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Gene structure of the murine NK cell receptor 2B4: presence of two alternatively spliced isoforms with distinct cytoplasmic domains.

作者信息

Stepp S E, Schatzle J D, Bennett M, Kumar V, Mathew P A

机构信息

Immunology Graduate Program University of Texas Southwestern Medical Center, Dallas, USA.

出版信息

Eur J Immunol. 1999 Aug;29(8):2392-9. doi: 10.1002/(SICI)1521-4141(199908)29:08<2392::AID-IMMU2392>3.0.CO;2-R.

Abstract

The NK cell receptor 2B4 is expressed on the surface of all murine NK cells and a subset of T cells. Ligation of 2B4 with monoclonal antibodies increases target cell lysis and IFN-gamma production. 2B4 is the high-affinity counter-receptor for CD48 in mice and humans. 2B4-L is a member of the CD2 subgroup of the immunoglobulin supergene family, which includes CD48, LFA-3, CD84, Ly9 and SLAM. Here we describe 2B4-S, a second 2B4 isoform, and the genomic structure of the 2B4 gene. 2B4-S is identical to the 5' end of 2B4-L, differing only at the 3' end, corresponding to a portion of the cytoplasmic domain and the 3' untranslated sequence. Both 2B4-L and 2B4-S are expressed on IL-2-activated NK cells. The genomic clone of 2B4 reveals that the two cDNA clones are products of alternative splicing. Since they differ only in a portion of the cytoplasmic domain, it is likely that they transduce different signals.

摘要

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