NKR-P1, an activating molecule on rat natural killer cells, stimulates phosphoinositide turnover and a rise in intracellular calcium - PubMed (original) (raw)

. 1991 Nov 1;147(9):3244-50.

Affiliations

PMID: 1919012

NKR-P1, an activating molecule on rat natural killer cells, stimulates phosphoinositide turnover and a rise in intracellular calcium

J C Ryan et al. J Immunol. 1991.

Abstract

NKR-P1 is a 60-kDa homodimer expressed on all rat NK cells. Previous studies by others suggest that NKR-P1 may play a role in NK cell activation because antibody to NKR-P1 stimulates the release of granules from NK cells, and anti-NKR-P1 causes redirected lysis by activated NK cells against targets that express FcR. To examine the mechanism of transmembrane signaling by NKR-P1, we studied the rat NK cell line, RNK-16. We here demonstrate that F(ab')2 antibody to NKR-P1 stimulates phosphoinositide turnover and a rise in intracellular calcium within RNK-16 cells. The response is augmented by cross-linking the F(ab')2 antibody. The phosphoinositide/calcium pathway is also stimulated by NKR-P1 in activated rat NK cells, although no response is detectable in polymorphonuclear cells, which also express NKR-P1. We also demonstrate that RNK-16 cells kill the anti-NKR-P1 (3.2.3) hybridoma and that exposure to the hybridoma target cells stimulates phosphoinositide turnover in RNK-16 cells. Both killing and phosphoinositide turnover are inhibited by F(ab')2 anti-NKR-P1, implicating NKR-P1 in both responses. In contrast, neither cytotoxicity nor phosphoinositide turnover is appreciably blocked by F(ab')2 anti-NKR-P1 in response to YAC-1 targets. Thus, with either target, killing is linked to phosphoinositide turnover, but killing of YAC-1 involves pathways that differ from those that direct killing of the anti-NKR-P1 hybridoma. Our studies support the hypothesis that NKR-P1 may serve as an activating cell-surface receptor on NK cells, and they clarify the mechanisms by which it activates NK cells.

PubMed Disclaimer

Cited by

CD161B:ClrB interactions mediate activation of enhanced lysis of tumor target cells following NK cell:DC co-culture.
Yang T, Flint MS, Webb KM, Chambers WH. Yang T, et al. Immunol Res. 2006;36(1-3):43-50. doi: 10.1385/IR:36:1:43. Immunol Res. 2006. PMID: 17337765
Immunohistochemical Evidence of the Involvement of Natural Killer (CD161+) Cells in Spontaneous Regression of Lewis Rat Sarcoma.
Kovalska J, Cervinkova M, Chmelikova E, Planska D, Cizkova J, Horak V. Kovalska J, et al. In Vivo. 2019 Jan-Feb;33(1):47-52. doi: 10.21873/invivo.11437. In Vivo. 2019. PMID: 30587601 Free PMC article.
Transformation-associated 86 kDa natural killer target molecule expressed on the mouse, rat and human cell surface.
Qi W, Tamura Y, Takashima S, Sato N, Kikuchi K. Qi W, et al. Jpn J Cancer Res. 1994 Aug;85(8):862-8. doi: 10.1111/j.1349-7006.1994.tb02959.x. Jpn J Cancer Res. 1994. PMID: 7928633 Free PMC article.
Recognition of Listeria monocytogenes infection by natural killer cells: Towards a complete picture by experimental studies in rats.
Shegarfi H. Shegarfi H. Innate Immun. 2023 Aug;29(6):110-121. doi: 10.1177/17534259231178223. Epub 2023 Jun 7. Innate Immun. 2023. PMID: 37285590 Free PMC article. Review.
Association with FcRgamma is essential for activation signal through NKR-P1 (CD161) in natural killer (NK) cells and NK1.1+ T cells.
Arase N, Arase H, Park SY, Ohno H, Ra C, Saito T. Arase N, et al. J Exp Med. 1997 Dec 15;186(12):1957-63. doi: 10.1084/jem.186.12.1957. J Exp Med. 1997. PMID: 9396764 Free PMC article.

NKR-P1, an activating molecule on rat natural killer cells, stimulates phosphoinositide turnover and a rise in intracellular calcium - PubMed (original) (raw)