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Soluble CD30 binds to CD153 with high affinity and blocks transmembrane signaling by CD30

Soluble CD30 binds to CD153 with high affinity and blocks transmembrane signaling by CD30
Soluble CD30 binds to CD153 with high affinity and blocks transmembrane signaling by CD30
CD30 is an unusual member of the TNF receptor superfamily with a duplicated segment within its extracellular domain that may function as an additional ligand binding site. The extracellular domain of CD30 is shed from cells and soluble CD30 levels are elevated in certain disease states. Soluble CD30 may bind to its ligand, CD153, with high affinity and block its interaction with membrane-bound CD30. We have generated soluble recombinant forms of CD30 and CD153 in order to characterize their interaction and assess their biological activity. Soluble trimeric CD153 bound to membrane-anchored CD30 with a relatively high affinity (KD=23 nM) and was effective in triggering cell death and TNF- production in the presence of cross-linking antibodies. The affinity and kinetics of the interaction between soluble CD30 and CD153 were determined using the BIAcore biosensor. In contrast to other members of the TNF receptor superfamily, soluble monomeric CD30 bound to itsligand with high affinity (KD=4.5 nM) and prevented the interaction of cellular CD153 with immobilized CD30. Furthermore, soluble CD30 blocked cell death signals generated by cell surface-expressed CD30 effectively. These data suggest that soluble CD30 may have biological functions in vivo.
human TNF, TNF receptor superfamily, lymphoma, cell death
0014-2980
163-173
Hargreaves, Phillip G.
12b76f31-15ba-4f85-af32-a66e6c949416
Al-Shamkhani, Aymen
0a40b3ce-9d71-4d41-9369-7212f0a84504
Hargreaves, Phillip G.
12b76f31-15ba-4f85-af32-a66e6c949416
Al-Shamkhani, Aymen
0a40b3ce-9d71-4d41-9369-7212f0a84504

Hargreaves, Phillip G. and Al-Shamkhani, Aymen (2002) Soluble CD30 binds to CD153 with high affinity and blocks transmembrane signaling by CD30. European Journal of Immunology, 32 (1), 163-173. (doi:10.1002/1521-4141(200201)32:1<163::AID-IMMU163>3.0.CO;2-T).

Record type: Article

Abstract

CD30 is an unusual member of the TNF receptor superfamily with a duplicated segment within its extracellular domain that may function as an additional ligand binding site. The extracellular domain of CD30 is shed from cells and soluble CD30 levels are elevated in certain disease states. Soluble CD30 may bind to its ligand, CD153, with high affinity and block its interaction with membrane-bound CD30. We have generated soluble recombinant forms of CD30 and CD153 in order to characterize their interaction and assess their biological activity. Soluble trimeric CD153 bound to membrane-anchored CD30 with a relatively high affinity (KD=23 nM) and was effective in triggering cell death and TNF- production in the presence of cross-linking antibodies. The affinity and kinetics of the interaction between soluble CD30 and CD153 were determined using the BIAcore biosensor. In contrast to other members of the TNF receptor superfamily, soluble monomeric CD30 bound to itsligand with high affinity (KD=4.5 nM) and prevented the interaction of cellular CD153 with immobilized CD30. Furthermore, soluble CD30 blocked cell death signals generated by cell surface-expressed CD30 effectively. These data suggest that soluble CD30 may have biological functions in vivo.

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More information

Published date: 2002
Keywords: human TNF, TNF receptor superfamily, lymphoma, cell death

Identifiers

Local EPrints ID: 26359
URI: http://eprints.soton.ac.uk/id/eprint/26359
ISSN: 0014-2980
PURE UUID: 5a92251f-c7e9-4c57-89b1-03b87042f23f
ORCID for Aymen Al-Shamkhani: ORCID iD orcid.org/0000-0003-0727-4189

Catalogue record

Date deposited: 20 Apr 2006
Last modified: 03 Dec 2019 01:56

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