Physiological Role of Heat Shock Proteins, Molecular Function and Stress Removal in Fishes

2017 ◽  
pp. 215-246
Author(s):  
Shib Sankar Sen ◽  
Sib Sankr Giri
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Physiological Role ◽  
Molecular Function ◽  
Shock Proteins

scholarly journals The Role ofα-Synuclein and LRRK2 in Tau Phosphorylation

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Fumitaka Kawakami ◽  
Takafumi Ichikawa
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Experimental Evidence ◽  
Physiological Role ◽  
Tau Phosphorylation ◽  
Therapeutic Strategies ◽  
Tau Pathology ◽  
Shock Proteins ◽  
Considerable Body

There is now a considerable body of experimental evidence that Parkinson’s disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role ofα-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition ofα-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

ATPase inhibition by omeprazole reveals role of heat shock proteins on testicular torsion

Andrologia ◽  
2020 ◽  
Author(s):  
Cengiz Güney ◽  
Kübra Açıkalın Coşkun ◽  
Yusuf Tutar
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Testicular Torsion ◽  
Shock Proteins ◽  
Atpase Inhibition

Role of heat shock proteins in the formation of stress resistance in different animal strains

1994 ◽  
Vol 118 (1) ◽  
pp. 689-691 ◽  
Author(s):  
E. V. Malysheva ◽  
A. V. Zamotrinskii ◽  
I. Yu. Malyshev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Resistance ◽  
Shock Proteins ◽  
Animal Strains

The Unique Role of Heat Shock Proteins in Infections

2020 ◽  
pp. 27-51
Author(s):  
Bernd Schoel ◽  
Stefan H. E. Kaufmann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Unique Role ◽  
Shock Proteins

The Presence and Role of Heat- Shock Proteins in Creeping Bentgrass

2000 ◽  
Author(s):  
Dongfang Wang ◽  
Dawn Luthe ◽  
Jeffrey Krans ◽  
Sang Park
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Creeping Bentgrass ◽  
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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