Families of heat shock proteins and their role in response to exercise

Journal Title: Antropomotoryka. Journal of Kinesiology and Exercise Sciences - Year 2011, Vol 21, Issue 54

Abstract

Heat shock proteins (HSP) are important effectors of stress response in all living bodies. They are extraordinarily phylogenetically conservative since they have not changed their structure for three billion years of evolution. These proteins do not only constitute a new universal system of protecting cells from external effects but they also modulate a number of reactions under non-stress conditions, such as DNA replication and transcription and proteolysis. They are typically divided into 7 families, whose names refer to their average molecular mass. Apart from the stressors such as environmental stress or pathophysiological conditions, physical exercise is another factor which induces HSP synthesis in cells. Elevated aerobic metabolism, which is typical of physical exercise, leads to oxidative stress in muscle cells and other cells in body organs. In order to protect tissues from harmful effects of reactive forms of oxygen and nitrogen, endogenous protective mechanisms are initiated, which activate antioxidative enzymes, non-enzymatic antioxidants and heat shock proteins which belong to the families of HSP27 and HSP70 (HSP72 and HSP73). Intensification of synthesis of heat shock proteins observed after physical exercise depends mainly on its intensity and the type of muscle tissues activated during the exercise. Finding the mechanism of intensified synthesis of these proteins will allow for creation of new very interesting research areas. Exploration of these areas will improve understanding of sport physiology and biochemistry at the molecular level.

Authors and Affiliations

Wanda Pilch, Anna Piotrowska

Keywords

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  • EP ID EP60230
  • DOI -
  • Views 70
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How To Cite

Wanda Pilch, Anna Piotrowska (2011). Families of heat shock proteins and their role in response to exercise. Antropomotoryka. Journal of Kinesiology and Exercise Sciences, 21(54), 121-130. https://europub.co.uk/articles/-A-60230