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Gene Review

Klrb1@  -  Killer cell lectin-like receptor subfamily...

Rattus norvegicus

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Disease relevance of Klrb1@

  • We also compared the lytic capacity of NKR-P1+ populations derived from normal animals and from 9L gliosarcomas [1].
 

High impact information on Klrb1@

  • Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity [2].
  • 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 [2].
  • Rat spleen dendritic cells express natural killer cell receptor protein 1 (NKR-P1) and have cytotoxic activity to select targets via a Ca2+-dependent mechanism [3].
  • By one-parameter flow cytometry, it was determined that NKR-P1+ cells constituted 30-60% of the lymphocytes in 9L tumors [1].
  • Previous investigations have determined the existence of three populations of NKR-P1+ lymphocytes in normal rats, including NKR-P1bright/T-cell receptor (TCR)-/CD3-/CD5- (approximately 5-15%), NKR-P1dim-/TCRalphabeta+/CD3+/CD5+ (approximately 1-5%), and NKR-P1dim/TCRgammadelta+/CD3+/CD5+ (approximately 0.5-2%) [1].
 

Biological context of Klrb1@

  • NKR-P1, a signal transduction molecule on natural killer cells [4].
  • Cells of this phenotype have not been reported previously, and most likely represent NK cells down-modulated for expression of NKR-P1 [1].
  • These data indicate that NKR-P1bright/L.E.bright and NKR-P1bright/L.E.dim subpopulations of rat NK cells have different capacities for: 1) triggering through NKR-P1; and 2) E-A rosette formation and lysis of antibody-sensitized target cells by ADCC [5].
  • Dimerization of soluble NKR-P1 is predominantly dependent on the presence of an intact juxta-membrane stalk region and independent of N-glycosylation [6].
  • However, spontaneous functions of liver-resident NK cells, including killing of YAC-1 and P815 targets, Ab-dependent cellular cytotoxicity, and redirected killing via NKR-P1, were continuously suppressed throughout the entire period of liver regeneration (from 3 h to 14 days) [7].
 

Anatomical context of Klrb1@

  • We have expressed a full-length NKR-P1 protein of the rat in COS cells and prepared soluble extracellular fragments by controlled proteolysis or by expression of truncated cDNA in bacteria [6].
  • We previously reported that the 70-kDa heat shock cognate protein-like molecule (hsc70) is expressed on the cell surface along with the neoplastic transformation of rat fibroblast and that this molecule is recognized by CD3+, CD4-, CD8-, NKR-P1-, and TCR-alphabeta- T (DNT) killer cells in an MHC class I-unrestricted fashion [8].
  • Immunoprecipitation studies showed that p56(lck) can be co-immunoprecipitated with NKR-P1 from a rat NK tumor cell line [9].
  • Flow cytometry analysis before and at disease onset revealed a higher proportion of lymph node T cells expressing NKR-P1 in the disease-resistant LEW.1AV1 compared with the disease-susceptible DA strain, suggesting that NK T cells might be disease protective [10].
  • In graft recipients it was evident that activated monocytes were able to express and upregulate NKR-P1 and CD8, which have not been detected in these cells to date [11].
 

Associations of Klrb1@ with chemical compounds

  • We here demonstrate that F(ab')2 antibody to NKR-P1 stimulates phosphoinositide turnover and a rise in intracellular calcium within RNK-16 cells [12].
  • The CD45-negative cells expressed CD2, CD53, and NKR-P1, but mAb-induced perturbations of these molecules did not induce protein tyrosine phosphorylations and increases in the concentration of cytoplasmic-free calcium, as occurred in the wild-type RNK-16 [13].
  • Binding and inhibition studies using monosaccharides and neoglycoconjugates indicate that NKR-P1 is a lectin with a preference order of GalNAc > GlcNAc >> Fuc >> Gal > Man. At neutral pH, Ca2+ is tightly associated with the protein such that only a proportion can be removed by 10 mM EGTA [6].
  • Thy cytoplamic domain of rat NKR-P1 receptor interacts with the N-terminal domain of p56(lck) via cysteine residues [14].
  • NKR-P1 triggering, which is known to induce NK cell activation and mediate reverse ADCC, was able to induce arginine metabolism with consequent increase of nitrite and citrulline levels [15].
 

Other interactions of Klrb1@

  • In contrast, this protection was not abolished by the addition of anti-rat IL-2 or anti-rat TNF-alpha, or by the depletion of NKR-P1-bearing cells within gammadelta T cells [16].
  • 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-gamma from these cells [17].
  • Functional coupling of NKR-P1 receptors to various heterotrimeric G proteins in rat interleukin-2-activated natural killer cells [17].
  • In addition, the NK subpopulation exhibiting the allocytolytic activity in alloimmunized rats exhibited a decreased expression of the NKR-P1 and L-selectin molecules, but an increased expression of the LFA-1 molecule when compared to NK cells from naive rats [18].
 

Analytical, diagnostic and therapeutic context of Klrb1@

References

  1. NKR-P1+ cells localize selectively in Rat 9L gliosarcomas but have reduced cytolytic function. Chambers, W.H., Bozik, M.E., Brissette-Storkus, S.C., Basse, P., Redgate, E., Watkins, S., Boggs, S.S. Cancer Res. (1996) [Pubmed]
  2. Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity. Bezouska, K., Yuen, C.T., O'Brien, J., Childs, R.A., Chai, W., Lawson, A.M., Drbal, K., Fiserová, A., Pospísil, M., Feizi, T. Nature (1994) [Pubmed]
  3. Rat spleen dendritic cells express natural killer cell receptor protein 1 (NKR-P1) and have cytotoxic activity to select targets via a Ca2+-dependent mechanism. Josien, R., Heslan, M., Soulillou, J.P., Cuturi, M.C. J. Exp. Med. (1997) [Pubmed]
  4. NKR-P1, a signal transduction molecule on natural killer cells. Giorda, R., Rudert, W.A., Vavassori, C., Chambers, W.H., Hiserodt, J.C., Trucco, M. Science (1990) [Pubmed]
  5. Functional heterogeneity between NKR-P1bright/Lycopersicon esculentum lectin (L.E.)bright and NKR-P1bright/L.E.dim subpopulations of rat natural killer cells. Chambers, W.H., Brumfield, A.M., Hanley-Yanez, K., Lakomy, R., Herberman, R.B., McCaslin, D.C., Olszowy, M.W., McCoy, J.P. J. Immunol. (1992) [Pubmed]
  6. Rat natural killer cell antigen, NKR-P1, related to C-type animal lectins is a carbohydrate-binding protein. Bezouska, K., Vlahas, G., Horváth, O., Jinochová, G., Fiserová, A., Giorda, R., Chambers, W.H., Feizi, T., Pospísil, M. J. Biol. Chem. (1994) [Pubmed]
  7. Changes of liver-resident NK cells during liver regeneration in rats. Vujanovic, N.L., Polimeno, L., Azzarone, A., Francavilla, A., Chambers, W.H., Starzl, T.E., Herberman, R.B., Whiteside, T.L. J. Immunol. (1995) [Pubmed]
  8. Involvement of peptide antigens in the cytotoxicity between 70-kDa heat shock cognate protein-like molecule and CD3+, CD4-, CD8-, TCR-alpha beta- killer T cells. Takashima, S., Sato, N., Kishi, A., Tamura, Y., Hirai, I., Torigoe, T., Yagihashi, A., Takahashi, S., Sagae, S., Kudo, R., Kikuchi, K. J. Immunol. (1996) [Pubmed]
  9. The cytoplasmic domain of rat NKR-P1 receptor interacts with the N-terminal domain of p56(lck) via cysteine residues. Campbell, K.S., Giorda, R. Eur. J. Immunol. (1997) [Pubmed]
  10. CD8+ cells suppress oil-induced arthritis. Jansson, A.M., Lorentzen, J.C., Bucht, A. Clin. Exp. Immunol. (2000) [Pubmed]
  11. Phenotype of rat monocytes during acute kidney allograft rejection: increased expression of NKR-P1 and reduction of CD43. Scriba, A., Grau, V., Steiniger, B. Scand. J. Immunol. (1998) [Pubmed]
  12. NKR-P1, an activating molecule on rat natural killer cells, stimulates phosphoinositide turnover and a rise in intracellular calcium. Ryan, J.C., Niemi, E.C., Goldfien, R.D., Hiserodt, J.C., Seaman, W.E. J. Immunol. (1991) [Pubmed]
  13. CD45-negative mutants of a rat natural killer cell line fail to lyse tumor target cells. Bell, G.M., Dethloff, G.M., Imboden, J.B. J. Immunol. (1993) [Pubmed]
  14. Thy cytoplamic domain of rat NKR-P1 receptor interacts with the N-terminal domain of p56(lck) via cysteine residues. Campbell, K.S., Giorda, R. Eur. J. Immunol. (1997) [Pubmed]
  15. Induction of the nitric oxide-synthesizing pathway in fresh and interleukin 2-cultured rat natural killer cells. Cifone, M.G., Festuccia, C., Cironi, L., Cavallo, G., Chessa, M.A., Pensa, V., Tubaro, E., Santoni, A. Cell. Immunol. (1994) [Pubmed]
  16. Phenotypic profile and functional characterization of rat lymph node-derived gammadelta T cells: implication in the immune response to cytomegalovirus. Dyugovskaya, L., Hirsh, M., Ginsburg, H. Immunology (2003) [Pubmed]
  17. Functional coupling of NKR-P1 receptors to various heterotrimeric G proteins in rat interleukin-2-activated natural killer cells. Al-Aoukaty, A., Rolstad, B., Maghazachi, A.A. J. Biol. Chem. (1997) [Pubmed]
  18. Proliferation and differentiation of alloselective NK cells after alloimmunization-evidence for an adaptive NK response. Petersson, E., Hedlund, G. Cell. Immunol. (1999) [Pubmed]
 
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