Browse by author
Lookup NU author(s): Dr Andrew Knight
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Ectodomain shedding is a mechanism that regulates numerous functions of cell surface proteins. The extracellular domain of the human complement receptor 2 (CR2/CD21) is released by proteolytic cleavage as a soluble protein through a variety of stimuli including the thiol antioxidants N-acetylcysteine (NAC) and glutathione (GSH), and the oxidant pervanadate (PV). In addition, PV mimics B cell antigen receptor (BCR) signaling. Here, we show that murine CD21 is shed upon those stimuli and that the cytoplasmic domain is an important modulator for CD21-shedding. B cells expressing a mutant CD21 cytoplasmic domain with only three amino acids (KHR) showed increased CD21-shedding and required lower stimuli concentrations. At lower PV concentrations, wildtype CD21 was up-regulated on the cell surface, whereas at higher PV concentrations the ectodomain was shed. These findings further indicate that GSH and NAC utilize different pathways than PV to activate CD21-shedding. Altogether, as pre-activated B cells express higher CD21 levels than resting mature B cells or fully activated and antigen-experienced B cells, we suggest CD21-shedding to be a mechanism to fine-tune B cell activation. © 2007 Elsevier Ltd. All rights reserved.
Author(s): Hoefer MM, Aichem A, Knight AM, Illges H
Publication type: Article
Publication status: Published
Journal: Molecular Immunology
Year: 2008
Volume: 45
Issue: 8
Pages: 2127-2137
ISSN (print): 0161-5890
ISSN (electronic): 1872-9142
Publisher: Pergamon
URL: http://dx.doi.org/10.1016/j.molimm.2007.12.015
DOI: 10.1016/j.molimm.2007.12.015
PubMed id: 18295335
Altmetrics provided by Altmetric