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CLEC2D  -  C-type lectin domain family 2, member D

Homo sapiens

Synonyms: C-type lectin domain family 2 member D, CLAX, LLT-1, LLT1, Lectin-like NK cell receptor, ...
 
 
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Disease relevance of CLEC2D

  • The extracellular domain of hOCIL was expressed as a soluble recombinant protein in E. coli, and its biological effects were determined [1].
 

High impact information on CLEC2D

 

Biological context of CLEC2D

  • MATERIALS AND METHODS: We isolated the human homolog of OCIL (hOCIL) from a human fetal cDNA library that predicts a 191 amino acid type II membrane protein, with the 112 amino acid C-type lectin region in the extracellular domain having 53% identity with the C-type lectin sequences of rOCIL and mOCIL [1].
 

Associations of CLEC2D with chemical compounds

 

Physical interactions of CLEC2D

 

Regulatory relationships of CLEC2D

  • Moreover, LLT1 on target cells can inhibit NK cytotoxicity via interactions with NKR-P1A [5].
  • Binding of mAb L9.7 to surface LLT1 induced IFN-gamma production, but did not modulate cytotoxicity by YT cells, a human NK cell line [6].
  • Interactions between NKR-P1A on NK cells and LLT1 on target cells inhibit NK cell-mediated cytotoxicity and cytokine production and can inhibit TNF-alpha production by TCR-activated NKR-P1A(+) CD8(+) T cells [7].

References

  1. Isolation of a human homolog of osteoclast inhibitory lectin that inhibits the formation and function of osteoclasts. Hu, Y.S., Zhou, H., Myers, D., Quinn, J.M., Atkins, G.J., Ly, C., Gange, C., Kartsogiannis, V., Elliott, J., Kostakis, P., Zannettino, A.C., Cromer, B., McKinstry, W.J., Findlay, D.M., Gillespie, M.T., Ng, K.W. J. Bone Miner. Res. (2004) [Pubmed]
  2. Cutting edge: lectin-like transcript 1 is a ligand for the CD161 receptor. Aldemir, H., Prod'homme, V., Dumaurier, M.J., Retiere, C., Poupon, G., Cazareth, J., Bihl, F., Braud, V.M. J. Immunol. (2005) [Pubmed]
  3. Characterization of the chicken C-type lectin-like receptors B-NK and B-lec suggests that the NK complex and the MHC share a common ancestral region. Rogers, S.L., Göbel, T.W., Viertlboeck, B.C., Milne, S., Beck, S., Kaufman, J. J. Immunol. (2005) [Pubmed]
  4. A novel osteoblast-derived C-type lectin that inhibits osteoclast formation. Zhou, H., Kartsogiannis, V., Hu, Y.S., Elliott, J., Quinn, J.M., McKinstry, W.J., Gillespie, M.T., Ng, K.W. J. Biol. Chem. (2001) [Pubmed]
  5. Cutting edge: lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A receptor. Rosen, D.B., Bettadapura, J., Alsharifi, M., Mathew, P.A., Warren, H.S., Lanier, L.L. J. Immunol. (2005) [Pubmed]
  6. The LLT1 receptor induces IFN-gamma production by human natural killer cells. Mathew, P.A., Chuang, S.S., Vaidya, S.V., Kumaresan, P.R., Boles, K.S., Pham, H.T. Mol. Immunol. (2004) [Pubmed]
  7. Functional consequences of interactions between human NKR-P1A and its ligand LLT1 expressed on activated dendritic cells and B cells. Rosen, D.B., Cao, W., Avery, D.T., Tangye, S.G., Liu, Y.J., Houchins, J.P., Lanier, L.L. J. Immunol. (2008) [Pubmed]
 
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