Are mineral adjuvants triggering TLR2/TLR4 on dendritic cells by a secondary cascade reaction in vivo through the action of heat shock proteins and danger signals?

Vaccine ◽  
2006 ◽  
Vol 24 (6) ◽  
pp. 697-698 ◽  
Author(s):  
Erik B. Lindblad
Keyword(s):  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cascade Reaction ◽  
Danger Signals ◽  
Shock Proteins

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

scholarly journals Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96.

1995 ◽  
Vol 182 (3) ◽  
pp. 885-889 ◽  
Author(s):  
D Arnold ◽  
S Faath ◽  
H Rammensee ◽  
H Schild
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Tumor Cells ◽  
Mhc Class I ◽  
Donor Cell ◽  
Class I ◽  
Heat Shock Protein Gp96 ◽  
Shock Proteins

Vaccination of mice with heat shock proteins isolated from tumor cells induces immunity to subsequent challenge with those tumor cells the heat shock protein was isolated from but not with other tumor cells (Udono, H., and P.K. Srivastava. 1994. J. Immunol. 152:5398-5403). The specificity of this immune response is caused by tumor-derived peptides bound to the heat shock proteins (Udono., H., and P.K. Srivastava. 1993. J. Exp. Med. 178:1391-1396). Our experiments show that a single immunization with the heat shock protein gp96 isolated from beta-galactosidase (beta-gal) expressing P815 cells (of DBA/2 origin) induces cytotoxic T lymphocytes (CTLs) specific for beta-gal, in addition to minor H antigens expressed by these cells. CTLs can be induced in mice that are major histocompatibility complex (MHC) identical to the gp96 donor cells (H-2d) as well as in mice with a different MHC (H-2b). Thus gp96 is able to induce "cross priming" (Matzinger, P., and M.J. Bevan. 1977. Cell. Immunol. 33:92-100), indicating that gp96-associated peptides are not limited to the MHC class I ligands of the gp96 donor cell. Our data confirm the notion that samples of all cellular antigens presentable by MHC class I molecules are represented by peptides associated with gp96 molecules of that cell, even if the fitting MHC molecule is not expressed. In addition, we extend previous reports on the in vivo immunogenicity of peptides associated gp96 molecules to two new groups of antigens, minor H antigens, and proteins expressed in the cytosol.

A family of related proteins is encoded by the major Drosophila heat shock gene family

1982 ◽  
Vol 2 (3) ◽  
pp. 286-292
Author(s):  
S C Wadsworth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Sodium Dodecyl ◽  
Heat Shock Gene ◽  
Partial Digestion ◽  
Shock Gene ◽  
Shock Proteins

At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.

scholarly journals Different Efficiency of Heat Shock Proteins (HSP) to Activate Human Monocytes and Dendritic Cells: Superiority of HSP60

2002 ◽  
Vol 169 (11) ◽  
pp. 6141-6148 ◽  
Author(s):  
Karen Bethke ◽  
Frank Staib ◽  
Martin Distler ◽  
Ute Schmitt ◽  
Helmut Jonuleit ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Human Monocytes ◽  
Shock Proteins

In vivo evidence from an Agrostis stolonifera selection genotype that chloroplast small heat-shock proteins can protect photosystem II during heat stress

2002 ◽  
Vol 29 (8) ◽  
pp. 935 ◽  
Author(s):  
Scott A. Heckathorn ◽  
Samantha L. Ryan ◽  
Joanne A. Baylis ◽  
Dongfang Wang ◽  
E. William Hamilton III ◽  
...  
Keyword(s):  
Heat Stress ◽  
Electron Transport ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Agrostis Stolonifera ◽  
Small Heat Shock Proteins ◽  
O2 Evolution ◽  
Shock Proteins ◽  
Tolerant Genotype

Previous in vitro experiments indicated that chloroplast small heat-shock proteins (sHsp) could associate with thylakoids and protect PSII during heat and other stresses, possibly by stabilizing the O2-evolving complex (OEC). However, in vivo evidence of sHsp protection of PSII is equivocal at present. Using previously characterized selection genotypes of Agrostis stolonifera Huds. that differ in thermotolerance and production of chloroplast sHsps, we show that both genotypes contain thylakoid-associating sHsps, but the heat-tolerant genotype, which produces an additional sHsp isoform not made by the sensitive genotype, produces a greater quantity of chloroplast and thylakoid sHsp. Following a pre-heat stress to induce sHsps, in vivo PSII function decreased less at high temperatures in the tolerant genotype. Differences in PSII thermotolerance in vivo were associated with increased thermotolerance of the OEC proteins and O2-evolving function of PSII, and not with other PSII proteins or functions examined. In vivo cross-linking experiments indicated that a greater amount of sHsp associated with PSII proteins during heat stress in the tolerant genotype. PSII was the most thermosensitive component of photosynthetic electron transport, and no differences between genotypes in the thermotolerance of other electron transport components were observed. These results indicate that in vivo chloroplast sHsps can protect O2 evolution and the OEC proteins of PSII during heat stress.

scholarly journals Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway

2000 ◽  
Vol 12 (11) ◽  
pp. 1539-1546 ◽  
Author(s):  
Sreyashi Basu ◽  
Robert J. Binder ◽  
Ryuichiro Suto ◽  
Kirstin M. Anderson ◽  
Pramod K. Srivastava
Keyword(s):  
Cell Death ◽  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Shock Proteins

Heat shock proteins and dendritic cells: effects on maturation and antigen presentation

2001 ◽  
Vol 37 ◽  
pp. S31
Author(s):  
M. Kuppner ◽  
V. Milani ◽  
R. Gastpar ◽  
E. Noessner ◽  
M. Roos ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Antigen Presentation ◽  
Shock Proteins

scholarly journals Protective Effect of Post-Ischaemic Viral Delivery of Heat Shock Proteins in vivo

2008 ◽  
Vol 29 (2) ◽  
pp. 254-263 ◽  
Author(s):  
Romina A Badin ◽  
Michael Modo ◽  
Mike Cheetham ◽  
David L Thomas ◽  
David G Gadian ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Viral Vector ◽  
Lesion Size ◽  
In Vivo Studies ◽  
Current Evidence ◽  
Time Points ◽  
Shock Proteins

Heat shock proteins (HSPs) function as molecular chaperones involved in protein folding, transport and degradation and, in addition, they can promote cell survival both in vitro and in vivo after a range of stresses. Although some in vivo studies have suggested that HSP27 and HSP70 can be neuroprotective, current evidence is limited, particularly when HSPs have been delivered after an insult. The effect of overexpressing HSPs after transient occlusion of the middle cerebral artery in rats was investigated by delivering an attenuated herpes simplex viral vector (HSV-1) engineered to express HSP27 or HSP70 30 mins after tissue reperfusion. Magnetic resonance imaging scans were used to determine lesion size and cerebral blood flow at six different time points up to 1 month after stroke. Animals underwent two sensorimotor tests at the same time points to assess the relationship between lesion size and function. Results indicate that post-ischaemic viral delivery of HSP27, but not of HSP70, caused a statistically significant reduction in lesion size and induced a significant behavioural improvement compared with controls. This is the first evidence of effective post-ischaemic gene therapy with a viral vector expressing HSP27 in an experimental model of stroke.

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