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 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 Molecular chaperones and heat shock proteins in atherosclerosis

2012 ◽  
Vol 302 (3) ◽  
pp. H506-H514 ◽  
Author(s):  
Qingbo Xu ◽  
Bernhard Metzler ◽  
Marjan Jahangiri ◽  
Kaushik Mandal
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Mammalian Cells ◽  
Vessel Wall ◽  
Protective Role ◽  
Research Field ◽  
Stressed Cells ◽  
Shock Proteins ◽  
Prevention Of Atherosclerosis

In response to stress stimuli, mammalian cells activate an ancient signaling pathway leading to the transient expression of heat shock proteins (HSPs). HSPs are a family of proteins serving as molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Physiologically, HSPs play a protective role in the homeostasis of the vessel wall but have an impact on immunoinflammatory processes in pathological conditions involved in the development of atherosclerosis. For instance, some members of HSPs have been shown to have immunoregulatory properties and modification of innate and adaptive response to HSPs, and can protect the vessel wall from the disease. On the other hand, a high degree of sequence homology between microbial and mammalian HSPs, due to evolutionary conservation, carries a risk of misdirected autoimmunity against HSPs expressed on the stressed cells of vascular endothelium. Furthermore, HSPs and anti-HSP antibodies have been shown to elicit production of proinflammatory cytokines. Potential therapeutic use of HSP in prevention of atherosclerosis involves achieving optimal balance between protective and immunogenic effects of HSPs and in the progress of research on vaccination. In this review, we update the progress of studies on HSPs and the integrity of the vessel wall, discuss the mechanism by which HSPs exert their role in the disease development, and highlight the potential clinic translation in the research field.

Protective role of TAT-HSP70 after myocardial I/R injury

2017 ◽  
Vol 5 (3) ◽  
pp. 279-284
Author(s):  
Martin A. Meenakshi ◽  
Erik G. Seth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protective Role ◽  
Inflammatory Mechanism ◽  
Myocardial Ischemia Reperfusion Injury ◽  
Myocardial Ischemia Reperfusion ◽  
Shock Proteins

Myocardial ischemia reperfusion injury I/R adversely affects cardiac function. Heat shock proteins (HSPs) are a highly conserved family of proteins with diverse functions expressed by all cells exposed to environmental stress including myocardila injury. We investigated release of small constitutive heat shock proteins (HSPs) from mouse myocardium and the effects of TAT-HSP70 after myocardial I/R via occluding the left coronary artery (LAD). The results support the hypothesis that elevated HSPs in myocardium after ischemia and reperfusion and contributes to the inflammatory mechanism of myocardial functional injury. Further investigation of the significance of HSPs accumulation to the evolution of myocardial injury.

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 Heat shock proteins and exercise adaptations. Our knowledge thus far and the road still ahead

2016 ◽  
Vol 120 (6) ◽  
pp. 683-691 ◽  
Author(s):  
Darren C. Henstridge ◽  
Mark A. Febbraio ◽  
Mark Hargreaves
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Acute Exercise ◽  
Exercise Physiology ◽  
Protective Role ◽  
Protective Mechanisms ◽  
The Road ◽  
Exercise Activity ◽  
Exercise Induced ◽  
Shock Proteins

By its very nature, exercise exerts a challenge to the body's cellular homeostatic mechanisms. This homeostatic challenge affects not only the contracting skeletal muscle but also a number of other organs and results over time in exercise-induced adaptations. Thus it is no surprise that heat shock proteins (HSPs), a group of ancient and highly conserved cytoprotective proteins critical in the maintenance of protein and cellular homeostasis, have been implicated in exercise/activity-induced adaptations. It has become evident that HSPs such as HSP72 are induced or activated with acute exercise or after chronic exercise training regimens. These observations have given scientists an insight into the protective mechanisms of these proteins and provided an opportunity to exploit their protective role to improve health and physical performance. Although our knowledge in this area of physiology has improved dramatically, many questions still remain unanswered. Further understanding of the role of HSPs in exercise physiology may prove beneficial for therapeutic targeting in diseased patient cohorts, exercise prescription for disease prevention, and training strategies for elite athletes.

Sign in / Sign up

Export Citation Format

Share Document