AJP - Heart Watch the video to see how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Am J Physiol Heart Circ Physiol (February 16, 2007). doi:10.1152/ajpheart.01355.2006
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
292/6/H3052    most recent
01355.2006v1
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 Web of Science
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 Web of Science (10)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gupta, S.
Right arrow Articles by Knowlton, A. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gupta, S.
Right arrow Articles by Knowlton, A. A.
Submitted on December 12, 2006
Accepted on February 12, 2007

HSP60 Trafficking in Adult Cardiac Myocytes: Role of the Exosomal Pathway

Sanjiv Gupta1 and Anne A. Knowlton2*

1 Medicine, University of California, Davis, Davis, California, United States
2 Cardiovascular Division, University of California, Davis, Davis, California, United States

* To whom correspondence should be addressed. E-mail: aaknowlton{at}ucdavis.edu.

The heat shock proteins (HSP) are highly conserved family of proteins with critical functions in protein folding, protein trafficking and cell signaling. These proteins also protect the cell against injury. HSP60 has been found in the extracellular space and has been identified in the plasma of some individuals. HSP60 is thought to be a "danger signal" to the immune system and is also highly immunogenic. Thus, extracellular HSP60 is possibly toxic to the cell. The mechanism by which HSP60 is released into the extracellular space is unknown. We investigated several different pathways controlling protein release including the classic, Golgi-mediated pathway. We found that HSP60 is released via exosomes, and that within the exosome, HSP60 is tightly attached to the exosome membrane.




This article has been cited by other articles:


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
K. Rayner, J. Sun, Y.-X. Chen, M. McNulty, T. Simard, X. Zhao, D. J. Wells, J. de Belleroche, and E. R. O'Brien
Heat Shock Protein 27 Protects Against Atherogenesis via an Estrogen-Dependent Mechanism: Role of Selective Estrogen Receptor Beta Modulation
Arterioscler Thromb Vasc Biol, November 1, 2009; 29(11): 1751 - 1756.
[Abstract] [Full Text] [PDF]


Home page
CirculationHome page
Y. M. Tsutsumi, Y. T. Horikawa, M. M. Jennings, M. W. Kidd, I. R. Niesman, U. Yokoyama, B. P. Head, Y. Hagiwara, Y. Ishikawa, A. Miyanohara, et al.
Cardiac-Specific Overexpression of Caveolin-3 Induces Endogenous Cardiac Protection by Mimicking Ischemic Preconditioning
Circulation, November 4, 2008; 118(19): 1979 - 1988.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
B. J.J.M. Brundel, L. Ke, A.-J. Dijkhuis, X. Qi, A. Shiroshita-Takeshita, S. Nattel, R. H. Henning, and H. H. Kampinga
Heat shock proteins as molecular targets for intervention in atrial fibrillation
Cardiovasc Res, June 1, 2008; 78(3): 422 - 428.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 1977 by the American Physiological Society.