Abstract
Heat shock proteins (HSPs) are a large family of proteins highly conserved throughout evolution because of their unique cytoprotective properties. Besides assisting protein refolding and regulating proteostasis under stressful conditions, HSPs also play an important role in protecting cells from oxidative stress, inflammation, and apoptosis. Therefore, HSPs are crucial in counteracting the deleterious effects of hyperglycemia in target organs of diabetes vascular complications. Changes in HSP expression have been demonstrated in diabetic complications and functionally related to hyperglycemia-induced cell injury. Moreover, associations between diabetic complications and altered circulating levels of both HSPs and anti-HSPs have been shown in clinical studies. HSPs thus represent an exciting therapeutic opportunity and might also be valuable as clinical biomarkers. However, this field of research is still in its infancy and further studies in both experimental diabetes and humans are required to gain a full understanding of HSP relevance. In this review, we summarize current knowledge and discuss future perspective.
Highlights
Vascular complications are the major causes of morbidity and mortality in people with diabetes (DM)
HSPD1/HSP60 is globally enhanced in diabetic complications, though a reduction of mitochondrial HSPD1/HSP60 has been reported in diabetic retinopathy, suggesting mitochondrial stress resulting in translocation of HSPD1/HSP60 from the mitochondria to the cell membrane/extracellular space where HSPD1/HSP60 can elicit an immune/autoimmune reaction contributing to cell damage
Overall data reported above show that expression of Heat shock proteins (HSPs) is modulated in diabetic complications with preliminary proof of functional relevance; the strength of evidence varies by complication
Summary
Vascular complications are the major causes of morbidity and mortality in people with diabetes (DM). Their underlying mechanisms are not fully understood, advanced glycated end products (AGEs), oxidative stress, and a low-grade inflammation are believed to play a key role in mediating hyperglycemia-induced cell dysfunction and damage [1]. Heat shock proteins (HSPs) are a family of proteins highly conserved throughout evolution because of their key role in cytoprotection. Both pharmacological and genetic modulation of HSP expression has been tested in animal models as a strategy to enhance cytoprotection in the context of DM. We summarize current knowledge of the role of HSP27, HSP47, HSP60, HSP70, and HSP90 in DM complications and discuss the potential clinical relevance
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