Hyperthermic intraperitoneal chemotherapy leads to an anticancer immune response via exposure of cell surface heat shock protein 90

Oncogene ◽  
2015 ◽  
Vol 35 (2) ◽  
pp. 261-268 ◽  
Author(s):  
B Zunino ◽  
C Rubio-Patiño ◽  
E Villa ◽  
O Meynet ◽  
E Proics ◽  
...  
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Intraperitoneal Chemotherapy ◽  
Hyperthermic Intraperitoneal Chemotherapy ◽  
Heat Shock Protein 90 ◽  
Surface Heat

Heat shock protein 90 is a stress and immune response gene in the giant spiny frog Quasipaa spinosa

2017 ◽  
Vol 83 (2) ◽  
pp. 251-258 ◽  
Author(s):  
Shu Miao-An ◽  
Tu Dan-Dan ◽  
Zhang Pan ◽  
Long Chen ◽  
Gu Wen-Bin ◽  
...  
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Immune Response Gene ◽  
Response Gene

scholarly journals Influenza A Virus Induces Autophagy by Its Hemagglutinin Binding to Cell Surface Heat Shock Protein 90AA1

2020 ◽  
Vol 11 ◽  
Author(s):  
Xingbo Wang ◽  
Tuyuan Zheng ◽  
Lulu Lin ◽  
Yina Zhang ◽  
Xiran Peng ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Influenza A Virus ◽  
Influenza A ◽  
Surface Heat

Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide

2004 ◽  
Vol 32 (4) ◽  
pp. 636-639 ◽  
Author(s):  
M. Triantafilou ◽  
K. Triantafilou
Keyword(s):  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Surface Receptors ◽  
Innate Recognition ◽  
Shock Proteins

Mammalian responses to bacterial LPS (lipopolysaccharide) from the outer membrane of Gram-negative bacteria can lead to an uncontrolled inflammatory response that can be deadly for the host. It has been shown that the innate immune system employs at least three cell surface receptors, CD14, TLR4 (Toll-like receptor 4) and MD-2, in order to recognize bacterial LPS. In our previous work we have found that Hsps (heat-shock proteins) are also involved in the innate recognition of bacterial products. Their presence on the cell surface, as well as their involvement in the innate recognition process, are poorly understood. In the present study we have investigated the association of TLR4 with Hsp70 and Hsp90 following LPS stimulation, both on the cell surface and intracellularly. Our results show that Hsp70 and Hsp90 form a cluster with TLR4 within lipid microdomains following LPS stimulation. In addition, Hsp70 and Hsp90 seem to be involved in TLR4/LPS trafficking and targeting to the Golgi apparatus, since upon LPS stimulation we found that both Hsps are targeted to the Golgi along with TLR4. The present study sheds new light into the involvement of Hsps in the innate immune response.

scholarly journals Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells

2008 ◽  
Vol 14 (3) ◽  
pp. 321-327 ◽  
Author(s):  
Cristina Cid ◽  
Ignacio Regidor ◽  
Pedro D. Poveda ◽  
Alberto Alcazar
Keyword(s):  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Neuroblastoma Cells ◽  
Heat Shock Protein 90 ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma

Glycyrrhizin effects rat hepatocytes via the reduction of heat shock protein 90 expression

2001 ◽  
Vol 120 (5) ◽  
pp. A357-A357
Author(s):  
T YOH ◽  
T NAKASHIMA ◽  
Y SUMIDA ◽  
Y KAKISAKA ◽  
H ISHIKAWA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Rat Hepatocytes
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