Optimal ligand binding by the recombinant human glucocorticoid receptor and assembly of the receptor complex with heat shock protein 90 correlate with high intracellular ATP levels in Spodoptera frugiperda cells

1997 ◽  
Vol 60 (1-2) ◽  
pp. 1-9 ◽  
Author(s):  
Ganesan Srinivasan ◽  
Jan F.M. Post ◽  
E.Brad Thompson
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Glucocorticoid Receptor ◽  
Ligand Binding ◽  
Spodoptera Frugiperda ◽  
Heat Shock Protein 90 ◽  
Receptor Complex ◽  
Intracellular Atp ◽  
Atp Levels

Determination of the volume changes induced by ligand binding to heat shock protein 90 using high-pressure denaturation

2011 ◽  
Vol 413 (2) ◽  
pp. 171-178 ◽  
Author(s):  
Zigmantas Toleikis ◽  
Piotras Cimmperman ◽  
Vytautas Petrauskas ◽  
Daumantas Matulis
Keyword(s):  
High Pressure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Ligand Binding ◽  
Heat Shock Protein 90 ◽  
Volume Changes

scholarly journals Inhibition of infectious bursal disease virus infection by artificial microRNAs targeting chicken heat-shock protein 90

2012 ◽  
Vol 93 (4) ◽  
pp. 876-879 ◽  
Author(s):  
Weifeng Yuan ◽  
Xinyu Zhang ◽  
Xiaoli Xia ◽  
Huaichang Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Infectious Bursal Disease Virus ◽  
Heat Shock Protein 90 ◽  
Infectious Bursal Disease ◽  
Cellular Receptor ◽  
Receptor Complex ◽  
Rt Pcr ◽  
Transfected Cells ◽  
Bursal Disease

Infectious bursal disease virus (IBDV) causes an important disease in young chickens. Chicken heat-shock protein 90 (cHsp90) has been shown to be a functional component of the cellular receptor complex for IBDV infection. This study demonstrates the inhibitory effect of vector-expressed anti-cHsp90α microRNA (miRNA) on IBDV infection. The reporter vectors pcHsp90α-EGFP and pcHsp90β-EGFP were constructed to facilitate effective miRNA selection. Two anti-cHsp90α and one anti-cHsp90β miRNA-expression vectors were constructed for a stable transfection study. Poly(A)-tailed RT-PCR detected sequence-specific miRNA transcription in transfected cells. Semiquantitative RT-PCR showed inhibition of cHsp90 transcription in transfected cells. A virus-titration assay showed that the anti-cHsp90α miRNA, but not the anti-cHsp90β miRNA, had inhibitory effects on IBDV infection. These results suggest that cHsp90α is a functional component of the cellular receptor complex for IBDV infection, and that anti-cHsp90α miRNA could be used as an anti-IBDV reagent.

Interaction of glucocorticoid receptor with heat shock protein 90 after chronic stress

1996 ◽  
Vol 6 ◽  
pp. 110
Author(s):  
Y. Sasuga ◽  
M. Asakura ◽  
M. Miyamoto ◽  
N. Bodaiji ◽  
J. Imafuku ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Glucocorticoid Receptor ◽  
Chronic Stress ◽  
Heat Shock Protein 90

scholarly journals Heat Shock Protein 90-Dependent (Geldanamycin-Inhibited) Movement of the Glucocorticoid Receptor through the Cytoplasm to the Nucleus Requires Intact Cytoskeleton

1998 ◽  
Vol 12 (12) ◽  
pp. 1903-1913 ◽  
Author(s):  
Mario D. Galigniana ◽  
Jennifer L. Scruggs ◽  
James Herrington ◽  
Michael J. Welsh ◽  
Christin Carter-Su ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Glucocorticoid Receptor ◽  
Heat Shock Protein 90

scholarly journals Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells

2005 ◽  
Vol 79 (8) ◽  
pp. 4557-4567 ◽  
Author(s):  
Jorge Reyes-del Valle ◽  
Salvador Chávez-Salinas ◽  
Fernando Medina ◽  
Rosa M. del Angel
Keyword(s):  
Heat Shock ◽  
Virus Infection ◽  
Heat Shock Protein ◽  
Dengue Virus ◽  
Affinity Chromatography ◽  
Virus Entry ◽  
Heat Shock Protein 90 ◽  
Membrane Microdomains ◽  
Receptor Complex ◽  
Dengue Virus Infection

ABSTRACT Dengue virus requires the presence of an unidentified cellular receptor on the surface of the host cell. By using a recently published affinity chromatography approach, an 84-kDa molecule, identified as heat shock protein 90 (HSP90) by matrix-assisted laser desorption ionization-time of flight mass spectrometry, was isolated from neuroblastoma and U937 cells. Based on the ability of HSP90 (84 kDa) to interact with HSP70 (74 kDa) on the surface of monocytes during lipopolysaccharide (LPS) signaling and evidence that LPS inhibits dengue virus infection, the presence of HSP70 was demonstrated in affinity chromatography eluates and by pull-down experiments. Infection inhibition assays support the conclusion that HSP90 and HSP70 participate in dengue virus entry as a receptor complex in human cell lines as well as in monocytes/macrophages. Additionally, our results indicate that both HSPs are associated with membrane microdomains (lipid rafts) in response to dengue virus infection. Moreover, methyl-β-cyclodextrin, a raft-disrupting drug, inhibits dengue virus infection, supporting the idea that cholesterol-rich membrane fractions are important in dengue virus entry.

Sign in / Sign up

Export Citation Format

Share Document