PMID: 8955184Dec 15, 1996Paper

Biochemical and serologic evidence for the existence of functionally distinct forms of the CD94 NK cell receptor

The Journal of Immunology : Official Journal of the American Association of Immunologists
J J Pérez-VillarM López-Botet

Abstract

The CD94 NK cell receptor is assembled as a disulfide-linked dimer and appears to be encoded by a single-copy gene of the C-type lectin superfamily. In reverse Ab-dependent cellular cytotoxicity assays, CD94-specific mAbs may either trigger or inhibit cytotoxicity in distinct subsets of NK clones, termed groups A and B, respectively. The molecular basis for this functional ambivalence of CD94 has been addressed. CD94 molecules immunoprecipitated with the HP-3B1 mAb from the two different subsets of NK clones were comparatively analyzed by SDS-PAGE. Under reducing conditions, the stimulating form of CD94 from group A clones displayed a significantly lower Mr (39 kDa) than the inhibitory form of group B clones (Mr = 43 kDa). Analyses of N-glycanase and V8 protease-digested samples indicated that the two CD94 forms are homologous. A CD94-specific mAb (Z199) that did not recognize cells transfected with a CD94 cDNA (LL288) was characterized. Z199 did not bind to group A clones, whereas its reactivity with group B NK cells was indistinguishable from that of other CD94-specific mAbs. Different from the HP-3B1 mAb, the Z199 mAb displayed only inhibitory effects in reverse Ab-dependent cellular cytotoxicity assays. Immunoprecipitation ...Continue Reading

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