Constitutive expression of an endoplasmic reticulum small heat shock protein alleviates endoplasmic reticulum stress in transgenic tomato

2007 ◽  
Vol 164 (7) ◽  
pp. 835-841 ◽  
Author(s):  
Chunmei Zhao ◽  
Mariko Shono ◽  
Aiqing Sun ◽  
Shuying Yi ◽  
Minghui Li ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Endoplasmic Reticulum Stress ◽  
Heat Shock Protein ◽  
Constitutive Expression ◽  
Small Heat Shock Protein ◽  
Transgenic Tomato

Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27

2005 ◽  
Vol 95 (5) ◽  
pp. 932-941 ◽  
Author(s):  
Hidenori Ito ◽  
Ikuko Iwamoto ◽  
Yutaka Inaguma ◽  
Takenori Takizawa ◽  
Koh-ichi Nagata ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Endoplasmic Reticulum Stress ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

scholarly journals Study of HSPB6: Insights into the Properties of the Multifunctional Protective Agent

2017 ◽  
Vol 44 (1) ◽  
pp. 314-332 ◽  
Author(s):  
Fazhao Li ◽  
Han Xiao ◽  
Fangfang Zhou ◽  
Zhiping Hu ◽  
Binbin Yang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Muscle Relaxation ◽  
Constitutive Expression ◽  
Small Heat Shock Protein ◽  
Protective Role ◽  
Smooth Muscle Relaxation ◽  
Protective Agent ◽  
Cellular Targets ◽  
The Central Nervous System

HSPB6(Heat shock protein B6), is also referred to as P20/HSP20. Unlike other many other members of sHSP(small Heat shock protein) family, which tend to form high-molecular-mass oligomers, in solution, human HSPB6 only forms dimers. However, it still exhibits chaperon-like activity comparable with that of HSPB5. It is expressed ubiquitously, with high and constitutive expression in muscular tissues. sHSPs characteristically function as molecular chaperones and HSPB6 also has a molecular chaperone activity. HSPB6 is up-regulated in response to diverse cellular stress or damage and protect cells from otherwise lethal conditions. HSPB6 is widely recognized as a principle mediator of cardioprotective signaling and recent studies have unraveled the protective role of HSPB6 in disease or injury to the central nervous system. Moreover, accumulating evidence has implicated HSPB6 as a key mediator of diverse vital physiological processes, such as smooth muscle relaxation, platelet aggregation. The versatility of HSPB6 can be explained by its direct involvement in regulating different client proteins and its ability to form heterooligomer with other sHSPs, which seems to be dependent on HSPB6 phosphorylation. This review focuses on the properties including expression and regulation pattern, phosphorylation, chaperon activity, multiple cellular targets of HSPB6, as well as its possible role in physical and pathological conditions.

Heat shock protein 72 protects insulin-secreting beta cells from lipopolysaccharide-induced endoplasmic reticulum stress

2009 ◽  
Vol 25 (8) ◽  
pp. 626-633 ◽  
Author(s):  
Satoshi Hagiwara ◽  
Hideo Iwasaka ◽  
Chihiro Shingu ◽  
Shigekiyo Matsumoto ◽  
Akira Hasegawa ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Endoplasmic Reticulum Stress ◽  
Heat Shock Protein ◽  
Beta Cells ◽  
Heat Shock Protein 72
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