A Role for Heat Shock Proteins in Antigen Processing and Presentation

Author(s):  
S. K. Pierce ◽  
D. C. DeNagel ◽  
A. M. VanBuskirk
2021 ◽  
Vol 43 (2) ◽  
pp. 887-899
Author(s):  
Enrique Ambrocio-Ortiz ◽  
Gloria Pérez-Rubio ◽  
Alejandra Ramírez-Venegas ◽  
Rafael de Jesús Hernández-Zenteno ◽  
Armando Paredes-López ◽  
...  

Background: Chronic Obstructive Pulmonary Disease (COPD) is an inflammatory disease characterized by airflow obstruction, commonly present in smokers and subjects exposed to noxious particles product of biomass-burning smoke (BBS). Several association studies have identified single-nucleotide polymorphisms (SNP) in coding genes related to the heat shock proteins family-genes that codify the heat shock proteins (Hsp). Hsp accomplishes critical roles in regulating immune response, antigen-processing, eliminating protein aggregates and co-activating receptors. The presence of SNPs in these genes can lead to alterations in immune responses. We aimed to evaluate the association of SNPs in the HSP90 gene complex and COPD. Methods: We enrolled 1549 participants, divided into two comparison groups; 919 tobacco-smoking subjects (cases COPD-TS n = 294 and, controls SWOC n = 625) and 630 chronic exposed to BBS (cases COPD-BBS n = 186 and controls BBES n = 444). We genotyped 2 SNPs: the rs13296 in HSP90AB1 and rs2070908 in HSP90B1. Results: Through the dominant model (GC + CC), the rs2070908 is associated with decreased risk (p < 0.01, OR = 0.6) to suffer COPD among chronic exposed BBS subjects. We found an association between rs13296 GG genotype and lower risk (p = 0.01, OR = 0.22) to suffer severe COPD-TS forms in the severity analysis. Conclusions: single-nucleotide variants in the HSP90AB1 and HSP90B1 genes are associated with decreased COPD risk in subjects exposed to BBS and the most severe forms of COPD in tobacco-smoking subjects.


2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Stuart K. Calderwood ◽  
Mary Ann Stevenson ◽  
Ayesha Murshid

Heat shock proteins (HSPs) have been linked to the therapy of both cancer and inflammatory diseases, approaches that utilize contrasting immune properties of these proteins. It would appear that HSP family members Hsp60 and Hsp70, whether from external sources or induced locally during inflammation, can be processed by antigen-presenting cells and that HSP-derived epitopes then activate regulatory T cells and suppress inflammatory diseases. These effects also extend to the HSP-rich environments of cancer cells where elevated HSP concentrations may participate in the immunosuppressive tumor milieu. However, HSPs can also be important mediators of tumor immunity. Due to their molecular chaperone properties, some HSPs can bind tumor-specific peptides and deliver them deep into the antigen-processing pathways of antigen-presenting cells (APCs). In this context, HSP-based vaccines can activate tumor-specific immunity, trigger the proliferation and CTL capabilities of cancer-specific CD8+ T cells, and inhibit tumor growth. Further advances in HSP-based anticancer immunotherapy appear to involve improving the properties of the molecular chaperone vaccines by enhancing their antigen-binding properties and combating the immunosuppressive tumor milieu to permit programming of active CTL capable of penetrating the tumor milieu and specifically targeting tumor cells.


1994 ◽  
Vol 39 (2) ◽  
Author(s):  
PramodK. Srivastava ◽  
Heiichiro Udono ◽  
NathalieE. Blachere ◽  
Zihai Li

2005 ◽  
Vol 36 (10) ◽  
pp. 14
Author(s):  
PATRICE WENDLING

1990 ◽  
Vol 80 (2) ◽  
pp. 301-306
Author(s):  
Tiina Vahala ◽  
Tage Eriksson ◽  
Peter Engstrom

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