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Pre-assembly of the extracellular domains of CD40 is not necessary for rescue of mouse B cells from anti-immunoglobulin M-induced apoptosis

Author:
  • Peter Ellmark
  • Christina Furebring
  • Carl Borrebaeck
Publishing year: 2003
Language: English
Pages: 452-457
Publication/Series: Immunology
Volume: 108
Issue: 4
Document type: Journal article
Publisher: Wiley-Blackwell

Abstract english

CD40 is a tumour necrosis factor receptor (TNFR) family member of central importance for the adaptive immune system. To elucidate the functional role of the different extracellular domains of CD40, we have created a set of truncated CD40 molecules where domains, or parts of domains, have been removed. These CD40 proteins, which contain a peptide tag in the N-terminal end, have been expressed in a murine B-cell line, WEHI 231. It was found that ligation of these engineered CD40 proteins via the peptide tag, was sufficient to rescue as well as to promote proliferation of apoptotic WEHI 231 cells, even when all the extracellular domains of CD40 were absent. Our results suggest that pre association of CD40 in the cell membrane plays no critical role for the CD40 signalling pathway. Furthermore, our data imply that conformational changes initiated in the extracellular domains of CD40 are not essential for signal transduction.

Keywords

  • Immunology in the medical area

Other

Published
  • ISSN: 0019-2805
Carl B
Carl Borrebaeck
E-mail: carl.borrebaeck [at] immun.lth.se

Professor

Department of Immunotechnology

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