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Gene Review

CD274  -  CD274 molecule

Homo sapiens

Synonyms: B7 homolog 1, B7-H, B7-H1, B7H1, PD-L1, ...
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Disease relevance of CD274

  • RESULTS: B7h and B7-H1 messenger RNA was detected in IEC lines and IECs from healthy controls and patients with inflammatory bowel disease (IBD) [1].
  • Human rhinoviruses inhibit the accessory function of dendritic cells by inducing sialoadhesin and B7-H1 expression [2].
  • CONCLUSIONS: The expression of B7-H1 on tumor cells in local areas reciprocally correlated with the number of TILs, and this may contribute to negative regulation in antitumor immune responses in non-small cell lung cancer [3].
  • Expression of Costimulatory Molecules on Human Retinoblastoma Cells Y-79: Functional Expression of CD40 and B7H1 [4].
  • These results suggest that epithelial B7-H1 and B7-DC play a role in virus-associated immune responses in the airways [5].
  • Blockade of B7-H1 signaling could improve hepatitis B c Ag-pulsed monocyte-derived DC-induced IFN-gamma production by autologous hepatitis B virus-specific T cells [6].
  • The PD-1/PD-L pathway can be a good target for restoring antitumor immunity in ovarian cancer [7].
  • PD-L1 may thwart effective antitumor immune responses and represents an attractive target for lymphoma immunotherapy [8].
  • AP-1 signaling and EBV infection represent alternative mechanisms of PD-L1 induction and extend the spectrum of tumors in which to consider PD-1 blockade [9].
  • T-cell-infiltrated melanomas, particularly those with high CD8 T-cell content, are more likely to be associated with PD-L1 expression in tumor cells, an improved prognosis, and increased time to development of brain metastases [10].

High impact information on CD274

  • Loss of tumor suppressor PTEN function increases B7-H1 expression and immunoresistance in glioma [11].
  • Ligation of B7-H1 co-stimulated T-cell responses to polyclonal stimuli and allogeneic antigens, and preferentially stimulated the production of interleukin-10 [12].
  • Interleukin-2, although produced in small amounts, was required for the effect of B7-H1 co-stimulation [12].
  • B7h interacts with inducible costimulator (ICOS) on T cells and provides a positive signal, whereas B7-H1 and B7-DC interact with PD-1 and transmit an inhibitory signal [1].
  • The expression and function of costimulatory molecules B7H and B7-H1 on colonic epithelial cells [1].

Chemical compound and disease context of CD274


Biological context of CD274

  • Most importantly, blocking of B7-H1 and Sn on R-DC with specific mAbs against both receptors reverted the inhibitory phenotype [2].
  • Expression of B7-H1 protein was low in first-trimester placenta compared to second- and third-trimester tissue (P < 0.05) and was enhanced in cultured cytotrophoblasts by treatment with either interferon-gamma or epidermal growth factor (P < 0.05), suggesting that one or both of these mediators regulates B7-H1 expression in the placenta [15].
  • The effect of transduced B7H1-EC was more apparent when the EC were fixed prior to coculture, a manipulation that reduces the strength of costimulation and prevents upregulation of the endogenous B7-H1 molecule [16].
  • Aberrant antigen presentation by antigen-presenting cells (APCs) that exhibit increased B7-H1 expression and IL-10 production in HIV infection could be responsible for T-lymphocyte unresponsiveness and loss of protective immunity [17].
  • Western blot analysis showed that B7-H1 expression was induced by various H. pylori strains and was independent of H. pylori virulence factors such as Cag, VacA, and Urease [18].

Anatomical context of CD274


Associations of CD274 with chemical compounds


Physical interactions of CD274

  • Furthermore, the soluble PD-1 with high purity possessed specific binding activity with its cognate ligand PD-L1, and the dissociation constant was 0.43 nmol/L as determined by Scatchard plot analysis [23].

Regulatory relationships of CD274

  • The costimulatory effect of B7H1-expressing IFN-gamma-treated Y-79 cells on proliferation of purified T cells was studied in Y-79/T-cell coculture experiments with a blocking anti-B7H1 monoclonal antibody (mAb) [4].
  • In contrast, expression of inhibitory B7-H1 molecules was up-regulated and R-DC de novo expressed sialoadhesin (Sn) [2].
  • ICOS-B7H interaction induces the production of IL-10 which inhibits the antitumor immune responses [24].
  • Importantly, B7-H1 expressed on APC strongly inhibits autologous CD4 T-cell activation [25].
  • Accordingly, protein expression of B7-H1 on monocytes was up-regulated after 24 h of IFN-beta application [25].

Other interactions of CD274

  • In contrast, the expression of B7H1 on IFN-gamma-treated Y-79 cells contributes to the suppression of T cells [4].
  • Functional relevance of B7-H1 for tumor-immune interactions was assessed by coculture experiments using purified, alloreactive CD4 and CD8 T cells in the presence of a neutralizing anti-B7-H1 antibody [19].
  • Furthermore, in the presence of neutralizing B7-H1 antibody (mAb 5H1) occurred no significant changes in T cell IFN-gamma or IL-2 production or proliferation [19].
  • Expression of B7-H1 and B7-DC on the airway epithelium is enhanced by double-stranded RNA [5].
  • B7-H1 reduced secretion of IL-2 and IL-10 by memory T cells [16].
  • Blocking the MEK/ERK pathway inhibited IFN-gamma-mediated and TLR-mediated expression of B7-H1 [26].

Analytical, diagnostic and therapeutic context of CD274


  1. The expression and function of costimulatory molecules B7H and B7-H1 on colonic epithelial cells. Nakazawa, A., Dotan, I., Brimnes, J., Allez, M., Shao, L., Tsushima, F., Azuma, M., Mayer, L. Gastroenterology (2004) [Pubmed]
  2. Human rhinoviruses inhibit the accessory function of dendritic cells by inducing sialoadhesin and B7-H1 expression. Kirchberger, S., Majdic, O., Steinberger, P., Blüml, S., Pfistershammer, K., Zlabinger, G., Deszcz, L., Kuechler, E., Knapp, W., Stöckl, J. J. Immunol. (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. Expression of Costimulatory Molecules on Human Retinoblastoma Cells Y-79: Functional Expression of CD40 and B7H1. Usui, Y., Okunuki, Y., Hattori, T., Takeuchi, M., Kezuka, T., Goto, H., Usui, M. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  5. 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]
  6. B7-H1 up-regulation on myeloid dendritic cells significantly suppresses T cell immune function in patients with chronic hepatitis B. Chen, L., Zhang, Z., Chen, W., Zhang, Z., Li, Y., Shi, M., Zhang, J., Chen, L., Wang, S., Wang, F.S. J. Immunol. (2007) [Pubmed]
  7. Programmed cell death 1 ligand 1 and tumor-infiltrating CD8+ T lymphocytes are prognostic factors of human ovarian cancer. Hamanishi, J., Mandai, M., Iwasaki, M., Okazaki, T., Tanaka, Y., Yamaguchi, K., Higuchi, T., Yagi, H., Takakura, K., Minato, N., Honjo, T., Fujii, S. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  8. Programmed death ligand 1 is expressed by non-hodgkin lymphomas and inhibits the activity of tumor-associated T cells. Andorsky, D.J., Yamada, R.E., Said, J., Pinkus, G.S., Betting, D.J., Timmerman, J.M. Clin. Cancer Res. (2011) [Pubmed]
  9. Constitutive AP-1 Activity and EBV Infection Induce PD-L1 in Hodgkin Lymphomas and Posttransplant Lymphoproliferative Disorders: Implications for Targeted Therapy. Green, M.R., Rodig, S., Juszczynski, P., Ouyang, J., Sinha, P., O'Donnell, E., Neuberg, D., Shipp, M.A. Clin. Cancer Res. (2012) [Pubmed]
  10. Characterization of PD-L1 Expression and Associated T-cell Infiltrates in Metastatic Melanoma Samples from Variable Anatomic Sites. Kluger, H.M., Zito, C.R., Barr, M.L., Baine, M.K., Chiang, V.L., Sznol, M., Rimm, D.L., Chen, L., Jilaveanu, L.B. Clin. Cancer Res. (2015) [Pubmed]
  11. Loss of tumor suppressor PTEN function increases B7-H1 expression and immunoresistance in glioma. Parsa, A.T., Waldron, J.S., Panner, A., Crane, C.A., Parney, I.F., Barry, J.J., Cachola, K.E., Murray, J.C., Tihan, T., Jensen, M.C., Mischel, P.S., Stokoe, D., Pieper, R.O. Nat. Med. (2007) [Pubmed]
  12. B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation and interleukin-10 secretion. Dong, H., Zhu, G., Tamada, K., Chen, L. Nat. Med. (1999) [Pubmed]
  13. A comparative study of the potentiating effect of caffeine and poly-D-lysine on chromosome damage induced by X-rays in plant cells. Mateos, S., Panneerselvam, N., Mateos, J.C., Cortés, F. Mutat. Res. (1992) [Pubmed]
  14. B7-H1 glycoprotein blockade: a novel strategy to enhance immunotherapy in patients with renal cell carcinoma. Thompson, R.H., Webster, W.S., Cheville, J.C., Lohse, C.M., Dong, H., Leibovich, B.C., Kuntz, S.M., Sengupta, S., Kwon, E.D., Blute, M.L. Urology (2005) [Pubmed]
  15. B7 family molecules are favorably positioned at the human maternal-fetal interface. Petroff, M.G., Chen, L., Phillips, T.A., Azzola, D., Sedlmayr, P., Hunt, J.S. Biol. Reprod. (2003) [Pubmed]
  16. Immune accessory functions of human endothelial cells are modulated by overexpression of B7-H1 (PDL1). LaGier, A.J., Pober, J.S. Hum. Immunol. (2006) [Pubmed]
  17. B7-H1 is up-regulated in HIV infection and is a novel surrogate marker of disease progression. Trabattoni, D., Saresella, M., Biasin, M., Boasso, A., Piacentini, L., Ferrante, P., Dong, H., Maserati, R., Shearer, G.M., Chen, L., Clerici, M. Blood (2003) [Pubmed]
  18. Expression of B7-H1 on gastric epithelial cells: its potential role in regulating T cells during Helicobacter pylori infection. Das, S., Suarez, G., Beswick, E.J., Sierra, J.C., Graham, D.Y., Reyes, V.E. J. Immunol. (2006) [Pubmed]
  19. The role of leukemia-derived B7-H1 (PD-L1) in tumor-T-cell interactions in humans. Salih, H.R., Wintterle, S., Krusch, M., Kroner, A., Huang, Y.H., Chen, L., Wiendl, H. Exp. Hematol. (2006) [Pubmed]
  20. Costimulatory B7-H1 in renal cell carcinoma patients: Indicator of tumor aggressiveness and potential therapeutic target. Thompson, R.H., Gillett, M.D., Cheville, J.C., Lohse, C.M., Dong, H., Webster, W.S., Krejci, K.G., Lobo, J.R., Sengupta, S., Chen, L., Zincke, H., Blute, M.L., Strome, S.E., Leibovich, B.C., Kwon, E.D. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  21. High-level expression of B7-H1 molecules by dendritic cells suppresses the function of activated T cells and desensitizes allergen-primed animals. Kim, H.K., Guan, H., Zu, G., Li, H., Wu, L., Feng, X., Elmets, C., Fu, Y., Xu, H. J. Leukoc. Biol. (2006) [Pubmed]
  22. 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]
  23. Expression and purification of soluble human programmed death-1 in Escherichia coli. Xu, L., Liu, Y., He, X. Cell. Mol. Immunol. (2006) [Pubmed]
  24. In situ expression and significance of B7 costimulatory molecules within tissues of human gastric carcinoma. Chen, X.L., Cao, X.D., Kang, A.J., Wang, K.M., Su, B.S., Wang, Y.L. World J. Gastroenterol. (2003) [Pubmed]
  25. Interferon-beta enhances monocyte and dendritic cell expression of B7-H1 (PD-L1), a strong inhibitor of autologous T-cell activation: relevance for the immune modulatory effect in multiple sclerosis. Schreiner, B., Mitsdoerffer, M., Kieseier, B.C., Chen, L., Hartung, H.P., Weller, M., Wiendl, H. J. Neuroimmunol. (2004) [Pubmed]
  26. Plasma cells from multiple myeloma patients express B7-H1 (PD-L1) and increase expression after stimulation with IFN-{gamma} and TLR ligands via a MyD88-, TRAF6-, and MEK-dependent pathway. Liu, J., Hamrouni, A., Wolowiec, D., Coiteux, V., Kuliczkowski, K., Hetuin, D., Saudemont, A., Quesnel, B. Blood (2007) [Pubmed]
  27. 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]
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