Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity
- 10 November 1994
- journal article
- retracted article
- Published by Springer Nature in Nature
- Vol. 372 (6502) , 150-157
- https://doi.org/10.1038/372150a0
Abstract
THIS PAPER HAS BEEN RETRACTED; see retraction. A diversity of high-affinity Oligosaccharide ligands are identified for NKR-P1, a membrane protein on natural killer (NK) cells which contains an extracellular Ca2+-dependent lectin domain. Interactions of such oligosaccharides on the target cell surface with NKR-P1 on the killer cell surface are crucial both for target cell recognition and for delivery of stimulatory or inhibitory signals linked to the NK cytolytic machinery. NK-resistant tumour cells are rendered susceptible by preincubation with liposomes expressing NKR-P1 ligands, suggesting that purging of tumour or virally infected cells in vivo may be a therapeutic possibility.Keywords
This publication has 44 references indexed in Scilit:
- The Ly-49 and NKR-P1 Gene Families Encoding Lectin-Like Receptors on Natural Killer Cells: The NK Gene ComplexAnnual Review of Immunology, 1993
- Recognition structures on natural killer cellsCurrent Opinion in Immunology, 1993
- Immunosuppression by human gangliosidesCellular Immunology, 1992
- Carbohydrates in the functions of natural killer cellsGlycobiology, 1991
- PROTEOGLYCANS: STRUCTURES AND INTERACTIONSAnnual Review of Biochemistry, 1991
- NKR-P1, a Signal Transduction Molecule on Natural Killer CellsScience, 1990
- Lymphokine-activated killer cells in rats. III. A simple method for the purification of large granular lymphocytes and their rapid expansion and conversion into lymphokine-activated killer cells.The Journal of Experimental Medicine, 1988
- Inhibition of mouse natural killer cytotoxicity by heparinCellular Immunology, 1985
- Three types of blood group I specificity among monoclonal anti-I autoantibodies revealed by analogues of a branched erythrocyte glycolipid.The Journal of Experimental Medicine, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970