a(MESH:"Protein Aggregates")

Entity

Name

Protein Aggregates

Namespace

MeSH

Namespace Version

20181007

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/01c9daa61012b37dd0a1bc962521ba51a15b38f1/external/mesh-names.belns

HSP70s function in a variety of basic cellular quality control and maintenance processes, such as proper folding of newly synthesized proteins, along with preventing protein misfolding and aggregation through the binding of exposed hydrophobic residues. PubMed:27491084

Multiple studies in model systems demonstrate that overexpression of HSP70 can reduce toxicity and protein aggregation. PubMed:27491084

In addition to co-chaperones, overexpression of the human sHSP (HSPB7), a Caenorhabditis elegans HSP100 homolog (tor-2), and the yeast HSP60 subunit (CCT-1) and HSP90 homolog (HSP82) reduced toxicity and aggregation (Cao et al., 2005; Tam et al., 2006; Liang et al., 2008; Vos et al., 2010). PubMed:27491084

In addition to co-chaperones, overexpression of the human sHSP (HSPB7), a Caenorhabditis elegans HSP100 homolog (tor-2), and the yeast HSP60 subunit (CCT-1) and HSP90 homolog (HSP82) reduced toxicity and aggregation (Cao et al., 2005; Tam et al., 2006; Liang et al., 2008; Vos et al., 2010). PubMed:27491084

In addition to co-chaperones, overexpression of the human sHSP (HSPB7), a Caenorhabditis elegans HSP100 homolog (tor-2), and the yeast HSP60 subunit (CCT-1) and HSP90 homolog (HSP82) reduced toxicity and aggregation (Cao et al., 2005; Tam et al., 2006; Liang et al., 2008; Vos et al., 2010). PubMed:27491084

In addition to co-chaperones, overexpression of the human sHSP (HSPB7), a Caenorhabditis elegans HSP100 homolog (tor-2), and the yeast HSP60 subunit (CCT-1) and HSP90 homolog (HSP82) reduced toxicity and aggregation (Cao et al., 2005; Tam et al., 2006; Liang et al., 2008; Vos et al., 2010). PubMed:27491084

A key role of molecular chaperones is preventing pro- tein aggregation, especially under conditions of cellular stress. PubMed:23746257

Aggregated proteins that cannot be un- folded for proteasomal degradation may be removed by autophagy and lysosomal/vacuolar degradation. PubMed:23746257

Binding to GroEL prevents aggregation of these flexible folding intermediates, and subsequent folding depends critically on the global encapsulation of the substrate in the chaperonin cavity by the cochaperone GroES (7, 132–135). PubMed:23746257

The Hsp70 system acts synergistically with the cytosolic chaperonin TRiC to prevent aggregation of proteins with expanded polyglutamine tracts (165–168). PubMed:23746257

Hsp110 may function as holdases for nonnative proteins and cooperate with Hsp70 and Hsp40 in protein disaggregation (104, 124, 125). PubMed:23746257

ATP-independent chaperones, such as the small Hsps, may function as additional holdases that buffer aggregation. PubMed:23746257

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Heavily carbonylated proteins tend to form aggregates that are resistant to degradation and accumulate as unfolded or damaged proteins [101]. PubMed:24563850

Additional studies in mammalian peroxiredoxins showed that over-oxidation induces the formation of high molecular weight oligomers which function as potent chaperones and prevent protein aggregation [128,129]; PubMed:24563850

PDI is a redox sensitive chaperone that acts not only as a sensor but also as a protein involved in the processing of oxidized proteins and in preventing misfolding and/or aggregation of proteins. PubMed:24563850