AJP - Regu Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Regul Integr Comp Physiol 269: R608-R613, 1995;
0363-6119/95 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Beck, S. C.
Right arrow Articles by De Maio, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beck, S. C.
Right arrow Articles by De Maio, A.

AJP - Regulatory, Integrative and Comparative Physiology, Vol 269, Issue 3 608-R613, Copyright © 1995 by American Physiological Society

ARTICLES

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

S. C. Beck, C. N. Paidas, H. Tan, J. Yang and A. De Maio
Division of Pediatric Surgery, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287-3716, USA.

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.


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
L. H. E. H. Snoeckx, R. N. Cornelussen, F. A. Van Nieuwenhoven, R. S. Reneman, and G. J. Van der Vusse
Heat Shock Proteins and Cardiovascular Pathophysiology
Physiol Rev, October 1, 2001; 81(4): 1461 - 1497.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Wyttenbach, J. Carmichael, J. Swartz, R. A. Furlong, Y. Narain, J. Rankin, and D. C. Rubinsztein
Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
PNAS, March 14, 2000; 97(6): 2898 - 2903.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. F. Winklhofer, A. Reintjes, M. C. Hoener, R. Voellmy, and J. Tatzelt
Geldanamycin Restores a Defective Heat Shock Response in Vivo
J. Biol. Chem., November 21, 2001; 276(48): 45160 - 45167.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online