scholarly journals Exercise, heat shock proteins and insulin resistance

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160529 ◽  
Author(s):  
Ashley E. Archer ◽  
Alex T. Von Schulze ◽  
Paige C. Geiger
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Metabolic Effects ◽  
Diabetic Patients ◽  
Alcoholic Fatty Liver ◽  
Insulin Resistant ◽  
Exercise Induced ◽  
Shock Proteins

Best known as chaperones, heat shock proteins (HSPs) also have roles in cell signalling and regulation of metabolism. Rodent studies demonstrate that heat treatment, transgenic overexpression and pharmacological induction of HSP72 prevent high-fat diet-induced glucose intolerance and skeletal muscle insulin resistance. Overexpression of skeletal muscle HSP72 in mice has been shown to increase endurance running capacity nearly twofold and increase mitochondrial content by 50%. A positive correlation between HSP72 mRNA expression and mitochondrial enzyme activity has been observed in human skeletal muscle, and HSP72 expression is markedly decreased in skeletal muscle of insulin resistant and type 2 diabetic patients. In addition, decreased levels of HSP72 correlate with insulin resistance and non-alcoholic fatty liver disease progression in livers from obese patients. These data suggest the targeted induction of HSPs could be a therapeutic approach for preventing metabolic disease by maintaining the body's natural stress response. Exercise elicits a number of metabolic adaptations and is a powerful tool in the prevention and treatment of insulin resistance. Exercise training is also a stimulus for increased HSP expression. Although the underlying mechanism(s) for exercise-induced HSP expression are currently unknown, the HSP response may be critical for the beneficial metabolic effects of exercise. Exercise-induced extracellular HSP release may also contribute to metabolic homeostasis by actively restoring HSP72 content in insulin resistant tissues containing low endogenous levels of HSPs. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

scholarly journals Overload Induced Heat Shock Proteins (HSPs), MAPK and miRNA (miR-1 and miR133a) Response in Insulin-Resistant Skeletal Muscle

2013 ◽  
Vol 31 (2-3) ◽  
pp. 219-229 ◽  
Author(s):  
Anjaiah Katta ◽  
Srinivasarao Thulluri ◽  
Nandini D.P.K. Manne ◽  
Hari S. Addagarla ◽  
Ravikumar Arvapalli ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Insulin Resistant ◽  
Shock Proteins

scholarly journals Microwave hyperthermia treatment increases heat shock proteins in human skeletal muscle * COMMENTARY

2007 ◽  
Vol 41 (7) ◽  
pp. 453-455 ◽  
Author(s):  
Y. Ogura ◽  
H. Naito ◽  
T. Tsurukawa ◽  
N. Ichinoseki-Sekine ◽  
N. Saga ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Human Skeletal Muscle ◽  
Hyperthermia Treatment ◽  
Shock Proteins ◽  
Microwave Hyperthermia

scholarly journals Preservation of skeletal muscle by the heat shock proteins following frostbite injury

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Ruben Mestril ◽  
Colin Schweigert ◽  
Jason Batey ◽  
Tomas Liskutin ◽  
John Baldwin
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Role of Heat Shock Proteins in Skeletal Muscle

10.5772/47815 ◽  
2012 ◽  
Author(s):  
Thiago Gomes ◽  
Sofia Pizzato ◽  
Mirna Stela ◽  
Paulo Ivo Homem de Bittencourt Jr.
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

Heat shock proteins and exercise: a primer

2008 ◽  
Vol 33 (5) ◽  
pp. 1050-1075 ◽  
Author(s):  
Earl G. Noble ◽  
Kevin J. Milne ◽  
C.W. James Melling
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ion Channel ◽  
The Other ◽  
Cellular Environment ◽  
Shock Proteins ◽  
Fertile Area ◽  
Area Of Study

Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review is to introduce the reader to the major HSP families, the control of their expression, and some of their biologic functions, specifically with respect to the influence of exercise. Moreover, as the first in a series of reviews from a common symposium, we will briefly introduce the concepts presented by the other authors, which include the effects of different exercise paradigms on skeletal muscle HSPs in the adult and aged systems, HSPs as regulators of inflammation, and the ion channel stabilizing effects of HSPs.

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.

scholarly journals Apelin and APJ regulation in adipose tissue and skeletal muscle of type 2 diabetic mice and humans

2010 ◽  
Vol 298 (6) ◽  
pp. E1161-E1169 ◽  
Author(s):  
Cédric Dray ◽  
Cyrille Debard ◽  
Jennifer Jager ◽  
Emmanuel Disse ◽  
Danièle Daviaud ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Adipose Tissue ◽  
Receptor Expression ◽  
Diabetic Patients ◽  
Mrna Levels ◽  
Type 2 Diabetic Patients ◽  
Insulin Resistant ◽  
Type 2 Diabetic

Apelin, an adipocyte-secreted factor upregulated by insulin, is increased in adipose tissue (AT) and plasma with obesity. Apelin was recently identified as a new player in the control of glucose homeostasis. However, the regulation of apelin and APJ (apelin receptor) expression in skeletal muscle in relation to insulin resistance or type 2 diabetes is not known. Thus we studied apelin and APJ expression in AT and muscle in different mice models of obesity and in type 2 diabetic patients. In insulin-resistant high-fat (HF)-fed mice, apelin and APJ expression were increased in AT compared with control. This was not the case in AT of highly insulin-resistant db/ db mice. In skeletal muscle, apelin expression was similar in control and HF-fed mice and decreased in db/ db mice. APJ expression was decreased in both HF-fed and db/ db mice. Control subjects and type 2 diabetic patients were subjected to a hyperinsulinemic-euglycemic clamp, and tissues biopsies were obtained before and at the end of the clamp. There was no significant difference in basal apelin and APJ expression in AT and muscle between control and diabetic patients. However, apelin plasma levels were significantly increased in diabetic patients. During the clamp, hyperinsulinemia increased apelin and APJ expression in AT of control but not in diabetic subjects. In muscle, only APJ mRNA levels were increased in control but also in diabetic patients. Taken together, these data show that apelin and APJ expression in mice and humans is regulated in a tissue-dependent manner and according to the severity of insulin resistance.

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