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 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.

Heat shock proteins: the hsp70 family

1994 ◽  
Vol 50 (11-12) ◽  
pp. 979-986 ◽  
Author(s):  
U. Feige ◽  
B. S. Polla
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp70 Family ◽  
Shock Proteins

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.

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