Molecular chaperones: Toward new therapeutic tools

Almeida, Mauro Brito de; Nascimento, José Luíz Martins do; Herculano, Anderson Manoel; Crespo-López, María Elena

doi:10.1016/j.biopha.2011.04.025

Cited by 45 publications

(43 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Molecular chaperones have been proposed to be therapeutic targets (Almeida et al 2011). TRiC may play a role in suppressing Huntington's disease by decreasing huntingtin aggregate formation (Kitamura et al 2006;Tam et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro

Knee

Sergeeva

King

2013

Cell Stress and Chaperones

View full text Add to dashboard Cite

Archaeal and eukaryotic cytosols contain group II chaperonins, which have a double-barrel structure and fold proteins inside a cavity in an ATP-dependent manner. The most complex of the chaperonins, the eukaryotic TCP-1 ring complex (TRiC), has eight different subunits, chaperone containing TCP-1 (CCT1-8), that are arranged so that there is one of each subunit per ring. Aspects of the structure and function of the bovine and yeast TRiC have been characterized, but studies of human TRiC have been limited. We have isolated and purified endogenous human TRiC from HeLa suspension cells. This purified human TRiC contained all eight CCT subunits organized into double-barrel rings, consistent with what has been found for bovine and yeast TRiC. The purified human TRiC is active as demonstrated by the luciferase refolding assay. As a more stringent test, the ability of human TRiC to suppress the aggregation of human γD-crystallin was examined. In addition to suppressing offpathway aggregation, TRiC was able to assist the refolding of the crystallin molecules, an activity not found with the lens chaperone, α-crystallin. Additionally, we show that human TRiC from HeLa cell lysate is associated with the heat shock protein 70 and heat shock protein 90 chaperones. Purification of human endogenous TRiC from HeLa cells will enable further characterization of this key chaperonin, required for the reproduction of all human cells.

show abstract

Section: Discussionmentioning

confidence: 99%

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro

Knee

Sergeeva

King

2013

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…2 It was later shown that the HSPs allow cells to survive a wide range of both endogenous and exogenous insults including cytotoxic agents, oxidants, heavy metals and infection. 3,4 In response to these stressors, the transcriptional regulator HSF1, in concert with family member HSF2, mediates heat shock gene transcription to enact the stress response and increase cellular HSP levels. 5 The HSPs are categorized by molecular weight and include members Hsp100 (this HSP has no mammalian homolog, though is characterized in bacteria and yeast), Hsp90, Hsp70, Hsp60, HSP40 and the small HSPs, which range between 13-42 kDa 3,[6][7][8] ( Table 1).…”

Section: The Heat Shock Proteins-overviewmentioning

confidence: 99%

“…3,4 In response to these stressors, the transcriptional regulator HSF1, in concert with family member HSF2, mediates heat shock gene transcription to enact the stress response and increase cellular HSP levels. 5 The HSPs are categorized by molecular weight and include members Hsp100 (this HSP has no mammalian homolog, though is characterized in bacteria and yeast), Hsp90, Hsp70, Hsp60, HSP40 and the small HSPs, which range between 13-42 kDa 3,[6][7][8] ( Table 1). The HSPs serve predominantly as molecular chaperones for other cellular proteins; high molecular weight HSPs require ATP as well, whereas low molecular weight HSPs are ATP-independent.…”

Section: The Heat Shock Proteins-overviewmentioning

confidence: 99%

The heat shock proteins as targets for radiosensitization and chemosensitization in cancer

Guttmann

Koumenis²

2011

Cancer Biology & Therapy

View full text Add to dashboard Cite

“…54 The report of 14-3-3 proteins relationship with DR is limited to a study that shows expression change in early diabetic rat retinal proteomes versus normal. 25 Chaperones like HSPA8 increase cell survival 55 and play a key role in the maintenance of epithelial cell structure and function and are also responsible for cell repair processes after damage, proliferation, apoptosis and modulate cell signaling. 56 .…”

Section: Discussionmentioning

confidence: 99%

Diabetic Retinopathy and Laser Therapy in Rats: A Protein-Protein Interaction Network Analysis

et al. 2017

View full text Add to dashboard Cite

Introduction: Diabetic retinopathy (DR) is a serious microvascular complication of diabetes which can cause vision loss or blindness ultimately. Non enzymatic glycation of proteins leads to advanced glycation end products (AGEs) in DR. Since laser therapy is a well-established method, in this study, protein-protein interaction (PPI) network is applied for protein targets in DR disease in rats treated by laser. Methods: In this study, we focused on articles that investigated and compared the proteome profiles of DR rats with healthy control and also DR rats before and after laser therapy. The networks of related differentially expressed proteins were explored using Cytoscape version 3.3.0, the PPI analysis methods and ClueGO. Results: Analysis of PPI network of 37 related proteins to DR rats including 108 nodes, introduced 10 hub-bottleneck proteins and 5 concerned biochemical pathways. On the other hand, PPI analysis of related proteins to DR rats before and after laser therapy corresponded to 33 proteins and 2 biological pathways. Discussion: Centrality and cluster screening identified hub-bottelneck genes, including Aldoa, HSPD1, Pgam2, Mapk3, SLC2A4, Ctnnb1, Ywhab, HSPA8, GAPDH and Actb for DR rats versus healthy control and ENO1, Aldoa, GAPDH for DR samples after laser therapy. Conclusion: Gene expression analysis of the DR samples treated via laser therapy provides a molecular evidence in support of the therapeutic effect of laser.

show abstract

Molecular chaperones: Toward new therapeutic tools

Cited by 45 publications

References 52 publications

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro

The heat shock proteins as targets for radiosensitization and chemosensitization in cancer

Diabetic Retinopathy and Laser Therapy in Rats: A Protein-Protein Interaction Network Analysis

Contact Info

Product

Resources

About