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Volume 272, Number 50, Issue of December 12, 1997 pp. 31604-31608

Functional Coupling of NKR-P1 Receptors to Various Heterotrimeric G Proteins in Rat Interleukin-2-activated Natural Killer Cells

(Received for publication, August 7, 1997, and in revised form, September 19, 1997)

From the Department of Anatomy, Institute of Basic Medical Sciences, University of Oslo, N-0317 Oslo, Norway

NKR-P1 molecules constitute a family of type II membrane receptors in natural killer (NK) cells that preferentially activate NK cell killing and release of interferon- from these cells. Here, we demonstrate that anti-NKR-P1 enhances GTP binding in rat interleukin-2-activated NK cell membranes; GTP binding to G_i3, G_s, G_q,11, and G_z increased noticeably in these cell membranes after treatment with anti-NKR-P1. Western blot analysis of membrane proteins prepared from interleukin-2-activated NK cells reveals the presence of G_i1,2, G_i3, G_o, G_s, G_q,11, G_z, and G₁₂, but not G₁₃. However, only _i3, _s, _q,11, and _z, but not _i1,2, _o, ₁₂, or ₁₃ subunits when immunoprecipitated with the appropriate anti-G protein antibodies, are associated with NKR-P1 when immunoblotted with anti-NKR-P1. Reciprocally, NKR-P1 immunoprecipitated with anti-NKR-P1 is associated with _i3, _s, _q,11, and _z immunoblotted with anti-G proteins. These results are the first to demonstrate the physical and functional coupling of NKR-P1 to the heterotrimeric G proteins in NK cells.

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