| The islet-specific glucose-6-phosphatase-related protein, implicated in diabetes, is a glycoprotein embedded in the endoplasmic reticulum membrane. | |
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MedLine Citation:
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PMID: 15044018 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The islet-specific glucose-6-phosphatase-related protein (IGRP) has no known catalytic activity, but is of interest because it is the source of the peptide autoantigen targeted by a prevalent population of pathogenic CD8(+) T cells in non-obese diabetic mice. To better understand the potential roles of this protein in diabetes mellitus, we examine the subcellular localization and membrane topography of human IGRP. We show that IGRP is a glycoprotein, held in the endoplasmic reticulum by nine transmembrane domains, which is degraded in cells predominantly through the proteasome pathway that generates the major histocompatibility complex class I-presented peptides. |
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Authors:
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Jeng-Jer Shieh; Chi-Jiunn Pan; Brian C Mansfield; Janice Yang Chou |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: FEBS letters Volume: 562 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2004 Mar |
Date Detail:
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Created Date: 2004-03-26 Completed Date: 2004-05-11 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 160-4 Citation Subset: IM |
Affiliation:
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Section on Cellular Differentiation, Heritable Disorders Branch, National Institute of Child Health and Human Development, Building 10, Room 9S241, National Institutes of Health, Bethesda, MD 20892-1830, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acetylcysteine
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analogs & derivatives*,
metabolism Amino Acid Sequence Animals COS Cells Calreticulin / metabolism Cysteine Endopeptidases / metabolism Diabetes Mellitus / metabolism* Endoplasmic Reticulum / chemistry, metabolism* Enzyme Inhibitors / metabolism Glucose-6-Phosphatase* Glycoproteins / chemistry, genetics, metabolism* Humans Membrane Proteins / chemistry, genetics, metabolism* Mice Multienzyme Complexes / antagonists & inhibitors, metabolism Proteasome Endopeptidase Complex Protein Structure, Secondary Proteins / chemistry, genetics, metabolism* Recombinant Fusion Proteins / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Calreticulin; 0/Enzyme Inhibitors; 0/Glycoproteins; 0/Membrane Proteins; 0/Multienzyme Complexes; 0/Proteins; 0/Recombinant Fusion Proteins; 133343-34-7/lactacystin; 616-91-1/Acetylcysteine; EC 3.1.3.9/Glucose-6-Phosphatase; EC 3.1.3.9./G6PC2 protein, human; EC 3.1.3.9./G6pc2 protein, mouse; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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