Depressed expression of the inducible form of HSP 70 (HSP 72) in brain and heart after in vivo heat shock

1995 ◽  
Vol 269 (3) ◽  
pp. R608-R613 ◽  
Author(s):  
S. C. Beck ◽  
C. N. Paidas ◽  
H. Tan ◽  
J. Yang ◽  
A. De Maio

The heat shock gene expression plays a role in the protection of cells from injury. In the present study, we have analyzed the expression of heat shock protein (HSP) 72 (the major inducible form of the HSP 70 family) in different rat organs after a total body hyperthermia. The content of HSP 72 was greatest in liver and colon. In contrast, accumulation of HSP 72 was low in heart and brain (3-5% and < 1% of the amount in liver, respectively). This low expression of HSP 72 in heart and brain could not be explained by a difference in the actual temperature within these organs. Analysis of cells in culture that resemble hepatocytes, myoblast, and neurons showed a pattern of HSP 72 expression similar to that observed in liver, heart, and brain in vivo after heat shock. These results suggest that this disparate expression of HSP 72 is due to intrinsic characteristics of the cell types rather than to physiological or environmental conditions. The differential expression of HSP 72 among different cell lines could be correlated with the different levels of protein synthesis protection.

2004 ◽  
Vol 186 (10) ◽  
pp. 2956-2965 ◽  
Author(s):  
Gunther Spohn ◽  
Alberto Danielli ◽  
Davide Roncarati ◽  
Isabel Delany ◽  
Rino Rappuoli ◽  
...  

ABSTRACT The HspR repressor regulates transcription of the groESL, hrcA-grpE-dnaK, and cbpA-hspR-orf operons of Helicobacter pylori. Here we show that two of the HspR-regulated operons, namely, the groESL and dnaK operons, encoding the major cellular chaperone machineries are also regulated by the H. pylori homologue of the HrcA repressor. Similarly to the hspR mutation, deletion of the hrcA gene also leads to complete derepression of the P gro and P hrc promoters. The presence of both HspR and HrcA is therefore necessary for regulated transcription from these promoters. HrcA binds directly to P gro and P hrc , likely contacting two inverted repeats with similarity to the CIRCE motif, which are present on both promoters. HrcA regulation is, however, shown to depend on binding of the HspR protein, since deletion of the HspR-binding site of the P gro promoter leads to loss of heat inducibility of this promoter. In contrast, transcription from the P cbp promoter is regulated solely by HspR. HspR is also shown to form oligomers in vivo through a stretch of hydrophobic repeats between amino acid positions 66 and 97. The implications of these findings for the elucidation of the networks regulating heat shock gene expression in H. pylori are discussed.


1998 ◽  
Vol 4 (4) ◽  
pp. 236-239
Author(s):  
B. Joy Snider

Heat shock proteins were initially described as the predominant proteins expressed immediately after a thermal stress. These ubiquitously expressed proteins function as molecular chaperones; they aid in the folding, subcellular translocation, and assembly of other proteins. Although most of these proteins are expressed constitutively, enhanced expression, induced by stress or genetic manipulations, can reduce subsequent cellular injury in many cell types, including neurons and glia. Further understanding of how the expression of these proteins is controlled in the nervous system, and how they can be manipulated to attenuate injury, could provide therapeutic targets for cerebral ischemia and neurodegenerative disorders.


1982 ◽  
Vol 2 (3) ◽  
pp. 286-292
Author(s):  
S C Wadsworth

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.


1998 ◽  
Vol 25 (1) ◽  
pp. 31-43 ◽  
Author(s):  
Saadat Mohsenzadeh ◽  
Wolfgang Saupe-Thies ◽  
Gabriele Steier ◽  
Torsten Schroeder ◽  
Franco Fracella ◽  
...  

PLoS Genetics ◽  
2011 ◽  
Vol 7 (7) ◽  
pp. e1002206 ◽  
Author(s):  
Magdalena Murawska ◽  
Markus Hassler ◽  
Renate Renkawitz-Pohl ◽  
Andreas Ladurner ◽  
Alexander Brehm

Sign in / Sign up

Export Citation Format

Share Document