0000000001064117

AUTHOR

Benjamin Renner

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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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