scholarly journals Heat Shock Proteins and Inflammasomes

2019 ◽  
Vol 20 (18) ◽  
pp. 4508 ◽  
Author(s):  
Pierre Martine ◽  
Cédric Rébé
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Inflammatory Cytokine ◽  
Molecular Pathways ◽  
Multiple Functions ◽  
Danger Signals ◽  
Caspase 1 ◽  
Shock Proteins ◽  
Inflammatory Caspases

Heat shock proteins (HSP) regulate inflammation in many physiological contexts. However, inflammation is a broad process, involving numerous cytokines produced by different molecular pathways with multiple functions. In this review, we focused on the particular role of HSP on the inflammasomes intracellular platforms activated by danger signals and that enable activation of inflammatory caspases, mainly caspase-1, leading to the production of the pro-inflammatory cytokine IL-1β. Interestingly, some members of the HSP family favor inflammasomes activation whereas others inhibit it, suggesting that HSP modulators for therapeutic purposes, must be carefully chosen.

Molecular Pathways Induced by Tumor–Microenvironment Interactions in Myeloma and the Regulatory Role of Heat-Shock Proteins

2009 ◽  
Vol 9 ◽  
pp. S13-S14
Author(s):  
Constantine S. Mitsiades ◽  
Douglas W. McMillin ◽  
Jake Delmore ◽  
Joseph Negri ◽  
Steffen Klippel ◽  
...  
Keyword(s):  
Heat Shock ◽  
Tumor Microenvironment ◽  
Heat Shock Proteins ◽  
Regulatory Role ◽  
Molecular Pathways ◽  
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.

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