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Gene Review

PDCD1LG2  -  programmed cell death 1 ligand 2

Homo sapiens

Synonyms: B7-DC, B7DC, Btdc, Butyrophilin B7-DC, CD273, ...


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Disease relevance of PDCD1LG2

  • Second, we assessed the therapeutic potential of neutralizing anti-B7-H1 and/or B7-DC mAbs using this colitis model [1].
  • These results suggest that epithelial B7-H1 and B7-DC play a role in virus-associated immune responses in the airways [2].
  • In the present study, we investigated the expression of B7-H1 and B7-DC in tumor specimens of non-small cell lung cancer and their relationships with clinicopathological variables and postoperative survival [3].
  • In this study, we investigated the expression of PD-L1 and PD-L2 in human esophageal cancer to define their clinical significance in patients' prognosis after surgery [4].
  • Expression of programmed death-1 ligand (PD-L) 1, PD-L2, B7-H3, and inducible costimulator ligand on human respiratory tract epithelial cells and regulation by respiratory syncytial virus and type 1 and 2 cytokines [5].

High impact information on PDCD1LG2

  • In addition, the PD-1:PD-L1/PD-L2 pathway plays a critical role in regulating T cell activation and tolerance [6].
  • PD-1 has two ligands: PD-1 ligand 1 (PD-L1), which is expressed broadly on hematopoietic and parenchymal cells, including pancreatic islet cells; and PD-L2, which is restricted to macrophages and dendritic cells [7].
  • The genomic loci for PDL2 and several neighboring genes were amplified in over half of the PMBLs and in Hodgkin lymphoma cell lines [8].
  • B7-DC, a new dendritic cell molecule with potent costimulatory properties for T cells [9].
  • These properties of B7-DC may account for some of the unique activity of DCs, such as their ability to initiate potent T helper cell type 1 responses [9].

Biological context of PDCD1LG2


Anatomical context of PDCD1LG2


Associations of PDCD1LG2 with chemical compounds

  • B7-H1 and B7-DC were constitutively expressed on the cells, and their expression was profoundly upregulated by stimulation with an analog of viral dsRNA, polyinosinic-polycytidylic acid [2].
  • Fluticasone treatment (10(-7) M) reduced the baseline expression and inhibited the induction of B7-H1 and B7-DC in BEAS2B cells [14].
  • Comparison of their N-terminal sequences, up to residue 45, showed that PD-L1 is identical to PD-L2 [designated the isoleucine (Ile) form from the N-terminal residue] and PD-L3 is identical to PD-L4 [designated the valine (Val) form from the N-terminal residue] and that there are 35 identical residues between the two forms [15].

Regulatory relationships of PDCD1LG2


Other interactions of PDCD1LG2

  • Blocking PD-1 reverted the inhibitory effect of PD-L2, demonstrating involvement of this pathway [16].
  • PD-L2 inhibition affected CD4(+) and CD8(+) T cells and was not abrogated by costimulation via CD28 [16].
  • Unstimulated cultured KCs expressed both B7-H1 and B7-DC, and their expression was upregulated by proinflammatory cytokines, particularly IFN-gamma [17].
  • Anti-CD3 mAb + PD-L2 stimulation also increased the level of SHP-2 associated with the PD-1 receptor [18].
  • B7-DC was a strong inhibitor of CD4+T-cell activation, as assessed by increased cytokine (interferon-gamma and interleukin-2) production and enhanced levels of T-cell activation marker CD69 in the presence of its blocking antibody [19].

Analytical, diagnostic and therapeutic context of PDCD1LG2

  • CONCLUSIONS: These data suggest that PD-L1 and PD-L2 status may be a new predictor of prognosis for patients with esophageal cancer and provide the rationale for developing novel immunotherapy of targeting PD-1/PD-L pathway [4].
  • Blockade of PD-1 or B7-H1, but not B7-DC, led to accelerated corneal allograft rejection [20].
  • Adoptive transfer from mice pretreated with intratracheal delivery of alloantigen plus control IgG or anti-PD-L2 mAb prolonged survival of C57BL/10 grafts in secondary CBA recipients (MST, 72 and 56 days, respectively) [21].
  • With the exception of PD-L4, the purified RIPs gave a positive reaction when stained for sugars on SDS-PAGE gels and, when analyzed by electrospray mass spectrometry, had M(r) values of 32,715 +/- 1 (PD-L1), 31,542 +/- 1 (PD-L2), 30,356 +/- 1 (PD-L3) and 29,185 +/- 1 Da (PD-L4) [15].


  1. Blockade of B7-H1 suppresses the development of chronic intestinal inflammation. Kanai, T., Totsuka, T., Uraushihara, K., Makita, S., Nakamura, T., Koganei, K., Fukushima, T., Akiba, H., Yagita, H., Okumura, K., Machida, U., Iwai, H., Azuma, M., Chen, L., Watanabe, M. J. Immunol. (2003) [Pubmed]
  2. Expression of B7-H1 and B7-DC on the airway epithelium is enhanced by double-stranded RNA. Tsuda, M., Matsumoto, K., Inoue, H., Matsumura, M., Nakano, T., Mori, A., Azuma, M., Nakanishi, Y. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  3. B7-H1 expression on non-small cell lung cancer cells and its relationship with tumor-infiltrating lymphocytes and their PD-1 expression. Konishi, J., Yamazaki, K., Azuma, M., Kinoshita, I., Dosaka-Akita, H., Nishimura, M. Clin. Cancer Res. (2004) [Pubmed]
  4. Clinical significance of programmed death-1 ligand-1 and programmed death-1 ligand-2 expression in human esophageal cancer. Ohigashi, Y., Sho, M., Yamada, Y., Tsurui, Y., Hamada, K., Ikeda, N., Mizuno, T., Yoriki, R., Kashizuka, H., Yane, K., Tsushima, F., Otsuki, N., Yagita, H., Azuma, M., Nakajima, Y. Clin. Cancer Res. (2005) [Pubmed]
  5. Expression of programmed death-1 ligand (PD-L) 1, PD-L2, B7-H3, and inducible costimulator ligand on human respiratory tract epithelial cells and regulation by respiratory syncytial virus and type 1 and 2 cytokines. Stanciu, L.A., Bellettato, C.M., Laza-Stanca, V., Coyle, A.J., Papi, A., Johnston, S.L. J. Infect. Dis. (2006) [Pubmed]
  6. The B7 family revisited. Greenwald, R.J., Freeman, G.J., Sharpe, A.H. Annu. Rev. Immunol. (2005) [Pubmed]
  7. Tissue expression of PD-L1 mediates peripheral T cell tolerance. Keir, M.E., Liang, S.C., Guleria, I., Latchman, Y.E., Qipo, A., Albacker, L.A., Koulmanda, M., Freeman, G.J., Sayegh, M.H., Sharpe, A.H. J. Exp. Med. (2006) [Pubmed]
  8. Molecular diagnosis of primary mediastinal B cell lymphoma identifies a clinically favorable subgroup of diffuse large B cell lymphoma related to Hodgkin lymphoma. Rosenwald, A., Wright, G., Leroy, K., Yu, X., Gaulard, P., Gascoyne, R.D., Chan, W.C., Zhao, T., Haioun, C., Greiner, T.C., Weisenburger, D.D., Lynch, J.C., Vose, J., Armitage, J.O., Smeland, E.B., Kvaloy, S., Holte, H., Delabie, J., Campo, E., Montserrat, E., Lopez-Guillermo, A., Ott, G., Muller-Hermelink, H.K., Connors, J.M., Braziel, R., Grogan, T.M., Fisher, R.I., Miller, T.P., LeBlanc, M., Chiorazzi, M., Zhao, H., Yang, L., Powell, J., Wilson, W.H., Jaffe, E.S., Simon, R., Klausner, R.D., Staudt, L.M. J. Exp. Med. (2003) [Pubmed]
  9. B7-DC, a new dendritic cell molecule with potent costimulatory properties for T cells. Tseng, S.Y., Otsuji, M., Gorski, K., Huang, X., Slansky, J.E., Pai, S.I., Shalabi, A., Shin, T., Pardoll, D.M., Tsuchiya, H. J. Exp. Med. (2001) [Pubmed]
  10. Cloning and identification of two novel splice variants of human PD-L2. He, X.H., Liu, Y., Xu, L.H., Zeng, Y.Y. Acta Biochim. Biophys. Sin. (Shanghai) (2004) [Pubmed]
  11. Contribution of the PD-1 ligands/PD-1 signaling pathway to dendritic cell-mediated CD4(+) T cell activation. Kuipers, H., Muskens, F., Willart, M., Hijdra, D., van Assema, F.B., Coyle, A.J., Hoogsteden, H.C., Lambrecht, B.N. Eur. J. Immunol. (2006) [Pubmed]
  12. PD-L2 is a second ligand for PD-1 and inhibits T cell activation. Latchman, Y., Wood, C.R., Chernova, T., Chaudhary, D., Borde, M., Chernova, I., Iwai, Y., Long, A.J., Brown, J.A., Nunes, R., Greenfield, E.A., Bourque, K., Boussiotis, V.A., Carter, L.L., Carreno, B.M., Malenkovich, N., Nishimura, H., Okazaki, T., Honjo, T., Sharpe, A.H., Freeman, G.J. Nat. Immunol. (2001) [Pubmed]
  13. Blockade of programmed death-1 ligands on dendritic cells enhances T cell activation and cytokine production. Brown, J.A., Dorfman, D.M., Ma, F.R., Sullivan, E.L., Munoz, O., Wood, C.R., Greenfield, E.A., Freeman, G.J. J. Immunol. (2003) [Pubmed]
  14. Constitutive and inducible expression of b7 family of ligands by human airway epithelial cells. Kim, J., Myers, A.C., Chen, L., Pardoll, D.M., Truong-Tran, Q.A., Lane, A.P., McDyer, J.F., Fortuno, L., Schleimer, R.P. Am. J. Respir. Cell Mol. Biol. (2005) [Pubmed]
  15. Isolation and characterization of four type-1 ribosome-inactivating proteins, with polynucleotide:adenosine glycosidase activity, from leaves of Phytolacca dioica L. Di Maro, A., Valbonesi, P., Bolognesi, A., Stirpe, F., De Luca, P., Siniscalco Gigliano, G., Gaudio, L., Delli Bovi, P., Ferranti, P., Malorni, A., Parente, A. Planta (1999) [Pubmed]
  16. No evidence for dualism in function and receptors: PD-L2/B7-DC is an inhibitory regulator of human T cell activation. Pfistershammer, K., Klauser, C., Pickl, W.F., Stöckl, J., Leitner, J., Zlabinger, G., Majdic, O., Steinberger, P. Eur. J. Immunol. (2006) [Pubmed]
  17. The expression of B7-H1 on keratinocytes in chronic inflammatory mucocutaneous disease and its regulatory role. Youngnak-Piboonratanakit, P., Tsushima, F., Otsuki, N., Igarashi, H., Machida, U., Iwai, H., Takahashi, Y., Omura, K., Yokozeki, H., Azuma, M. Immunol. Lett. (2004) [Pubmed]
  18. PD-L2:PD-1 involvement in T cell proliferation, cytokine production, and integrin-mediated adhesion. Saunders, P.A., Hendrycks, V.R., Lidinsky, W.A., Woods, M.L. Eur. J. Immunol. (2005) [Pubmed]
  19. Renal tubular epithelial expression of the coinhibitory molecule B7-DC (programmed death-1 ligand). Zhang, J., Chen, Y., Li, J., Zhang, R., Wu, Y., Zou, L., Zhao, T., Zhang, X., Han, J., Chen, A., Wu, Y. J. Nephrol. (2006) [Pubmed]
  20. B7-h1-induced apoptosis as a mechanism of immune privilege of corneal allografts. Hori, J., Wang, M., Miyashita, M., Tanemoto, K., Takahashi, H., Takemori, T., Okumura, K., Yagita, H., Azuma, M. J. Immunol. (2006) [Pubmed]
  21. Programmed death-1-programmed death-L1 interaction is essential for induction of regulatory cells by intratracheal delivery of alloantigen. Aramaki, O., Shirasugi, N., Takayama, T., Shimazu, M., Kitajima, M., Ikeda, Y., Azuma, M., Okumura, K., Yagita, H., Niimi, M. Transplantation (2004) [Pubmed]
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