scholarly journals The Life Span Determinant p66Shc Localizes to Mitochondria Where It Associates with Mitochondrial Heat Shock Protein 70 and Regulates Trans-membrane Potential

2004 ◽  
Vol 279 (24) ◽  
pp. 25689-25695 ◽  
Author(s):  
Francesca Orsini ◽  
Enrica Migliaccio ◽  
Maurizio Moroni ◽  
Cristina Contursi ◽  
Veronica A. Raker ◽  
...  
2007 ◽  
Vol 28 (5) ◽  
pp. 1009-1016 ◽  
Author(s):  
Ludmila A Voloboueva ◽  
Melissa Duan ◽  
YiBing Ouyang ◽  
John F Emery ◽  
Christian Stoy ◽  
...  

Mitochondrial heat shock protein 70 (mtHsp70/Hsp75/Grp75/mortalin/TRAP-1/PBP74) is an essential mitochondrial chaperone and a member of the heat shock protein 70 (HSP70) family. Although many studies have shown the protective properties of overexpression of the cytosolic inducible member of the HSP70 family, Hsp72, few studies have investigated the protective potential of Hsp75 against ischemic injury. Mitochondria are one of the primary targets of ischemic injury in astrocytes. In this study, we analyzed the effects of Hsp75 overexpression on cellular levels of reactive oxygen species (ROS), mitochondrial membrane potential, ATP levels, and viability during the ischemia-like conditions of oxygen-glucose deprivation (OGD) or glucose deprivation (GD) in primary astrocytic cultures. We show that Hsp75 overexpression decreases ROS production and preserves mitochondrial membrane potential during GD, and preserves ATP levels and cell viability during OGD. These findings indicate that Hsp75 can provide protection against ischemia-like in vitro injury and suggest that it should be further studied as a potential candidate for protection against ischemic injury.


Polar Biology ◽  
2014 ◽  
Vol 37 (8) ◽  
pp. 1145-1155 ◽  
Author(s):  
Shenghao Liu ◽  
Jing Wang ◽  
Bailin Cong ◽  
Xiaohang Huang ◽  
Kaoshan Chen ◽  
...  

1994 ◽  
Vol 127 (4) ◽  
pp. 893-902 ◽  
Author(s):  
J M Herrmann ◽  
R A Stuart ◽  
E A Craig ◽  
W Neupert

Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix. Here, we describe a role for mt-Hsp70 in chaperoning proteins encoded by mitochondrial DNA and synthesized within mitochondria. The availability of mt-Hsp70 function influences the pattern of proteins synthesized in mitochondria of yeast both in vivo and in vitro. In particular, we show that mt-Hsp70 acts in maintaining the var1 protein, the only mitochondrially encoded subunit of mitochondrial ribosomes, in an assembly competent state, especially under heat stress conditions. Furthermore, mt-Hsp70 helps to facilitate assembly of mitochondrially encoded subunits of the ATP synthase complex. By interacting with the ATP-ase 9 oligomer, mt-Hsp70 promotes assembly of ATP-ase 6, and thereby protects the latter protein from proteolytic degradation. Thus mt-Hsp70 by acting as a chaperone for proteins encoded by the mitochondrial DNA, has a critical role in the assembly of supra-molecular complexes.


2014 ◽  
Vol 139 ◽  
pp. 1-10 ◽  
Author(s):  
Charles Schumpert ◽  
Indhira Handy ◽  
Jeffry L. Dudycha ◽  
Rekha C. Patel

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