The heat shock protein hsp70 binds in vivo to subregions 2-48BC and 3-58D of the polytene chromosomes ofDrosophila hydei

Chromosoma ◽  
1990 ◽  
Vol 99 (5) ◽  
pp. 315-320 ◽  
Author(s):  
Elizabeth Laran ◽  
José Maria Requena ◽  
Antonio Jimenez-Ruiz ◽  
Manuel Carlos Lopez ◽  
Carlos Alonso
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Polytene Chromosomes ◽  
Heat Shock Protein Hsp70

Membrane-bound Heat Shock Protein HSP70 as a Target for Theranostics of Tumors

2018 ◽  
pp. 802-804
Author(s):  
M. Shevtsov ◽  
B. Margulis ◽  
I. Guzhova ◽  
B. Nikolaev ◽  
A. Ischenko ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Membrane Bound ◽  
Heat Shock Protein Hsp70

Heat Shock Protein HSP70 in Oxidative Stress in Apnea Patients

2020 ◽  
Vol 169 (5) ◽  
pp. 695-697
Author(s):  
I. M. Madaeva ◽  
N. A. Kurashova ◽  
N. V. Semenova ◽  
E. B. Ukhinov ◽  
S. I. Kolesnikov ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein Hsp70

Exogenous heat shock protein HSP70 suppresses bacterial pathogen-induced activation of human neutrophils

2010 ◽  
Vol 435 (1) ◽  
pp. 316-319 ◽  
Author(s):  
M. M. Yurinskaya ◽  
M. B. Evgen’ev ◽  
O. Yu. Antonova ◽  
M. G. Vinokurov
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Bacterial Pathogen ◽  
Human Neutrophils ◽  
Heat Shock Protein Hsp70

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.

scholarly journals Dimeric heat shock protein 40 binds radial spokes for generating coupled power strokes and recovery strokes of 9 + 2 flagella

2008 ◽  
Vol 180 (2) ◽  
pp. 403-415 ◽  
Author(s):  
Chun Yang ◽  
Heather A. Owen ◽  
Pinfen Yang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Adenosine Triphosphatase ◽  
Stable Conformation ◽  
Initiation And Propagation ◽  
Evolutionarily Conserved ◽  
Radial Spokes ◽  
Cilia And Flagella ◽  
Hsp 40

T-shape radial spokes regulate flagellar beating. However, the precise function and molecular mechanism of these spokes remain unclear. Interestingly, Chlamydomonas reinhardtii flagella lacking a dimeric heat shock protein (HSP) 40 at the spokehead–spokestalk juncture appear normal in length and composition but twitch actively while cells jiggle without procession, resembling a central pair (CP) mutant. HSP40− cells begin swimming upon electroporation with recombinant HSP40. Surprisingly, the rescue doesn't require the signature DnaJ domain. Furthermore, the His-Pro-Asp tripeptide that is essential for stimulating HSP70 adenosine triphosphatase diverges in candidate orthologues, including human DnaJB13. Video microscopy reveals hesitance in bend initiation and propagation as well as irregular stalling and stroke switching despite fairly normal waveform. The in vivo evidence suggests that the evolutionarily conserved HSP40 specifically transforms multiple spoke proteins into stable conformation capable of mechanically coupling the CP with dynein motors. This enables 9 + 2 cilia and flagella to bend and switch to generate alternate power strokes and recovery strokes.

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