| Gamma-interferon-inducible lysosomal thiol reductase (GILT). Maturation, activity, and mechanism of action. | |
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MedLine Citation:
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PMID: 10852914 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We recently identified a gamma-interferon-inducible lysosomal thiol reductase (GILT), constitutively expressed in antigen-presenting cells, that catalyzes disulfide bond reduction both in vitro and in vivo and is optimally active at acidic pH. GILT is synthesized as a 35-kDa precursor, and following delivery to major histocompatibility complex (MHC) class II-containing compartments (MIICs), is processed to the mature 30-kDa form via cleavage of N- and C-terminal propeptides. The generation of MHC class II epitopes requires both protein denaturation and reduction of intra- and inter-chain disulfide bonds prior to proteolysis. GILT may be important in disulfide bond reduction of proteins delivered to MIICs and consequently in antigen processing. In this report we show that, like its mature form, precursor GILT reduces disulfide bonds with an acidic pH optimum, suggesting that it may also be involved in disulfide bond reduction in the endocytic pathway. We also show that processing of precursor GILT can be mediated by multiple lysosomal proteases and provide evidence that the mechanism of action of GILT resembles that of other thiol oxidoreductases. |
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Authors:
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U T Phan; B Arunachalam; P Cresswell |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 275 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2000 Aug |
Date Detail:
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Created Date: 2000-09-25 Completed Date: 2000-09-25 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 25907-14 Citation Subset: IM |
Affiliation:
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Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antigen-Presenting Cells / enzymology* COS Cells Catalysis Cell Line Disulfides / metabolism Endocytosis Enzyme Precursors / isolation & purification, metabolism* Histocompatibility Antigens Class II / metabolism Humans Hydrogen-Ion Concentration Molecular Weight Oxidoreductases / isolation & purification, metabolism* Oxidoreductases Acting on Sulfur Group Donors Protein Denaturation Rabbits |
| Grant Support | |
ID/Acronym/Agency:
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AI23081/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Disulfides; 0/Enzyme Precursors; 0/Histocompatibility Antigens Class II; EC 1.-/Oxidoreductases; EC 1.8.-/IFI30 protein, human; EC 1.8.-/Oxidoreductases Acting on Sulfur Group Donors |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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