scholarly journals Involvement of 70-kD heat-shock proteins in peroxisomal import.

1994 ◽  
Vol 125 (5) ◽  
pp. 1037-1046 ◽  
Author(s):  
P A Walton ◽  
M Wendland ◽  
S Subramani ◽  
R A Rachubinski ◽  
W J Welch
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Import ◽  
Peroxisomal Membrane ◽  
Permeabilized Cell ◽  
Hsp70 Family ◽  
Cell Biol ◽  
Exogenous Hsp70 ◽  
Shock Proteins ◽  
Liver Peroxisomes

This report describes the involvement of 70-kD heat-shock proteins (hsp70) in the import of proteins into mammalian peroxisomes. Employing a microinjection-based assay (Walton, P. A., S. J. Gould, J. R. Feramisco, and S. Subramani. 1992. Mol. Cell Biol. 12:531-541), we demonstrate that proteins of the hsp70 family were associated with proteins being imported into the peroxisomal matrix. Import of peroxisomal proteins could be inhibited by coinjection of antibodies directed against the constitutive hsp70 proteins (hsp73). In a permeabilized-cell assay (Wendland and Subramani. 1993. J. Cell Biol. 120:675-685), antibodies directed against hsp70 proteins were shown to inhibit peroxisomal protein import. Inhibition could be overcome by the addition of exogenous hsp70 proteins. Purified rat liver peroxisomes were shown to have associated hsp70 proteins. The amount of associated hsp70 was increased under conditions of peroxisomal proliferation. Furthermore, proteinase protection assays indicated that the hsp70 molecules were located on the outside of the peroxisomal membrane. Finally, the process of heat-shocking cells resulted in a considerable delay in the import of peroxisomal proteins. Taken together, these results indicate that heat-shock proteins of the cytoplasmic hsp70 family are involved in the import of peroxisomal proteins.

scholarly journals One domain fits all: Using disordered regions to sequester misfolded proteins

2018 ◽  
Vol 217 (4) ◽  
pp. 1173-1175 ◽  
Author(s):  
Edgar E. Boczek ◽  
Simon Alberti
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Adenosine Triphosphate ◽  
Small Heat Shock Proteins ◽  
Misfolded Proteins ◽  
Protein Deposition ◽  
Intrinsically Disordered ◽  
Cell Biol ◽  
Shock Proteins ◽  
Intrinsically Disordered Domain

Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.

Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins

Science ◽  
1992 ◽  
Vol 258 (5081) ◽  
pp. 484-486 ◽  
Author(s):  
S. Nadler ◽  
M. Tepper ◽  
B Schacter ◽  
C. Mazzucco
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp70 Family ◽  
Shock Proteins

scholarly journals Cold and Heat Stress Diversely Alters Both Cauliflower Respiration and Distinct Mitochondrial Proteins Including OXPHOS Components and Matrix Enzymes

2018 ◽  
Author(s):  
Michał Rurek ◽  
Magdalena Czołpińska ◽  
Tomasz Andrzej Pawłowski ◽  
Włodzimierz Krzesiński ◽  
Tomasz Spiżewski
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Protein Import ◽  
Plant Mitochondria ◽  
Complex Model ◽  
Mitochondrial Proteome ◽  
Metabolism Enzymes ◽  
Shock Proteins

Complex proteomic and physiological approaches to study cold and heat stress responses in plant mitochondria are still limited. Variations in the mitochondrial proteome of cauliflower (Brassica oleracea var. botrytis) curds after cold and heat and after stress recovery were assayed by 2D PAGE in relation to respiratory parameters. Quantitative analysis of the mitochondrial proteome revealed numerous stress-affected protein spots. In cold alternative oxidase isoforms were extensively upregulated; major downregulations in the level of photorespiratory enzymes, porine isoforms, oxidative phosphorylation (OXPHOS) and some low-abundant proteins were observed. On the contrary, distinct proteins, including carbohydrate metabolism enzymes, heat-shock proteins, translation, protein import, and OXPHOS components were involved in heat response and recovery. Few metabolic regulations were suggested. Cauliflower plants appeared less susceptible to heat; closed stomata in heat stress resulted in moderate photosynthetic, but only minor respiratory impairments, however photosystem II performance was unaffected. Decreased photorespiration corresponded with proteomic alterations in cold. Our results show that cold and heat stress not only operate in diverse mode (exemplified by cold-specific accumulation of some heat shock proteins), but exert some associations on molecular and physiological levels. This implies more complex model of action of investigated stresses on plant mitochondria.

scholarly journals Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection

2021 ◽  
Vol 22 (17) ◽  
pp. 9366
Author(s):  
Anna Lubkowska ◽  
Waldemar Pluta ◽  
Aleksandra Strońska ◽  
Alicja Lalko
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Viral Replication ◽  
Viral Infection ◽  
Viral Infections ◽  
Therapeutic Potential ◽  
Biological Significance ◽  
Hsp70 Family ◽  
The Stability ◽  
Shock Proteins

Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and bacteria. They are responsible for the correct protein folding, protection of the cell against stressors, presenting immune and inflammatory cytokines; furthermore, they are important factors in regulating cell differentiation, survival and death. Although the biological function of HSPs is to maintain cell homeostasis, some of them can be used by viruses both to fold their proteins and increase the chances of survival in unfavorable host conditions. Folding viral proteins as well as replicating many different viruses are carried out by, among others, proteins from the HSP70 and HSP90 families. In some cases, the HSP70 family proteins directly interact with viral polymerase to enhance viral replication or they can facilitate the formation of a viral replication complex and/or maintain the stability of complex proteins. It is known that HSP90 is important for the expression of viral genes at both the transcriptional and the translational levels. Both of these HSPs can form a complex with HSP90 and, consequently, facilitate the entry of the virus into the cell. Current studies have shown the biological significance of HSPs in the course of infection SARS-CoV-2. A comprehensive understanding of chaperone use during viral infection will provide new insight into viral replication mechanisms and therapeutic potential. The aim of this study is to describe the molecular basis of HSP70 and HSP90 participation in some viral infections and the potential use of these proteins in antiviral therapy.

The Effect of Age on the Synthesis of Two Heat Shock Proteins in the HSP70 Family

1993 ◽  
Vol 48 (2) ◽  
pp. B50-B56 ◽  
Author(s):  
B. Wu ◽  
M. J. Gu ◽  
A. R. Heydari ◽  
A. Richardson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp70 Family ◽  
Shock Proteins ◽  
Effect Of Age

Heat shock proteins in the mechanisms of stress adaptation in Baikal amphipods and palearctic Gammarus lacustris Sars. I. HSP70 family

2010 ◽  
Vol 3 (1) ◽  
pp. 41-49
Author(s):  
Zh. M. Shatilina ◽  
T. P. Pobezhimova ◽  
O. I. Grabel’nykh ◽  
D. S. Bedulina ◽  
M. V. Protopopova ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Adaptation ◽  
Gammarus Lacustris ◽  
Hsp70 Family ◽  
Shock Proteins

scholarly journals Autoantibodies to the constitutive 73-kD member of the hsp70 family of heat shock proteins in systemic lupus erythematosus.

1988 ◽  
Vol 168 (4) ◽  
pp. 1475-1480 ◽  
Author(s):  
S Minota ◽  
B Cameron ◽  
W J Welch ◽  
J B Winfield
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Lupus Erythematosus ◽  
Solid Phase ◽  
Systemic Lupus ◽  
Hsp70 Family ◽  
Hsp70 Protein ◽  
Sds Page ◽  
Shock Proteins

Serum from patients with systemic lupus erythematosus (SLE) frequently contain IgM and IgG autoantibodies to the constitutively expressed 73-kD/pI 5.5 member of the hsp70 family of heat shock proteins, as determined by one-dimensional (SDS-PAGE) and two-dimensional (IEF/SDS-PAGE) immunoblotting, and by solid-phase SLE Ig immunoprecipitation experiments using hsp70 protein-specific mAbs as probes. Autoantibodies to hsp70 also were detected in a minority of sera from patients with other rheumatic or viral diseases, but not in normal sera. These data may provide additional insight into etiologic and pathophysiologic mechanisms in this and related autoimmune disorders.

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