The Role of Heat Shock Factors in Mammalian Spermatogenesis

2017 ◽  
pp. 45-65 ◽  
Author(s):  
Wieslawa Widlak ◽  
Natalia Vydra
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

Role of Heat Shock Factors in Diseases and Immunity

2020 ◽  
Author(s):  
Boopathi Balasubramaniam ◽  
Krishnaswamy Balamurugan
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

scholarly journals The role of class A1 heat shock factors (HSFA1s) in response to heat and other stresses in Arabidopsis

2011 ◽  
Vol 34 (5) ◽  
pp. 738-751 ◽  
Author(s):  
HSIANG-CHIN LIU ◽  
HSIU-TING LIAO ◽  
YEE-YUNG CHARNG
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

scholarly journals Genome-wide identification of heat shock factors and heat shock proteins in response to UV and high intensity light stress in lettuce

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Taehoon Kim ◽  
Shafina Samraj ◽  
Juan Jiménez ◽  
Celina Gómez ◽  
Tie Liu ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Light Stress ◽  
Stress Conditions ◽  
Heat Shock Factors ◽  
Genome Wide Analysis ◽  
Genome Wide ◽  
Shock Proteins ◽  
High Intensity Light

Abstract Background Heat shock factors (Hsfs) and Heat shock proteins (Hsps) belong to an essential group of molecular regulators involved in controlling cellular processes under normal and stress conditions. The role of Hsfs and Hsps is well known in model plant species under diverse stress conditions. While plants Hsfs are vital components of the signal transduction response to maintain cellular homeostasis, Hsps function as chaperones helping to maintain folding of damaged and newly formed proteins during stress conditions. In lettuce (Lactuca sativa), a highly consumed vegetable crop grown in the field and in hydroponic systems, the role of these gene families in response to artificial light is not well characterized. Results Using a genome-wide analysis approach, we identified 32 Hsfs and 22 small heat shock proteins (LsHsps) in lettuce, some of which do not have orthologs in Arabidopsis, poplar, and rice. LsHsp60s, LsHsp90s, and LsHsp100s are highly conserved among dicot and monocot species. Surprisingly, LsHsp70s have three times more members than Arabidopsis and two times more than rice. Interestingly, the lettuce genome triplication did not contribute to the increased number of LsHsp70s genes. The large number of LsHsp70s was the result of genome tandem duplication. Chromosomal distribution analysis shows larger tandem repeats of LsHsp70s genes in Chr1, Chr7, Chr8, and Chr9. At the transcriptional level, some genes of the LsHsfs, LsHsps, LsHsp60s, and LsHsp70s families were highly responsive to UV and high intensity light stress, in contrast to LsHsp90s and LsHsp100s which did not respond to a light stimulus. Conclusions Our genome-wide analysis provides a detailed identification of Hsfs and Hsps in lettuce. Chromosomal location and syntenic region analysis together with our transcriptional analysis under different light conditions provide candidate genes for breeding programs aiming to produce lettuce varieties able to grow healthy under hydroponic systems that use artificial light.

scholarly journals The Role of Heat Shock Factors in Stress-Induced Transcription

2011 ◽  
pp. 21-32 ◽  
Author(s):  
Yue Zhang ◽  
Shiuh-Dih Chou ◽  
Ayesha Murshid ◽  
Thomas L. Prince ◽  
Sheila Schreiner ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

scholarly journals Role of Heat Shock Factors in Stress-Induced Transcription

2017 ◽  
pp. 23-34 ◽  
Author(s):  
Ayesha Murshid ◽  
Thomas L. Prince ◽  
Ben Lang ◽  
Stuart K. Calderwood
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

scholarly journals Clustering of heat-shock factors

2006 ◽  
Vol 395 (1) ◽  
Author(s):  
Johanna K. Björk ◽  
Lea Sistonen
Keyword(s):  
Heat Shock ◽  
Protein Accumulation ◽  
Heat Shock Factors ◽  
Exact Role ◽  
Unfolded Protein ◽  
Proteotoxic Stress ◽  
Trimeric Complex ◽  
Biochemical Journal ◽  
Cellular Defence

Clusterin is a ubiquitous glycoprotein found in most physiological fluids and tissues. Although not fully understood, the function of clusterin seems to be related to its ability to bind a wide variety of molecules. Since clusterin has been found associated with extracellular protein aggregates, a role as a molecular chaperone has been proposed. In this issue of the Biochemical Journal, Le Dréan and colleagues demonstrate an up-regulation of clusterin in neuronal cells exposed to proteotoxic stress that results in unfolded protein accumulation and proteasome impairment, both commonly associated with neurodegenerative diseases. Interestingly, expression of clusterin was found to be regulated by two members of the HSF (heat-shock factor) family, HSF1 and HSF2, which possibly form a trimeric complex on the clusterin promoter. The study proposes clusterin as a player in a cellular defence mechanism against harmful protein accumulation, and highlights the importance of elucidating further the exact role of clusterin and the intriguing interaction between HSF1 and HSF2.

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