Metabolic Stress, Heat Shock Proteins, and Innate Immune Response

2016 ◽  
pp. 107-131 ◽  
Author(s):  
Nicola Lacetera
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune Response ◽  
Metabolic Stress ◽  
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 (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 Induction of mitochondrial heat shock proteins and mitochondrial biogenesis in endothelial cells upon acute methylglyoxal stress: Evidence for hormetic autofeedback

2021 ◽  
Author(s):  
Ruben Bulkescher ◽  
Thomas Fleming ◽  
Claus Rodemer ◽  
Rebekka Medert ◽  
Marc Freichel ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mitochondrial Biogenesis ◽  
Metabolic Flux ◽  
Metabolic Stress ◽  
Oxidative Capacity ◽  
Mitochondrial Proteins ◽  
Shock Proteins

Increased metabolic flux produces potentially harmful side-products, such as reactive dicarbonyl and oxygen species. The reactive dicarbonly methylglyoxal (MG) can impair oxidative capacity, which is downregulated in type 2 diabetes. Heat shock proteins (HSPs) of subfamily A (Hsp70s) promote ATP-dependent processing of damaged proteins during MG exposure which also involve mitochondrial proteins. Since the protection of mitochondrial proteins could promote higher production of reactive metabolites due to increased substrate flux, tight regulation of HspA-mediated protein handling is important. We hypothesized that stress-inducible HspAs (HspA1A/HspA1B) are pivotal for maintaining mitochondrial biogenesis during acute MG-stress. To analyze the role of stress-inducible HspA1A/HspA1B for maintenance of mitochondrial homeostasis during acute MG exposure, we knocked out HSPA1A/HSPA1B in mouse endothelial cells. HSPA1A/HSPA1B KO cells showed upregulation of the mitochondrial chaperones HspA9 (mitochondrial Hsp70/mortalin) and HspD1 (Hsp60) as well as induction of mitochondrial biogenesis upon MG exposure. Increased mitochondrial biogenesis was reflected by elevated mitochondrial branching, total count and area as well as by upregulation of mitochondrial proteins and corresponding transcription factors. Our findings suggest that mitochondrial HspA9 and HspD1 promote mitochondrial biogenesis during acute MG stress, which is counterregulated by HspA1A/HspA1B to prevent mitochondrial overstimulation and to maintain balanced oxidative capacity under metabolic stress conditions. These data support an important role of HSPs in MG-induced hormesis.

Enhancement of Th1 immune response by CD8α+ dendritic cells loaded with heat shock proteins enriched tumor extract in tumor-bearing mice

2009 ◽  
Vol 260 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Abbas Azadmehr ◽  
Ali Akbar Pourfathollah ◽  
Zahra Amirghofran ◽  
Zuhair Mohammad Hassan ◽  
Seyed Mohammad Moazzeni
Keyword(s):  
Immune Response ◽  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tumor Bearing ◽  
Tumor Extract ◽  
Shock Proteins ◽  
Th1 Immune Response

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.

Detection of the host immune response to Burkholderia mallei heat-shock proteins GroEL and DnaK in a glanders patient and infected mice

2007 ◽  
Vol 59 (2) ◽  
pp. 137-147 ◽  
Author(s):  
Kei Amemiya ◽  
Jennifer L. Meyers ◽  
David DeShazer ◽  
Renaldo N. Riggins ◽  
Stephanie Halasohoris ◽  
...  
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Host Immune Response ◽  
Burkholderia Mallei ◽  
Shock Proteins

scholarly journals Violation of antimitochondrial tolerance in patients with multiple repreduction failure

2019 ◽  
pp. 93-98
Author(s):  
B. V. Dons’koi ◽  
V. P. Chernyshov ◽  
K. S. Stepaniuk ◽  
K. J. Krychkov
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Pregnant Women ◽  
Autoimmune Response ◽  
Implantation Failure ◽  
Repeated Implantation Failure ◽  
Shock Proteins ◽  
Antigen Structure ◽  
Specific Lipid

Mitochondria are semi-autonomic organelle that consist specific lipid and protein antigen structure. Evolutionary this structure is close to bacterial antigens (cardiolipin and heat shock proteins HSP). Immune response to pathogens can result to cross-reaction and development of proto-autoimmune and true autoimmune response in individuals with affected anti-mitochondrial tolerance. Serum from 127 healthy pregnant women (HPW), 58women with infertility (IF) and 149 patients with repeated implantation failure (RIF) (> 2) after IVF, was analyzed by ELISA for anti-Chlamidia IgG anti-HSP60 and cofactor-independent anti cardiolipin IgG (aCL). We show that in RIF patients aCL presence was significantly higher 23.9 % (34/142) than in HP women 7 % (9/127) and IF group 13.7 % (8/58). Anti-HSP60 ab was registered generally in RIF 8.6 % (11/98) while only one patient from IF group was anti-HSP60 positive 1.7 % (1/58) and any in HP group (0/127). We find the association between Anti-HSP60 and aCL ab. Patients with Anti-HSP60 ab was positive for aCL in 36.4 % (4/11) that was more frequently compared to both Anti-HSP60-negative: Chlamydia IgG positive 16.7 % (12/72) or Chlamydia IgG negative patients 10.9 % (33/302). We showed that aCL and Anti-HSP60 associated with repeated implantation failure and both reflect anti-mitochondrial tolerance dysfunction as hyper and hypo diagnostic markers.

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