cardiac Contractile Function ◽  
Cardiac Contractile

scholarly journals Prognostic value of peritumoral heat-shock factor-1 in patients receiving resection of hepatocellular carcinoma

2013 ◽  
Vol 109 (6) ◽  
pp. 1648-1656 ◽  
Author(s):  
J-B Zhang ◽  
K Guo ◽  
H-C Sun ◽  
X-D Zhu ◽  
B Zhang ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Heat Shock ◽  
Prognostic Value ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1
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