Results 181 to 190 of about 23,911 (226)

Expression of chaperonin 60 in the hippocampus of the streptozotocin diabetic rat

NeuroReport, 2006
Mitochondrial dysfunction and oxidative stress are implicated in the pathological changes observed in the diabetic central nervous system. In this study, using the streptozotocin-induced diabetic rat model we document for the first time the over-expression of a mitochondrial specific stress protein (chaperonin 60) in the CA1/CA3 regions of the diabetic
Jiang, Yuan, Brian J, Young, Ryan D, Martinus   +2 more
openaire   +2 more sources

Cloning, expression and purification of three Chaperonin 60 homologues

Journal of Chromatography B, 2003
The Chaperonin 60 (Cpn60) proteins have, in addition to their well-known functions of protein folding and protection, a range of intercellular signalling activities. As part of a study to investigate the biological activity of the Cpn60 proteins, particularly from pathogenic organisms, we have cloned and expressed three Cpn60 proteins from Homo sapiens,
Maria, Maguire, Anthony R M, Coates, Brian, Henderson   +2 more
openaire   +2 more sources

Purification and characterization of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brockii

European Journal of Biochemistry, 1994
Chaperonin 60 and chaperonin 10 (GroEL and GroES homologues, respectively) have been isolated from extracts of the anaerobic thermophile Thermoanaerobacter brockii. A simple and rapid purification for chaperonin 60 made use of hydrophobic and anion‐exchange chromatographies, and could be readily scaled up; approximately 2 mg pure chaperonin 60 was ...
Truscott, KN, Hoj, PB, Scopes, RK
openaire   +4 more sources

Conformational states of ribulose bisphosphate carboxylase and their interaction with chaperonin 60

Biochemistry, 1992
Conformational states of ribulosebisphosphate carboxylase (Rubisco) from Rhodospirillum rubrum were examined by far-UV circular dichroism (CD), tryptophan fluorescence, and 1-anilino-naphthalenesulfonate (ANS) binding. At pH 2 and low ionic strength (I = 0.01), Rubisco adopts an unfolded, monomeric conformation (UA1 state) as judged by far-UV CD and ...
S M, van der Vies, P V, Viitanen, A A, Gatenby, G H, Lorimer, R, Jaenicke   +4 more
openaire   +2 more sources

Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

Biochemistry, 1990
Both the chaperonin- and MgATP-dependent reconstitution of unfolded ribulosebisphosphate carboxylase (Rubisco) and the uncoupled ATPase activity of chaperonin 60 (groEL) require ionic potassium. The spontaneous, chaperonin-independent reconstitution of Rubisco, observed at 15 but not at 25 degrees C, requires no K+ and is actually inhibited by ...
P V, Viitanen, T H, Lubben, J, Reed, P, Goloubinoff, D P, O'Keefe, G H, Lorimer   +5 more
openaire   +2 more sources

Chaperonin 60 and macrophage activation.

Novartis Foundation symposium, 2008
Eukaryotic and prokaryotic chaperonin 60s (Cpn60s) activate macrophages to produce pro-inflammatory cytokines. CD14 and TLR4 have been proposed as potential Cpn receptors. In addition, Cpn60s can block LPS-induced activation. This is a dose-related effect, low concentrations block, and high concentrations activate.
Anthony R M, Coates, Ana, Cehovin, Yanmin, Hu   +2 more
openaire   +1 more source

The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter

Gene, 1997
Chaperonins are a class of stress-inducible molecular chaperones involved in protein folding. We report the cloning, sequencing and characterisation of the rat mitochondrial chaperonin 60 and chaperonin 10 genes. The two genes are arranged in a head-to-head configuration and together comprise 14 kb and contain 14 introns.
Ryan, Michael T., Herd, Susanna M., Sberna, Gian, Samuel, Melanie M., Hoogenraad, Nicholas J., Hoj, Peter Bordier   +5 more
openaire   +5 more sources

Chaperonin 60 and mitochondrial disease in Dictyostelium.

Journal of muscle research and cell motility, 2003
The single Dictyostelium chaperonin 60 gene, hspA, was cloned, sequenced and characterized. Sequence comparisons and a three-dimensional model for the structure of the encoded protein showed that it exhibits the conserved sequence and structural features expected for its role as the Dictyostelium mitochondrial chaperonin 60. Dictyostelium hspA contains
Kotsifas, Martha., Barth, Christian., Lay, Sui., De Losanne, Arturo., Fisher, Paul Robert.   +4 more
openaire   +1 more source

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

Biochemistry, 1991
The spontaneous refolding of chemically denatured dihydrofolate reductase (DHFR) is completely arrested by chaperonin 60 (GroEL). This inhibition presumably results from the formation of a stable complex between chaperonin 60 and one or more intermediates in the folding pathway. While sequestered on chaperonin 60, DHFR is considerably more sensitive to
P V, Viitanen, G K, Donaldson, G H, Lorimer, T H, Lubben, A A, Gatenby   +4 more
openaire   +2 more sources

Chaperonin 60 regulation of SOX9 ubiquitination mitigates the development of knee osteoarthritis

Journal of Molecular Medicine, 2016
Articular cartilage integrity loss is a prominently deleterious feature of osteoarthritis (OA). The mechanistic underlying the development of OA warrants characterization. Heat shock proteins (HSPs), members of the chaperone family, reportedly orchestrate tissue homeostasis and remodeling in response to detrimental stress.
Jih-Yang, Ko, Yi-Chih, Sun, Wen-Chin, Li, Feng-Sheng, Wang   +3 more
openaire   +2 more sources