scholarly journals Structure and Function: Heat Shock Proteins and Adaptive Immunity

2007 ◽  
Vol 179 (4) ◽  
pp. 2035-2040 ◽  
Author(s):  
Babak Javid ◽  
Paul A. MacAry ◽  
Paul J. Lehner
2010 ◽  
Vol 67 (12) ◽  
pp. 698-704 ◽  
Author(s):  
Tetsuya ABE ◽  
Shinpei ITO ◽  
Naoya NISHI ◽  
Yoshihiro TSUKADA ◽  
Takuo YASUNAGA ◽  
...  

1996 ◽  
Vol 47 (3) ◽  
pp. 325-338 ◽  
Author(s):  
Elizabeth R. Waters ◽  
Garrett J. Lee ◽  
Elizabeth Vierling

2005 ◽  
Vol 12 (10) ◽  
pp. 842-846 ◽  
Author(s):  
Martin Haslbeck ◽  
Titus Franzmann ◽  
Daniel Weinfurtner ◽  
Johannes Buchner

2018 ◽  
Vol 19 (11) ◽  
pp. 3441 ◽  
Author(s):  
Teresa Jagla ◽  
Magda Dubińska-Magiera ◽  
Preethi Poovathumkadavil ◽  
Małgorzata Daczewska ◽  
Krzysztof Jagla

Heat shock proteins (Hsps) form a large family of evolutionarily conserved molecular chaperones that help balance protein folding and protect cells from various stress conditions. However, there is growing evidence that Hsps may also play an active role in developmental processes. Here, we take the example of developmental expression and function of one class of Hsps characterized by low molecular weight, the small Hsps (sHsps). We discuss recent reports and genome-wide datasets that support vital sHsps functions in the developing nervous system, reproductive system, and muscles. This tissue- and time-specific sHsp expression is developmentally regulated, so that the enhancer sequence of an sHsp gene expressed in developing muscle, in addition to stress-inducible elements, also carries binding sites for myogenic regulatory factors. One possible reason for sHsp genes to switch on during development and in non-stress conditions is to protect vital developing organs from environmental insults.


2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Arman Kilic ◽  
Kaushik Mandal

Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.


FEBS Letters ◽  
2014 ◽  
Vol 588 (4) ◽  
pp. 517-530 ◽  
Author(s):  
Magda Dubińska-Magiera ◽  
Jadwiga Jabłońska ◽  
Jolanta Saczko ◽  
Julita Kulbacka ◽  
Teresa Jagla ◽  
...  

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