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dc.contributor.authorAllen, Jenny R.
dc.contributor.authorNguyen, Linh X.
dc.contributor.authorSargent, Karen E.G.
dc.contributor.authorLipson, Kathryn L.
dc.contributor.authorHackett, Anthony
dc.contributor.authorUrano, Fumihiko
dc.date2022-08-11T08:08:58.000
dc.date.accessioned2022-08-23T16:14:05Z
dc.date.available2022-08-23T16:14:05Z
dc.date.issued2004-10-07
dc.date.submitted2008-06-23
dc.identifier.citationBiochem Biophys Res Commun. 2004 Nov 5;324(1):166-70. <a href="http://dx.doi.org/10.1016/j.bbrc.2004.09.035">Link to article on publisher's site</a>
dc.identifier.issn0006-291X (Print)
dc.identifier.doi10.1016/j.bbrc.2004.09.035
dc.identifier.pmid15464997
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33779
dc.description.abstractEndoplasmic reticulum (ER) stress, which is caused by the accumulation of misfolded proteins in the ER, elicits an adaptive response, the unfolded protein response (UPR). One component of the UPR, the endoplasmic reticulum-associated protein degradation (ERAD) system, has an important function in the survival of ER stressed cells. Here, we show that HRD1, a component of the ERAD system, is upregulated in pancreatic islets of the Akita diabetes mouse model and enhances intracellular degradation of misfolded insulin. High ER stress in beta-cells stimulated mutant insulin degradation through HRD1 to protect beta-cells from ER stress and ensuing death. If HRD1 serves the same function in humans, it may serve as a target for therapeutic intervention in diabetes.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15464997&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.bbrc.2004.09.035
dc.subjectAnimals; COS Cells; Cercopithecus aethiops; Diabetes Mellitus; Disease Models, Animal; Endoplasmic Reticulum; Humans; Insulin; Islets of Langerhans; Mice; Mice, Inbred Strains; Proteasome Endopeptidase Complex; inhibitors; Protein Conformation; *Protein Folding; Protein Subunits; Ubiquitin; Ubiquitin-Protein Ligases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleHigh ER stress in beta-cells stimulates intracellular degradation of misfolded insulin
dc.typeJournal Article
dc.source.journaltitleBiochemical and biophysical research communications
dc.source.volume324
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/44
dc.identifier.contextkey537407
html.description.abstract<p>Endoplasmic reticulum (ER) stress, which is caused by the accumulation of misfolded proteins in the ER, elicits an adaptive response, the unfolded protein response (UPR). One component of the UPR, the endoplasmic reticulum-associated protein degradation (ERAD) system, has an important function in the survival of ER stressed cells. Here, we show that HRD1, a component of the ERAD system, is upregulated in pancreatic islets of the Akita diabetes mouse model and enhances intracellular degradation of misfolded insulin. High ER stress in beta-cells stimulated mutant insulin degradation through HRD1 to protect beta-cells from ER stress and ensuing death. If HRD1 serves the same function in humans, it may serve as a target for therapeutic intervention in diabetes.</p>
dc.identifier.submissionpathgsbs_sp/44
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentProgram in Gene Function and Expression
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages166-70


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