Cytokine function of heat shock proteins

2004 ◽  
Vol 286 (4) ◽  
pp. C739-C744 ◽  
Author(s):  
Min-Fu Tsan ◽  
Baochong Gao
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune System ◽  
Therapeutic Potential ◽  
Innate Immune ◽  
Heat Sensitivity ◽  
Receptor Complex ◽  
Shock Proteins ◽  
Antigen Presenting ◽  
Tlr4 Receptor

Extensive work in the last 10 years has suggested that heat shock proteins (HSPs) may be potent activators of the innate immune system. It has been reported that Hsp60, Hsp70, Hsp90, and gp96 are capable of inducing the production of proinflammatory cytokines by the monocyte-macrophage system and the activation and maturation of dendritic cells (antigen-presenting cells) in a manner similar to the effects of lipopolysaccharide (LPS) and bacterial lipoprotein, e.g., via CD14/Toll-like receptor2 (TLR2) and CD14/TLR4 receptor complex-mediated signal transduction pathways. However, recent evidence suggests that the reported cytokine effects of HSPs may be due to the contaminating LPS and LPS-associated molecules. The reasons for previous failure to recognize the contaminant(s) as being responsible for the reported HSP cytokine effects include failure to use highly purified, low-LPS preparations of HSPs; failure to recognize the heat sensitivity of LPS; and failure to consider contaminant(s) other than LPS. Thus it is essential that efforts should be directed to conclusively determine whether the reported HSP cytokine effects are due to HSPs or to contaminant(s) present in the HSP preparations before further exploring the implication and therapeutic potential of the putative cytokine function of HSPs.

Heat-shock proteins as activators of the innate immune system

2002 ◽  
Vol 23 (3) ◽  
pp. 130-135 ◽  
Author(s):  
Robert P.A Wallin ◽  
Andreas Lundqvist ◽  
Solveig H Moré ◽  
Arne von Bonin ◽  
Rolf Kiessling ◽  
...  
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune System ◽  
Innate Immune ◽  
Shock Proteins

scholarly journals Heat Shock Proteins: Stimulators of Innate and Acquired Immunity

2013 ◽  
Vol 2013 ◽  
pp. 1-11 ◽  
Author(s):  
Camilo A. Colaco ◽  
Christopher R. Bailey ◽  
K. Barry Walker ◽  
James Keeble
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune Response ◽  
Innate Immune ◽  
Rational Vaccine Design ◽  
Definition Of ◽  
Shock Proteins ◽  
Antigen Presenting ◽  
Molecular Patterns

Adjuvants were reintroduced into modern immunology as the dirty little secret of immunologists by Janeway and thus began the molecular definition of innate immunity. It is now clear that the binding of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs) on antigen presenting cells (APCs) activates the innate immune response and provides the host with a rapid mechanism for detecting infection by pathogens and initiates adaptive immunity. Ironically, in addition to advancing the basic science of immunology, Janeway’s revelation on induction of the adaptive system has also spurred an era of rational vaccine design that exploits PRRs. Thus, defined PAMPs that bind to known PRRs are being specifically coupled to antigens to improve their immunogenicity. However, while PAMPs efficiently activate the innate immune response, they do not mediate the capture of antigen that is required to elicit the specific responses of the acquired immune system. Heat shock proteins (HSPs) are molecular chaperones that are found complexed to client polypeptides and have been studied as potential cancer vaccines. In addition to binding PRRs and activating the innate immune response, HSPs have been shown to both induce the maturation of APCs and provide chaperoned polypeptides for specific triggering of the acquired immune response.

Heat-shock proteins as activators of the innate immune system

2002 ◽  
Vol 23 (7) ◽  
pp. 342-343 ◽  
Author(s):  
Huguette Bausinger ◽  
Dan Lipsker ◽  
Daniel Hanau
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune System ◽  
Innate Immune ◽  
Shock Proteins

scholarly journals The role and therapeutic potential of heat shock proteins in haemorrhagic stroke

2019 ◽  
Vol 23 (9) ◽  
pp. 5846-5858 ◽  
Author(s):  
Anwen Shao ◽  
Yunxiang Zhou ◽  
Yihan Yao ◽  
Wenhua Zhang ◽  
Jianmin Zhang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Therapeutic Potential ◽  
Haemorrhagic Stroke ◽  
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.

Calcium Phosphate Powder for Cancer Vaccination

2007 ◽  
Vol 361-363 ◽  
pp. 1207-1210 ◽  
Author(s):  
Patrick Frayssinet ◽  
Daniel Ciocca ◽  
Nicole Rouquet
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cancer Tissue ◽  
Phosphate Powder ◽  
Cancer Vaccination ◽  
Shock Proteins ◽  
Antigen Presenting ◽  
Proteins And Peptides

Cancer cells synthesize abnormal proteins and peptides which are associated to heat shock proteins being overproduced by these cells due to the stress induced by the particular biology of cancer tissue. We have purified on hydroxylapatite powder heat shock proteins using the HAparticles as purification bed, vectors for the proteins and vaccination adjuvant. The powder make possible that the purified HSPs and their associated peptides are transfected to the antigen presenting cells and presented to the T cells for the destruction of the cancer cells bearing the antigens.

Innate Immune-Related Receptors in Normal and Psoriatic Skin

2003 ◽  
Vol 127 (2) ◽  
pp. 178-186 ◽  
Author(s):  
Jonathan L. Curry ◽  
Jian-Zhong Qin ◽  
Brian Bonish ◽  
Ryan Carrick ◽  
Patricia Bacon ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Normal Skin ◽  
Innate Immune ◽  
Receptor Expression ◽  
Interleukin 12 ◽  
Psoriatic Skin ◽  
Shock Proteins ◽  
And Function

Abstract Context.—A precise role for the innate immune system in psoriasis remains to be determined. Surface receptors, including Toll-like receptors (TLRs) that recognize bacterial ligands and CD91, which recognizes heat shock proteins (HSPs), are implicated in both innate and adaptive immunity. Objective.—Since skin is exposed to various exogenous stimuli, which can provoke or exacerbate psoriasis, we characterized expression and function of TLRs, CD91, and HSPs in normal and psoriatic skin. Design.—A variety of skin-derived cells and blood-derived cells were analyzed both in vivo and in vitro; samples were obtained from 24 different individuals for innate immune-related receptor expression and function. By comparing and contrasting individuals with healthy skin and psoriatic patients, several specific differences were identified. Results.—Immunohistochemistry-based expression profiling revealed TLR1 expression in epidermal dendritic cells (DCs) and dermal dendritic cells (DDCs) in normal skin, as well as in pre-psoriatic skin and psoriatic plaques, with enhanced basal layer keratinocyte (KC) expression in pre-psoriatic and psoriatic plaques compared with normal skin; TLR2 expression primarily by DDCs; and TLR4 expression by epidermal DCs and DDCs, with mid-epidermal-layer KCs displaying cell surface staining. No TLR9 or CD14 was detected on DCs or KCs, although psoriatic plaques contained CD14-positive macrophages. Analysis of psoriatic epidermis revealed HSPs 27, 60, and 70. Keratinocytes were CD91 negative, but CD91 was expressed by fibroblasts and DDCs in normal and pre-psoriatic skin, with prominent accumulation of CD91-positive DDCs in psoriatic plaques. Cultured KCs revealed no surface expression of TLR2, TLR4, TLR9, or CD91. Exposure of fibroblasts, but not KCs, to lipopolysaccharide or HSPs triggered nuclear factor (NF)-κB activation. Heat shock proteins did induce maturation of blood-derived DCs accompanied by increased interleukin-12 production and enhanced antigen-presenting function. Conclusions.—These data demonstrate distinctive patterns of innate immune-related receptors by specific subsets of cells in normal and psoriatic skin, suggesting functional roles for HSPs and DCs in psoriasis.

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