scholarly journals Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160521 ◽  
Author(s):  
Adrienne L. Edkins ◽  
John T. Price ◽  
A. Graham Pockley ◽  
Gregory L. Blatch
Keyword(s):  
Chronic Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Critical Role ◽  
Therapeutic Targets ◽  
Theme Issue ◽  
Human Disorders ◽  
Health And Disease ◽  
Shock Proteins ◽  
And Function

Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as molecular chaperones, and play a critical role in maintaining cellular proteostasis by integrating the fundamental processes of protein folding and degradation. HSPs are arguably among the most prominent classes of proteins that have been broadly linked to many human disorders, with changes in their expression profile and/or intracellular/extracellular location now being described as contributing to the pathogenesis of a number of different diseases. Although the concept was initially controversial, it is now widely accepted that HSPs have additional biological functions over and above their role in proteostasis (so-called ‘protein moonlighting’). Most importantly, these new insights are enlightening our understanding of biological processes in health and disease, and revealing novel and exciting therapeutic opportunities. This theme issue draws on therapeutic insights from established research on HSPs in cancer and other non-communicable disorders, with an emphasis on how the intracellular function of HSPs contrasts with their extracellular properties and function, and interrogates their potential diagnostic and therapeutic value to the prevention, management and treatment of chronic diseases. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

scholarly journals Developmental Expression and Functions of the Small Heat Shock Proteins in Drosophila

2018 ◽  
Vol 19 (11) ◽  
pp. 3441 ◽  
Author(s):  
Teresa Jagla ◽  
Magda Dubińska-Magiera ◽  
Preethi Poovathumkadavil ◽  
Małgorzata Daczewska ◽  
Krzysztof Jagla
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Large Family ◽  
Active Role ◽  
Stress Conditions ◽  
Developmental Expression ◽  
Shsp Gene ◽  
Time Specific ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (Hsps) form a large family of evolutionarily conserved molecular chaperones that help balance protein folding and protect cells from various stress conditions. However, there is growing evidence that Hsps may also play an active role in developmental processes. Here, we take the example of developmental expression and function of one class of Hsps characterized by low molecular weight, the small Hsps (sHsps). We discuss recent reports and genome-wide datasets that support vital sHsps functions in the developing nervous system, reproductive system, and muscles. This tissue- and time-specific sHsp expression is developmentally regulated, so that the enhancer sequence of an sHsp gene expressed in developing muscle, in addition to stress-inducible elements, also carries binding sites for myogenic regulatory factors. One possible reason for sHsp genes to switch on during development and in non-stress conditions is to protect vital developing organs from environmental insults.

scholarly journals Are the Effects of Heat on Physiology Due to Heat Shock Proteins?

HortScience ◽  
1996 ◽  
Vol 31 (4) ◽  
pp. 691c-691
Author(s):  
Robert E. Paull ◽  
Chris B. Watkins
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Critical Role ◽  
Chilling Injury ◽  
Heat Treatments ◽  
Adaptation To Heat ◽  
Heat Shock Responses ◽  
Shock Proteins

Production of heat shock proteins (HSP) in response to high temperatures are a highly recognizable feature of plant and animal systems. It is thought that such proteins play a critical role in survival under supraoptimal temperature conditions. The use of heat treatments has been examined extensively, especially for disinfestation of fruit and disease control. Heat treatments can affect physiological responses, such as ethylene production, softening, and other ripening factors, as well as reducing physiological disorders, including chilling injury. HSPs have been implicated in a number of stress responses, but the extent that they are involved, especially in amelioration of chilling injury, is a subject of debate. In a number of cases, heat shock proteins do not appear to be involved, and HSPs do not explain long-term adaptation to heat; other systems for which we do not have models may be at work. Resolution of these issues may require the use of transgenic plants with modified heat shock responses.

scholarly journals Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Arman Kilic ◽  
Kaushik Mandal
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Vascular Endothelial Cell ◽  
Vascular Wall ◽  
Protective Role ◽  
Therapeutic Implications ◽  
Endothelial Cell Surface ◽  
Disease States ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.

scholarly journals Structure and Function of Small Heat Shock Proteins from the Magnetotactic Bacterium Magnetospirillum magneticum AMB-1

2010 ◽  
Vol 67 (12) ◽  
pp. 698-704 ◽  
Author(s):  
Tetsuya ABE ◽  
Shinpei ITO ◽  
Naoya NISHI ◽  
Yoshihiro TSUKADA ◽  
Takuo YASUNAGA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Magnetotactic Bacterium ◽  
Shock Proteins ◽  
And Function ◽  
Magnetospirillum Magneticum

scholarly journals Evolution, structure and function of the small heat shock proteins in plants

1996 ◽  
Vol 47 (3) ◽  
pp. 325-338 ◽  
Author(s):  
Elizabeth R. Waters ◽  
Garrett J. Lee ◽  
Elizabeth Vierling
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Shock Proteins ◽  
And Function
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