Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells

1993 ◽  
Vol 339 (1289) ◽  
pp. 327-333 ◽  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Stress Proteins ◽  
Elevated Temperatures ◽  
Metabolic Stress ◽  
Hsp 70 ◽  
Degree Of Protection ◽  
Stressed Cells ◽  
Shock Proteins

In response to either elevated temperatures or several other metabolic insults, cells from all organisms respond by increasing the expression of so-called heat shock proteins (hsp or stress proteins). In general, the stress response appears to represent a universal cellular defence mechanism. The increased expression and accumulation of the stress proteins provides the cell with an added degree of protection. Studies over the past few years have revealed a role for some of the stress proteins as being intimately involved in protein maturation. Members of the hsp 70 family, distributed throughout various intracellular compartments, interact transiently with other proteins undergoing synthesis, translocation, or higher ordered assembly. Although not yet proven, it has been suggested that members of the hsp 70 family function to slow down or retard the premature folding of proteins in the course of synthesis and translocation. Yet another family of stress proteins, the hsp 60 or GroEL proteins (chaperonins), appear to function as catalysts of protein folding. Here I discuss the role of those stress proteins functioning as molecular chaperones, both within the normal cell and in the cell subjected to metabolic stress.

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.

Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance

2002 ◽  
Vol 92 (5) ◽  
pp. 2177-2186 ◽  
Author(s):  
Kevin C. Kregel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Stress Proteins ◽  
Elevated Temperatures ◽  
Physiological Stress ◽  
Critical Role ◽  
Cellular Damage ◽  
Modifying Factors ◽  
Shock Proteins

Cells from virtually all organisms respond to a variety of stresses by the rapid synthesis of a highly conserved set of polypeptides termed heat shock proteins (HSPs). The precise functions of HSPs are unknown, but there is considerable evidence that these stress proteins are essential for survival at both normal and elevated temperatures. HSPs also appear to play a critical role in the development of thermotolerance and protection from cellular damage associated with stresses such as ischemia, cytokines, and energy depletion. These observations suggest that HSPs play an important role in both normal cellular homeostasis and the stress response. This mini-review examines recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging.

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

Heat shock proteins: Molecular chaperones

1991 ◽  
Vol 19 (4) ◽  
pp. 166-172 ◽  
Author(s):  
Najma Ali ◽  
Naheed Banu
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Shock Proteins

scholarly journals Induction of mitochondrial heat shock proteins and mitochondrial biogenesis in endothelial cells upon acute methylglyoxal stress: Evidence for hormetic autofeedback

2021 ◽  
Author(s):  
Ruben Bulkescher ◽  
Thomas Fleming ◽  
Claus Rodemer ◽  
Rebekka Medert ◽  
Marc Freichel ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mitochondrial Biogenesis ◽  
Metabolic Flux ◽  
Metabolic Stress ◽  
Oxidative Capacity ◽  
Mitochondrial Proteins ◽  
Shock Proteins

Increased metabolic flux produces potentially harmful side-products, such as reactive dicarbonyl and oxygen species. The reactive dicarbonly methylglyoxal (MG) can impair oxidative capacity, which is downregulated in type 2 diabetes. Heat shock proteins (HSPs) of subfamily A (Hsp70s) promote ATP-dependent processing of damaged proteins during MG exposure which also involve mitochondrial proteins. Since the protection of mitochondrial proteins could promote higher production of reactive metabolites due to increased substrate flux, tight regulation of HspA-mediated protein handling is important. We hypothesized that stress-inducible HspAs (HspA1A/HspA1B) are pivotal for maintaining mitochondrial biogenesis during acute MG-stress. To analyze the role of stress-inducible HspA1A/HspA1B for maintenance of mitochondrial homeostasis during acute MG exposure, we knocked out HSPA1A/HSPA1B in mouse endothelial cells. HSPA1A/HSPA1B KO cells showed upregulation of the mitochondrial chaperones HspA9 (mitochondrial Hsp70/mortalin) and HspD1 (Hsp60) as well as induction of mitochondrial biogenesis upon MG exposure. Increased mitochondrial biogenesis was reflected by elevated mitochondrial branching, total count and area as well as by upregulation of mitochondrial proteins and corresponding transcription factors. Our findings suggest that mitochondrial HspA9 and HspD1 promote mitochondrial biogenesis during acute MG stress, which is counterregulated by HspA1A/HspA1B to prevent mitochondrial overstimulation and to maintain balanced oxidative capacity under metabolic stress conditions. These data support an important role of HSPs in MG-induced hormesis.

scholarly journals Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018 ◽  
Vol 19 (9) ◽  
pp. 2603 ◽  
Author(s):  
Claudia Campanella ◽  
Andrea Pace ◽  
Celeste Caruso Bavisotto ◽  
Paola Marzullo ◽  
Antonella Marino Gammazza ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Protein Misfolding ◽  
Point Of View ◽  
Toxic Species ◽  
Shock Proteins

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60, Hsp70 and Hsp90. The role of these proteins in AD is highlighted from a biological point of view. Pharmacological targeting of such HSPs with inhibitors or regulators is also discussed.

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