scholarly journals Binding of Antigenic Peptide to the Endoplasmic Reticulum-resident Protein gp96/GRP94 Heat Shock Chaperone Occurs in Higher Order Complexes

2001 ◽  
Vol 276 (14) ◽  
pp. 11049-11054 ◽  
Author(s):  
Nora A. Linderoth ◽  
Martha N. Simon ◽  
James F. Hainfeld ◽  
Srin Sastry
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Higher Order ◽  
Antigenic Peptide ◽  
Order Complexes

scholarly journals The Endoplasmic Reticulum-resident Heat Shock Protein Gp96 Activates Dendritic Cells via the Toll-like Receptor 2/4 Pathway

2002 ◽  
Vol 277 (23) ◽  
pp. 20847-20853 ◽  
Author(s):  
Ramunas M. Vabulas ◽  
Sibylla Braedel ◽  
Norbert Hilf ◽  
Harpreet Singh-Jasuja ◽  
Sylvia Herter ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Toll Like Receptor ◽  
Heat Shock Protein Gp96 ◽  
Toll Like Receptor 2

scholarly journals Calreticulin, a Peptide-binding Chaperone of the Endoplasmic Reticulum, Elicits Tumor- and Peptide-specific Immunity

1999 ◽  
Vol 189 (5) ◽  
pp. 797-802 ◽  
Author(s):  
Sreyashi Basu ◽  
Pramod K. Srivastava
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Antigen Processing ◽  
Peptide Binding ◽  
Cd8 T Cell ◽  
T Cell Response ◽  
Specific Immunity ◽  
Per Se

Calreticulin (CRT), a peptide-binding heat shock protein (HSP) of the endoplasmic reticulum (ER), has been shown previously to associate with peptides transported into the ER by transporter associated with antigen processing (Spee, P., and J. Neefjes. 1997. Eur. J. Immunol. 27: 2441–2449). Our studies show that CRT preparations purified from tumors elicit specific immunity to the tumor used as the source of CRT but not to an antigenically distinct tumor. The immunogenicity is attributed to the peptides associated with the CRT molecule and not to the CRT molecule per se. It is further shown that CRT molecules can be complexed in vitro to unglycosylated peptides and used to elicit peptide-specific CD8+ T cell response in spite of exogenous administration. These characteristics of CRT closely resemble those of HSPs gp96, hsp90, and hsp70, although CRT has no apparent structural homologies to them.

Mimicking a conformational B cell epitope of the heat shock protein PfHsp70-1 antigen of Plasmodium falciparum using a multiple antigenic peptide

2000 ◽  
Vol 22 (11) ◽  
pp. 535-543 ◽  
Author(s):  
Myoura Huynh Quan Dat ◽  
Charlotte Behr ◽  
Helene Jouin ◽  
Francoise Baleux ◽  
Odile Mercereau-Puijalon ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
B Cell ◽  
Cell Epitope ◽  
Antigenic Peptide ◽  
Multiple Antigenic Peptide ◽  
B Cell Epitope

scholarly journals P0015SIRT2 REGULATES CISPLATIN-INDUCED ENDOPLASMIC RETICULUM STRESS THROUGH HEAT SHOCK FACTOR 1 DEACETYLATION

2020 ◽  
Vol 35 (Supplement_3) ◽  
Author(s):  
Woong Park ◽  
Hyeongwan Kim ◽  
Yujin Jung ◽  
Kyung Pyo Kang ◽  
Won Kim
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Er Stress ◽  
Knockout Mice ◽  
Malignant Tumors ◽  
Heat Shock Factor ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Heat Shock Factor 1 ◽  
Caspase 12

Abstract Background and Aims Nephrotoxicity is an important cisplatin-induced adverse reaction and restricts the use of cisplatin to treat malignant tumors. Endoplasmic reticulum (ER) stress is caused by the accumulation of misfolded proteins, and is induced by cisplatin in kidneys. SIRT2 nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase is a member of the sirtuin family, but its role in cisplatin-induced ER stress remains unclear. Method To investigate the effect of SIRT2 on cisplatin-induced ER stress using SIRT2 knockout mice and human proximal tubular epithelial cells (HK-2 cells). We treated cisplatin (20 µg/mL) or induced by intraperitoneal injection of cisplatin (20 mg/kg) and evaluated the changes of ER stress and its signal mechanism. Results Cisplatin administration was found to significantly increase the expressions of PRKR-like ER kinase (PERK), phosphorylation of eukaryotic translation initiation factor 2α (eIF2α), and the C/EBP homologous protein (CHOP) and caspase-12 in the kidneys of SIRT2-wild type mice. However, cisplatin-induced increases in the expressions of p-PERK, p-eIF2α, CHOP and, caspase-12 were diminished in kidneys of SIRT2 knockout mice. In vitro, cisplatin significantly increased the expressions of p-PERK, p-eIF2α, CHOP, and caspase-12 in HK-2 cells. When the effect of SIRT2 on cisplatin-induced ER stress was evaluated using SIRT2-siRNA (ON-TARGET plus human SIRT2 siRNA) or the SIRT2 inhibitors, AGK2 and AK1, knockdown or inhibition of SIRT2 significantly attenuated the cisplatin-induced protein expression of p-PERK, p-eIF2α, CHOP, and caspase-12. Immunoprecipitation studies showed SIRT2 bound physically to heat shock factor (HSF)1 and that HSF1 acetylation was significantly increased by cisplatin. In addition, knockdown of SIRT2 increased cisplatin-induced HSF1 acetylation and increased the expression of heat shock protein (HSP)70. Conclusion These observations suggest that suppression of SIRT2 ameliorates cisplatin-induced ER stress by increasing HSF1 acetylation and HSP expression.

scholarly journals Profiling the Expression of Endoplasmic Reticulum Stress Associated Heat Shock Proteins in Animal Epilepsy Models

Neuroscience ◽  
2020 ◽  
Vol 429 ◽  
pp. 156-172 ◽  
Author(s):  
Marta Nowakowska ◽  
Fabio Gualtieri ◽  
Eva-Lotta von Rüden ◽  
Florian Hansmann ◽  
Wolfgang Baumgärtner ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Endoplasmic Reticulum Stress ◽  
Epilepsy Models ◽  
Shock Proteins

scholarly journals Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (ER) Aminopeptidase 2

2015 ◽  
Vol 290 (43) ◽  
pp. 26021-26032 ◽  
Author(s):  
Anastasia Mpakali ◽  
Petros Giastas ◽  
Nikolas Mathioudakis ◽  
Irene M. Mavridis ◽  
Emmanuel Saridakis ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Antigenic Peptide ◽  
Structural Basis ◽  
Peptide Recognition
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