Document Detail


The islet-specific glucose-6-phosphatase-related protein, implicated in diabetes, is a glycoprotein embedded in the endoplasmic reticulum membrane.
MedLine Citation:
PMID:  15044018     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Jeng-Jer Shieh; Chi-Jiunn Pan; Brian C Mansfield; Janice Yang Chou
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  562     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-26     Completed Date:  2004-05-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  160-4     Citation Subset:  IM    
Affiliation:
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.
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MeSH Terms
Descriptor/Qualifier:
Acetylcysteine / 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:
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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