The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway

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Standard

The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway. / Uhlenbrock, Franziska Katharina; Hagemann-Jensen, Michael Henrik; Kehlet, Stephanie; Andresen, Lars; Pastorekova, Silvia; Skov, Søren.

I: Journal of immunology (Baltimore, Md. : 1950), Bind 193, Nr. 4, 2014, s. 1654-1665.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Uhlenbrock, FK, Hagemann-Jensen, MH, Kehlet, S, Andresen, L, Pastorekova, S & Skov, S 2014, 'The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway', Journal of immunology (Baltimore, Md. : 1950), bind 193, nr. 4, s. 1654-1665. https://doi.org/10.4049/jimmunol.1303275

APA

Uhlenbrock, F. K., Hagemann-Jensen, M. H., Kehlet, S., Andresen, L., Pastorekova, S., & Skov, S. (2014). The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway. Journal of immunology (Baltimore, Md. : 1950), 193(4), 1654-1665. https://doi.org/10.4049/jimmunol.1303275

Vancouver

Uhlenbrock FK, Hagemann-Jensen MH, Kehlet S, Andresen L, Pastorekova S, Skov S. The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway. Journal of immunology (Baltimore, Md. : 1950). 2014;193(4):1654-1665. https://doi.org/10.4049/jimmunol.1303275

Author

Uhlenbrock, Franziska Katharina ; Hagemann-Jensen, Michael Henrik ; Kehlet, Stephanie ; Andresen, Lars ; Pastorekova, Silvia ; Skov, Søren. / The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway. I: Journal of immunology (Baltimore, Md. : 1950). 2014 ; Bind 193, Nr. 4. s. 1654-1665.

Bibtex

@article{5b898adb61dc4e05a584ffb850b50120,
title = "The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway",
abstract = "Soluble ULBP2 is a marker for poor prognosis in several types of cancer. In this study we demonstrate that both soluble and cell surface-bound ULBP2 is transported via a so far unrecognized endosomal pathway. ULBP2 surface expression, but not MICA/B, could specifically be targeted and retained by affecting endosomal/lysosomal integrity and protein kinase C activity. The invariant chain was further essential for endosomal transport of ULBP2. This novel pathway was identified through screening experiments by which methylselenic acid was found to possess notable NKG2D ligand regulatory properties. The protein kinase C inhibitor methylselenic acid induced MICA/B surface expression but dominantly blocked ULBP2 surface transport. Remarkably, by targeting this novel pathway we could specifically block the production of soluble ULBP2 from different, primary melanomas. Our findings strongly suggest that the endosomal transport pathway constitutes a novel therapeutic target for ULBP2-producing tumors.",
author = "Uhlenbrock, {Franziska Katharina} and Hagemann-Jensen, {Michael Henrik} and Stephanie Kehlet and Lars Andresen and Silvia Pastorekova and S{\o}ren Skov",
note = "Copyright {\textcopyright} 2014 by The American Association of Immunologists, Inc.",
year = "2014",
doi = "10.4049/jimmunol.1303275",
language = "English",
volume = "193",
pages = "1654--1665",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "4",

}

RIS

TY - JOUR

T1 - The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway

AU - Uhlenbrock, Franziska Katharina

AU - Hagemann-Jensen, Michael Henrik

AU - Kehlet, Stephanie

AU - Andresen, Lars

AU - Pastorekova, Silvia

AU - Skov, Søren

N1 - Copyright © 2014 by The American Association of Immunologists, Inc.

PY - 2014

Y1 - 2014

N2 - Soluble ULBP2 is a marker for poor prognosis in several types of cancer. In this study we demonstrate that both soluble and cell surface-bound ULBP2 is transported via a so far unrecognized endosomal pathway. ULBP2 surface expression, but not MICA/B, could specifically be targeted and retained by affecting endosomal/lysosomal integrity and protein kinase C activity. The invariant chain was further essential for endosomal transport of ULBP2. This novel pathway was identified through screening experiments by which methylselenic acid was found to possess notable NKG2D ligand regulatory properties. The protein kinase C inhibitor methylselenic acid induced MICA/B surface expression but dominantly blocked ULBP2 surface transport. Remarkably, by targeting this novel pathway we could specifically block the production of soluble ULBP2 from different, primary melanomas. Our findings strongly suggest that the endosomal transport pathway constitutes a novel therapeutic target for ULBP2-producing tumors.

AB - Soluble ULBP2 is a marker for poor prognosis in several types of cancer. In this study we demonstrate that both soluble and cell surface-bound ULBP2 is transported via a so far unrecognized endosomal pathway. ULBP2 surface expression, but not MICA/B, could specifically be targeted and retained by affecting endosomal/lysosomal integrity and protein kinase C activity. The invariant chain was further essential for endosomal transport of ULBP2. This novel pathway was identified through screening experiments by which methylselenic acid was found to possess notable NKG2D ligand regulatory properties. The protein kinase C inhibitor methylselenic acid induced MICA/B surface expression but dominantly blocked ULBP2 surface transport. Remarkably, by targeting this novel pathway we could specifically block the production of soluble ULBP2 from different, primary melanomas. Our findings strongly suggest that the endosomal transport pathway constitutes a novel therapeutic target for ULBP2-producing tumors.

U2 - 10.4049/jimmunol.1303275

DO - 10.4049/jimmunol.1303275

M3 - Journal article

C2 - 25024379

VL - 193

SP - 1654

EP - 1665

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 4

ER -

ID: 124556574