HSP70 and lysosomal storage disorders: novel therapeutic opportunities

2010 ◽  
Vol 38 (6) ◽  
pp. 1479-1483 ◽  
Author(s):  
Nikolaj H.T. Petersen ◽  
Thomas Kirkegaard
Keyword(s):  
Heat Shock ◽  
Stress Responses ◽  
Molecular Chaperone ◽  
Heat Shock Protein 70 ◽  
Physiological Stress ◽  
Lysosomal Storage ◽  
Catabolic Enzymes ◽  
Chaperone Hsp70 ◽  
Storage Disorders ◽  
Novel Therapeutic

Lysosomes, with their arsenal of catabolic enzymes and crucial metabolic housekeeping functions are experiencing a revived research interest after having lived a rather quiet life for the last few decades. With the discovery of the interaction of the lysosomes with another ancient component of cellular homoeostasis, the molecular chaperone HSP70 (heat-shock protein 70), the stage seems set for further discoveries of the mechanisms regulating cellular and physiological stress responses to otherwise detrimental challenges.

scholarly journals Effect of Sex and Breed on HSPA1A, Blood Stress Indicators and Meat Quality of Lambs

Animals ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1514
Author(s):  
Thuthuzelwa Stempa ◽  
Graeme Bradley
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Meat Quality ◽  
Heat Shock Protein 70 ◽  
Physiological Stress ◽  
Quality Attributes ◽  
Stress Indicators ◽  
Male And Female ◽  
Physiological Stress Response

The objective of this study was to examine sex and breed effects on heat shock protein 70 (HSPA1A), blood stress indicators and meat quality attributes of lambs. A hundred male and female lambs from the Dorper (n = 50) and Merino (n = 50) breeds were used in this study. Breed and sex had a significant (p < 0.05) effect on the levels of plasma HSPA1A and lactate; where the Merino lambs had higher levels than Dorper. The female lambs had higher levels of plasma HSPA1A than male lambs. Significant sex and breed interactions (p < 0.05) on the levels of plasma HSPA1A were seen. Females had higher (p < 0.05) pHu than males. Dorper lambs had higher (p < 0.05) pH45, meat lightness, thawing loss and tougher meat the Merino breed. Significant correlations were found amongst plasma stress indicators and meat quality attributes. The results indicate that female lambs were more stressed by the pre-slaughter period than males, while the Merino had a higher physiological stress response compared to the Dorper. However, the Dorper breed produced tougher meat.

scholarly journals Molecular chaperone heat shock protein 70 participates in the labile phase of the development of behavioural sensitization induced by a single morphine exposure in mice

2013 ◽  
Vol 16 (3) ◽  
pp. 647-659 ◽  
Author(s):  
Wang-Jun Qin ◽  
Yan-Ting Wang ◽  
Min Zhang ◽  
Rui-Ting Wen ◽  
Qing Liu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 70 ◽  
De Novo ◽  
Behavioural Plasticity ◽  
Protein Synthesis Inhibitor ◽  
Morphine Injection ◽  
Behavioural Sensitization

Abstract De-novo protein synthesis is required in the development of behavioural sensitization. A prior screening test from our laboratory has implicated heat shock protein 70 (Hsp70) as one of the proteins required in this behavioural plasticity. Thus, this study was designed to extend our understanding of the role of Hsp70 in the development of behavioural sensitization induced by a single morphine exposure in mice. First, by employing transcription inhibitor actinomycin D (AD) and protein synthesis inhibitor cycloheximide (CHX), we identified a protein synthesis-dependent labile phase (within 4 h after the first morphine injection) in the development of behavioural sensitization to a single morphine exposure. Second, Hsp70 protein expression in the nucleus accumbens correlated positively with locomotor responses of sensitized mice and, more importantly, the expression of Hsp70 increased within 1 h after the first morphine injection. Third, AD and CHX both prevented expression of Hsp70 and disrupted the development of the single morphine induced behavioural sensitization, which further implied Hsp70 was highly associated with behavioural sensitization. Finally, the selective Hsp70 inhibitor pifithrin-µ (PES) i.c.v. injected in mice prevented the development of behavioural sensitization and, critically, this inhibitory effect occurred only when PES was given within 1 h after the first morphine injection, which was within the labile phase of the development period. Taken together, we draw the conclusion that Hsp70 is crucially involved in the labile phase of the development of behavioural sensitization induced by a single morphine exposure, probably functioning as a molecular chaperone.

scholarly journals Adenosine Receptor and Its Downstream Targets, Mod(mdg4) and Hsp70, Work as a Signaling Pathway Modulating Cytotoxic Damage in Drosophila

2021 ◽  
Vol 9 ◽  
Author(s):  
Yu-Hsien Lin ◽  
Houda Ouns Maaroufi ◽  
Lucie Kucerova ◽  
Lenka Rouhova ◽  
Tomas Filip ◽  
...  
Keyword(s):  
Heat Shock ◽  
Stress Responses ◽  
Heat Shock Protein 70 ◽  
Mutant Huntingtin ◽  
Stress Reactions ◽  
Downstream Targets ◽  
Tissue Protection ◽  
Signaling Mechanisms ◽  
Mutant Huntingtin Protein

Adenosine (Ado) is an important signaling molecule involved in stress responses. Studies in mammalian models have shown that Ado regulates signaling mechanisms involved in “danger-sensing” and tissue-protection. Yet, little is known about the role of Ado signaling in Drosophila. In the present study, we observed lower extracellular Ado concentration and suppressed expression of Ado transporters in flies expressing mutant huntingtin protein (mHTT). We altered Ado signaling using genetic tools and found that the overexpression of Ado metabolic enzymes, as well as the suppression of Ado receptor (AdoR) and transporters (ENTs), were able to minimize mHTT-induced mortality. We also identified the downstream targets of the AdoR pathway, the modifier of mdg4 (Mod(mdg4)) and heat-shock protein 70 (Hsp70), which modulated the formation of mHTT aggregates. Finally, we showed that a decrease in Ado signaling affects other Drosophila stress reactions, including paraquat and heat-shock treatments. Our study provides important insights into how Ado regulates stress responses in Drosophila.

Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1

1999 ◽  
Vol 55 (6) ◽  
pp. 1234-1236 ◽  
Author(s):  
Bingdong Sha ◽  
Douglas Cyr
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Atpase Activity ◽  
Molecular Chaperone ◽  
Molecular Chaperones ◽  
Heat Shock Protein 70 ◽  
Peptide Binding ◽  
X Ray ◽  
Cellular Processes

Heat-shock protein 70 (Hsp70), one of the major molecular chaperones, has been shown to play a central role in many cellular processes. Heat-shock protein 40 (Hsp40) works as a co-chaperone for Hsp70. Hsp40, bound by unfolded polypeptide, can interact directly with Hsp70 to stimulate the ATPase activity of Hsp70. Hsp40 can also bind to unfolded polypeptides and prevent them from aggregating in vitro, thus acting as an independent molecular chaperone. The S. cerevisiae Hsp40 Sis1 C-terminal peptide-binding domain has been crystallized. The crystals diffract to 2.7 Å and belong to space group P41212 or P43212 with a = 73.63, c = 80.16 Å. The structure determination by the MAD method is under way.

Isolation of a Latimeria menadoensis heat shock protein 70 (Lmhsp70) that has all the features of an inducible gene and encodes a functional molecular chaperone

2009 ◽  
Vol 282 (2) ◽  
pp. 185-196 ◽  
Author(s):  
Keoagile W. Modisakeng ◽  
Meesbah Jiwaji ◽  
Eva-Rachele Pesce ◽  
Jacques Robert ◽  
Chris T. Amemiya ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 70 ◽  
Inducible Gene
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