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*
Sección de Inmunología, Hospital de la Princesa, Madrid, Spain;
Departamento de Bioquímica B e Inmunología, Universidad de Murcia, Murcia, Spain; and
Sección de Inmunología, Hospital Vírgen de la Arrixaca, Murcia, Spain
Some T lymphocytes express the CD94 Ag, which is known to form
heterodimers with members of the NKG2 family. We have studied the
expression pattern and function of CD94 heterodimers in different
ß or 
T cell clones. Most of the
CD94+NKG2A- T cells have a low to intermediate
expression of CD94 Ag. The cross-linking of the CD94/NKG2 heterodimer
in one of these CD8 ß CD94+NKG2A- T cell
clones (K14B06) was able to: 1) increase the intracellular
concentration of Ca2+, 2) induce the up-regulation of CD25
Ag expression and the secretion of IFN-, and 3) trigger redirected
cytotoxicity in a TCR-independent manner. This activatory property was
not shared by any other costimulatory molecule expressed by the K14B06
T cell clone, including CD8, CD28, CD45, CD69, or CD2 Ags. The
immunoprecipitation of CD94 heterodimer showed a 39-kDa band
with a similar m.w. to the activatory heterodimer found on some NK
clones. A novel form of the NKG2 family (NKG2H) was identified in
K14B06. NKG2H protein represents an alternative spliced form of the
NKG2E gene, displaying a charged residue in the transmembrane portion
and a cytoplasmic tail that lacks immunoreceptor tyrosine-based
inhibitory motifs. The expression of NKG2H in the cell membrane
through its association to CD94 and DAP-12 molecules supports that it
could form part of the activatory CD94/Kp39 heterodimer present on
K14B06 cells.
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