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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

Ellmark, Peter LU ; Furebring, Christina LU and Borrebaeck, Carl LU (2003) In Immunology 108(4). p.452-457
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Immunology
volume
108
issue
4
pages
452 - 457
publisher
Wiley-Blackwell
external identifiers
  • pmid:12667206
  • wos:000181966900004
  • scopus:0037394866
ISSN
0019-2805
DOI
10.1046/j.1365-2567.2003.01622.x
language
English
LU publication?
yes
id
b0d8f9cb-7484-4742-a57e-070ed376de69 (old id 134281)
date added to LUP
2007-06-28 09:38:40
date last changed
2018-01-07 05:52:04
@article{b0d8f9cb-7484-4742-a57e-070ed376de69,
  abstract     = {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.},
  author       = {Ellmark, Peter and Furebring, Christina and Borrebaeck, Carl},
  issn         = {0019-2805},
  language     = {eng},
  number       = {4},
  pages        = {452--457},
  publisher    = {Wiley-Blackwell},
  series       = {Immunology},
  title        = {Pre-assembly of the extracellular domains of CD40 is not necessary for rescue of mouse B cells from anti-immunoglobulin M-induced apoptosis},
  url          = {http://dx.doi.org/10.1046/j.1365-2567.2003.01622.x},
  volume       = {108},
  year         = {2003},
}