a(HBP:"protein aggregates")

Entity

Name

protein aggregates

Namespace

HBP

Namespace Version

20190126

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/77c0796c3ca82a80cb0eaf1c8380d6ccd7f323af/export/hbp-names.belns

Consequently, the formation of aggregates may increase when the UPS fails PubMed:14556719

Administration of cystamine, a transglutaminase inhibitor, can reduce aggregate formation and death in cells expressing atrophin-1 (DRPLA model) (Igarashi et al., 1998) and in cells expressing mutant androgen receptor (SBMA model) (Mandrusiak et al., 2003). PubMed:14556719

Administration of cystamine, a transglutaminase inhibitor, can reduce aggregate formation and death in cells expressing atrophin-1 (DRPLA model) (Igarashi et al., 1998) and in cells expressing mutant androgen receptor (SBMA model) (Mandrusiak et al., 2003). PubMed:14556719

Overexpression of the chaperone HSP70 has been found to reduce aggregate formation and death in nonneuronal cultured cells expressing mutant SOD1 (Bruening et al.,1999). PubMed:14556719

Alternatively, the enzyme itself may misfold and generate protein aggregates, thereby implicating a role for the UPS in disease pathogenesis (Cleveland and Liu, 2000; Julien, 2001;Valentine and Hart, 2003). PubMed:14556719

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Defective chaperone-mediated autophagy (CMA), a type of autophagy that targets proteins with a specific KFERQ-like motif recognizable to its chaperones, plays a significant role in aggregate formation of disease-related proteins [28]. PubMed:29758300

Although the UPS is accountable for the degradation of up to 80–90% of proteins, misfolded proteins and aggregates are too large to be processed through the proteasome barrel and can impede UPS function by physical occlusion, leaving autophagic-lysosomal breakdown as the only effective pathway to clear these proteins [25,26] PubMed:29758300

With neurons profoundly relying on macroautophagy for clearance of toxic protein aggregates, impairment in the proteolytic systems ultimately results in progressive neuronal death, a common feature in several neurodegenerative diseases [27]. PubMed:29758300

Lastly, macroautophagy, but not UPS or CMA can clear protein aggregates. PubMed:29758300

The presence of aberrant protein aggregates is common to neurodegenerative diseases PubMed:29758300

The lysosomal system, and specifically the autophagic pathway, is the principal mechanism for degrading proteins with long half-lives and is the only system in cells for degrading organelles and large protein aggregates or inclusions. PubMed:22908190

Recently, protein aggregates and certain organelles have been shown to be tagged with ubiquination for selective removal by autophagy (Narendra et al. 2009; Dikic et al. 2010; Youle et al. 2011), a degradative process previously believed to be only nonselective PubMed:22908190

Autophagy is the cell’s principal degradative pathway for eliminating unwanted organelles and long-lived proteins and for clearing damaged, aggregated, or obsolete proteins (Wong et al. 2010). PubMed:22908190

Preliminary in vitro studies demonstrated that two proteins, namely DISC1 and dysbindin-1, which are encoded by two susceptibility genes for schizophrenia, can form insoluble protein aggregates that are reminiscent of those occurring in neurodegenerative disorders PubMed:30061532

Preliminary in vitro studies demonstrated that two proteins, namely DISC1 and dysbindin-1, which are encoded by two susceptibility genes for schizophrenia, can form insoluble protein aggregates that are reminiscent of those occurring in neurodegenerative disorders PubMed:30061532

Recent findings demonstrate that soluble aggregated proteins can inhibit the ubiquitin system (Bence et al., 2001) PubMed:14556719

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

Overexpression of the HSPB8-BAG3 complex also stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, the accumulation of which characterizes many neurodegenerative disorders such as Alzheimer disease, Parkinson disease, and amyotrophic lateral sclerosis (Seidel et al., 2011). PubMed:22020111

The presence of aberrant protein aggregates is common to neurodegenerative diseases PubMed:29758300