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Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells

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Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells. / Burster, Timo; Beck, Alexander; Tolosa, Eva; Schnorrer, Petra; Weissert, Robert; Reich, Michael; Kraus, Marianne; Kalbacher, Hubert; Häring, Hans-Ulrich; Weber, Ekkehard; Overkleeft, Herman; Driessen, Christoph.

in: J IMMUNOL, Jahrgang 175, Nr. 9, 01.11.2005, S. 5940-9.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Burster, T, Beck, A, Tolosa, E, Schnorrer, P, Weissert, R, Reich, M, Kraus, M, Kalbacher, H, Häring, H-U, Weber, E, Overkleeft, H & Driessen, C 2005, 'Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells', J IMMUNOL, Jg. 175, Nr. 9, S. 5940-9.

APA

Burster, T., Beck, A., Tolosa, E., Schnorrer, P., Weissert, R., Reich, M., Kraus, M., Kalbacher, H., Häring, H-U., Weber, E., Overkleeft, H., & Driessen, C. (2005). Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells. J IMMUNOL, 175(9), 5940-9.

Vancouver

Burster T, Beck A, Tolosa E, Schnorrer P, Weissert R, Reich M et al. Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells. J IMMUNOL. 2005 Nov 1;175(9):5940-9.

Bibtex

@article{03f1ab557a6a4723ba8ad9db5059ab4e,
title = "Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells",
abstract = "Dendritic cells (DC) initiate immunity and maintain tolerance. Although in vitro-generated DC, usually derived from peripheral blood monocytes (MO-DC), serve as prototype DC to analyze the biology and biochemistry of DC, phenotypically distinct primary types of DC, including CD1c-DC, are present in peripheral blood (PB-DC). The composition of lysosomal proteases in PB-DC and the way their MHC class II-associated Ag-processing machinery handles a clinically relevant Ag are unknown. We show that CD1c-DC lack significant amounts of active cathepsins (Cat) S, L, and B as well as the asparagine-specific endopeptidase, the major enzymes believed to mediate MHC class II-associated Ag processing. However, at a functional level, lysosomal extracts from CD1c-DC processed the multiple sclerosis-associated autoantigens myelin basic protein and myelin oligodendrocyte glycoprotein in vitro more effectively than MO-DC. Although processing was dominated by CatS, CatD, and asparagine-specific endopeptidase in MO-DC, it was dominated by CatG in CD1c-DC. Thus, human MO-DC and PB-DC significantly differ with respect to their repertoire of active endocytic proteases, so that both proteolytic machineries process a given autoantigen via different proteolytic pathways.",
keywords = "Antigen Presentation, Antigens, CD1, Autoantigens, Cathepsins, Dendritic Cells, Endocytosis, Glycoproteins, Humans, Lysosomes, Monocytes, Myelin Basic Protein, Myelin Proteins, Myelin-Associated Glycoprotein, Myelin-Oligodendrocyte Glycoprotein, RNA, Messenger",
author = "Timo Burster and Alexander Beck and Eva Tolosa and Petra Schnorrer and Robert Weissert and Michael Reich and Marianne Kraus and Hubert Kalbacher and Hans-Ulrich H{\"a}ring and Ekkehard Weber and Herman Overkleeft and Christoph Driessen",
year = "2005",
month = nov,
day = "1",
language = "English",
volume = "175",
pages = "5940--9",
journal = "J IMMUNOL",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "9",

}

RIS

TY - JOUR

T1 - Differential processing of autoantigens in lysosomes from human monocyte-derived and peripheral blood dendritic cells

AU - Burster, Timo

AU - Beck, Alexander

AU - Tolosa, Eva

AU - Schnorrer, Petra

AU - Weissert, Robert

AU - Reich, Michael

AU - Kraus, Marianne

AU - Kalbacher, Hubert

AU - Häring, Hans-Ulrich

AU - Weber, Ekkehard

AU - Overkleeft, Herman

AU - Driessen, Christoph

PY - 2005/11/1

Y1 - 2005/11/1

N2 - Dendritic cells (DC) initiate immunity and maintain tolerance. Although in vitro-generated DC, usually derived from peripheral blood monocytes (MO-DC), serve as prototype DC to analyze the biology and biochemistry of DC, phenotypically distinct primary types of DC, including CD1c-DC, are present in peripheral blood (PB-DC). The composition of lysosomal proteases in PB-DC and the way their MHC class II-associated Ag-processing machinery handles a clinically relevant Ag are unknown. We show that CD1c-DC lack significant amounts of active cathepsins (Cat) S, L, and B as well as the asparagine-specific endopeptidase, the major enzymes believed to mediate MHC class II-associated Ag processing. However, at a functional level, lysosomal extracts from CD1c-DC processed the multiple sclerosis-associated autoantigens myelin basic protein and myelin oligodendrocyte glycoprotein in vitro more effectively than MO-DC. Although processing was dominated by CatS, CatD, and asparagine-specific endopeptidase in MO-DC, it was dominated by CatG in CD1c-DC. Thus, human MO-DC and PB-DC significantly differ with respect to their repertoire of active endocytic proteases, so that both proteolytic machineries process a given autoantigen via different proteolytic pathways.

AB - Dendritic cells (DC) initiate immunity and maintain tolerance. Although in vitro-generated DC, usually derived from peripheral blood monocytes (MO-DC), serve as prototype DC to analyze the biology and biochemistry of DC, phenotypically distinct primary types of DC, including CD1c-DC, are present in peripheral blood (PB-DC). The composition of lysosomal proteases in PB-DC and the way their MHC class II-associated Ag-processing machinery handles a clinically relevant Ag are unknown. We show that CD1c-DC lack significant amounts of active cathepsins (Cat) S, L, and B as well as the asparagine-specific endopeptidase, the major enzymes believed to mediate MHC class II-associated Ag processing. However, at a functional level, lysosomal extracts from CD1c-DC processed the multiple sclerosis-associated autoantigens myelin basic protein and myelin oligodendrocyte glycoprotein in vitro more effectively than MO-DC. Although processing was dominated by CatS, CatD, and asparagine-specific endopeptidase in MO-DC, it was dominated by CatG in CD1c-DC. Thus, human MO-DC and PB-DC significantly differ with respect to their repertoire of active endocytic proteases, so that both proteolytic machineries process a given autoantigen via different proteolytic pathways.

KW - Antigen Presentation

KW - Antigens, CD1

KW - Autoantigens

KW - Cathepsins

KW - Dendritic Cells

KW - Endocytosis

KW - Glycoproteins

KW - Humans

KW - Lysosomes

KW - Monocytes

KW - Myelin Basic Protein

KW - Myelin Proteins

KW - Myelin-Associated Glycoprotein

KW - Myelin-Oligodendrocyte Glycoprotein

KW - RNA, Messenger

M3 - SCORING: Journal article

C2 - 16237087

VL - 175

SP - 5940

EP - 5949

JO - J IMMUNOL

JF - J IMMUNOL

SN - 0022-1767

IS - 9

ER -