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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2004-4-21
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pubmed:abstractText |
The asparagine-specific endoprotease (AEP) controls lysosomal processing of the potential autoantigen myelin basic protein (MBP) by human B lymphoblastoid cells, a feature implicated in the immunopathogenesis of multiple sclerosis. In this study, we demonstrate that freshly isolated human B lymphocytes lack significant AEP activity and that cleavage by AEP is dispensable for proteolytic processing of MBP in this type of cell. Instead, cathepsin (Cat) G, a serine protease that is not endogenously synthesized by B lymphocytes, is internalized from the plasma membrane and present in lysosomes from human B cells where it represents a major functional constituent of the proteolytic machinery. CatG initialized and dominated the destruction of intact MBP by B cell-derived lysosomal extracts, degrading the immunodominant MBP epitope and eliminating both its binding to MHC class II and a MBP-specific T cell response. Degradation of intact MBP by CatG was not restricted to a lysosomal environment, but was also performed by soluble CatG. Thus, the abundant protease CatG might participate in eliminating the immunodominant determinant of MBP. Internalization of exogenous CatG represents a novel mechanism of professional APC to acquire functionally dominant proteolytic activity that complements the panel of endogenous lysosomal enzymes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/CTSG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin G,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsg protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/asparaginylendopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1767
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pubmed:author |
pubmed-author:BeckAlexanderA,
pubmed-author:BrandenburgJensJ,
pubmed-author:BursterTimoT,
pubmed-author:DriessenChristophC,
pubmed-author:FalkKirstenK,
pubmed-author:KalbacherHubertH,
pubmed-author:LautweinAlfredA,
pubmed-author:LehmannRainerR,
pubmed-author:Marin-EstebanVivianaV,
pubmed-author:MelmsArthurA,
pubmed-author:RötzschkeOlafO,
pubmed-author:ReichMichaelM,
pubmed-author:SchwarzGeroldG,
pubmed-author:StevanovicStefanS,
pubmed-author:TolosaEvaE,
pubmed-author:WiendlHeinzH
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
172
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5495-503
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15100291-Adult,
pubmed-meshheading:15100291-Amino Acid Sequence,
pubmed-meshheading:15100291-Animals,
pubmed-meshheading:15100291-Antigen-Presenting Cells,
pubmed-meshheading:15100291-Asparagine,
pubmed-meshheading:15100291-B-Lymphocyte Subsets,
pubmed-meshheading:15100291-Cathepsin G,
pubmed-meshheading:15100291-Cathepsins,
pubmed-meshheading:15100291-Cell Line,
pubmed-meshheading:15100291-Cell Line, Transformed,
pubmed-meshheading:15100291-Cell Separation,
pubmed-meshheading:15100291-Cysteine Endopeptidases,
pubmed-meshheading:15100291-Humans,
pubmed-meshheading:15100291-Hydrolysis,
pubmed-meshheading:15100291-Lymphocyte Activation,
pubmed-meshheading:15100291-Lysine,
pubmed-meshheading:15100291-Lysosomes,
pubmed-meshheading:15100291-Mice,
pubmed-meshheading:15100291-Molecular Sequence Data,
pubmed-meshheading:15100291-Myelin Basic Proteins,
pubmed-meshheading:15100291-Phenylalanine,
pubmed-meshheading:15100291-Protein Processing, Post-Translational,
pubmed-meshheading:15100291-Serine,
pubmed-meshheading:15100291-Serine Endopeptidases
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pubmed:year |
2004
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pubmed:articleTitle |
Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes.
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pubmed:affiliation |
Department of Medicine II, University of Tübingen, Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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