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Functional knockdown of VCAM-1 at the posttranslational level with ER retained antibodies

Vascular cell adhesion molecule 1 (VCAM-1) is involved in the recruitment of leukocytes to inflammatory sites. In this study we present the first functional knockdown of VCAM-1 using an ER retained antibody construct. We generated a knockdown construct encoding the VCAM-1 specific single chain varia...

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Hauptverfasser: Strebe, Nina (VerfasserIn) , Guse, Annika (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 25 November 2008
In: Journal of immunological methods
Year: 2009, Jahrgang: 341, Heft: 1/2, Pages: 30-40
ISSN:1872-7905
DOI:10.1016/j.jim.2008.10.012
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1016/j.jim.2008.10.012
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0022175908003232
Volltext
Verfasserangaben:N. Strebe, A. Guse, M. Schüngel, T. Schirrmann, M. Hafner, T. Jostock, M. Hust, W. Müller, S. Dübel
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Zusammenfassung:Vascular cell adhesion molecule 1 (VCAM-1) is involved in the recruitment of leukocytes to inflammatory sites. In this study we present the first functional knockdown of VCAM-1 using an ER retained antibody construct. We generated a knockdown construct encoding the VCAM-1 specific single chain variable fragment scFv6C7.1 fused to the C-terminal ER retention sequence KDEL. HEK-293:VCAM-YFP cells stably expressing a VCAM-YFP fusion protein were transiently transfected with the knockdown construct and showed down-regulation of surface VCAM-1. Knockdown efficiency of the system is time-dependent due to used transient transfection of the intrabody construct. Furthermore, intrabody mediated knockdown of HEK-293:VCAM-YFP cells also impaired cell-cell interaction with Jurkat cells that are endogenously expressing VLA-4, the physiological partner of VCAM-1. Posttranslational knockdown with ER retained antibodies seems to be a promising technique, as shown here for VCAM-1.
Beschreibung:Gesehen am 10.05.2017
Beschreibung:Online Resource
ISSN:1872-7905
DOI:10.1016/j.jim.2008.10.012

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