Search results for "proteostasis network"

showing 2 items of 2 documents

Novel Modulators of Proteostasis: RNAi Screen of Chromosome I in a Heat Stress Paradigm in C. elegans

2018

Proteostasis is of vital importance for cellular function and it is challenged upon exposure to acute or chronic insults during neurodegeneration and aging. The proteostasis network is relevant for the maintenance of proteome integrity and mainly comprises molecular chaperones and two degradation pathways, namely, autophagy and the ubiquitin proteasome system. This network is characterized by an impressive functional interrelation and complexity, and occasionally novel factors are discovered that modulate proteostasis. Here, we present an RNAi screen in C. elegans, which aimed to identify modulators of proteostasis in a heat stress paradigm. The screen comprised genes that are located on ch…

0301 basic medicineautophagyproteostasis networkUPSArticle03 medical and health sciences0302 clinical medicinemedicinechaperonelcsh:QH301-705.5GeneRNAi screenGene knockdownproteostasisbiologyAutophagyNeurodegenerationneurodegenerationGeneral Medicinemedicine.diseaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)ProteasomeChaperone (protein)Proteomebiology.proteinC. elegans<i>C. elegans</i>; RNAi screen; proteostasis; proteostasis network; autophagy; UPS; chaperone; neurodegeneration030217 neurology & neurosurgeryCells
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The Chaperone Activity of Clusterin is Dependent on Glycosylation and Redox Environment

2014

Background/Aims: Clusterin (CLU), also known as Apolipoprotein J (ApoJ) is a highly glycosylated extracellular chaperone. In humans it is expressed from a broad spectrum of tissues and related to a plethora of physiological and pathophysiological processes, such as Alzheimer's disease, atherosclerosis and cancer. In its dominant form it is expressed as a secretory protein (secreted CLU, sCLU). During its maturation, the sCLU-precursor is N-glycosylated and cleaved into an α- and a β-chain, which are connected by five symmetrical disulfide bonds. Recently, it has been demonstrated that besides the predominant sCLU, rare intracellular CLU forms are expressed in stressed cells. Since these for…

DNA ComplementaryGlycosylationGlycosylationPhysiologyMutantCarbohydrateslcsh:Physiologylcsh:Biochemistrychemistry.chemical_compoundChaperonesHumanslcsh:QD415-436Redox biologySecretory pathwaylcsh:QP1-981ClusterinbiologyRetro-translocationProprotein convertaseProteostasis networkOxidative StressClusterinSecretory proteinHeat shockchemistryBiochemistryApolipoprotein JChaperone (protein)Proteolysisbiology.proteinOxidation-ReductionIntracellularMolecular ChaperonesFurin-like proprotein convertasesCellular Physiology and Biochemistry
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