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Gene Review

Ppia  -  peptidylprolyl isomerase A

Mus musculus

Synonyms: 2700098C05, Cphn, CyP-18, Cyclophilin A, Cyclosporin A-binding protein, ...
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Disease relevance of Ppia

  • Here we present evidence supporting a role for viral-associated CyPA in the early events of HIV-1 infection [1].
  • More recently, host-derived cyclophilin A (CyPA) has been shown to be incorporated into HIV-1 virions and its incorporation essential for viral infectivity [1].
  • Collectively, our data reveal that a novel function of CypA is required in the processing of RA-induced neuronal differentiation in p19 embryonal carcinoma cells [2].
  • Elucidation of the precise role of CypA in these pathways may lead to new targeted therapies for lung cancer [3].
  • We recently identified CD147 as the main signaling receptor for cyclophilin A. In the current study we examined the contribution of cyclophilin-CD147 interactions to inflammatory responses in vivo using a mouse model of acute lung injury [4].

High impact information on Ppia


Biological context of Ppia


Anatomical context of Ppia


Associations of Ppia with chemical compounds

  • Immunosuppressive doses of cyclosporine failed to block the responses of Ppia(-/-) mice to allogeneic challenge [13].
  • Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known [12].
  • Stable transfectants with expression of small interfering RNA for targeting cyclophilin A (CypA) in p19 cells lose their potential for retinoic acid (RA)-induced neuronal differentiation but not Me(2)SO-induced mesodermal differentiation [2].
  • The founding member of the family, cyclophilin A (CyPA), is an abundant, ubiquitously expressed protein of unknown function that binds with nanomolar affinity to CsA [7].
  • Nuclear CypA binds to DNA in a zinc ion-dependent manner, in contrast to recombinant CypB [9].

Physical interactions of Ppia

  • However, the conformation of CsA when bound to CyPC is significantly different from that when bound to CyPA [11].

Regulatory relationships of Ppia

  • CypA accumulated within the nuclei of damaged neurons after HI, and this nuclear translocation of CypA was suppressed in AIF-deficient harlequin mice [14].

Other interactions of Ppia


Analytical, diagnostic and therapeutic context of Ppia


  1. Role of cyclophilin A in the uptake of HIV-1 by macrophages and T lymphocytes. Sherry, B., Zybarth, G., Alfano, M., Dubrovsky, L., Mitchell, R., Rich, D., Ulrich, P., Bucala, R., Cerami, A., Bukrinsky, M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Cyclophilin A is required for retinoic acid-induced neuronal differentiation in p19 cells. Song, J., Lu, Y.C., Yokoyama, K., Rossi, J., Chiu, R. J. Biol. Chem. (2004) [Pubmed]
  3. Stable RNA interference-mediated suppression of cyclophilin A diminishes non-small-cell lung tumor growth in vivo. Howard, B.A., Furumai, R., Campa, M.J., Rabbani, Z.N., Vujaskovic, Z., Wang, X.F., Patz, E.F. Cancer Res. (2005) [Pubmed]
  4. Extracellular cyclophilins contribute to the regulation of inflammatory responses. Arora, K., Gwinn, W.M., Bower, M.A., Watson, A., Okwumabua, I., MacDonald, H.R., Bukrinsky, M.I., Constant, S.L. J. Immunol. (2005) [Pubmed]
  5. Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk. Colgan, J., Asmal, M., Neagu, M., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A., Luban, J. Immunity (2004) [Pubmed]
  6. Laser capture microdissection analysis of gene expression in macrophages from atherosclerotic lesions of apolipoprotein E-deficient mice. Trogan, E., Choudhury, R.P., Dansky, H.M., Rong, J.X., Breslow, J.L., Fisher, E.A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Isolation, characterization and targeted disruption of mouse ppia: cyclophilin A is not essential for mammalian cell viability. Colgan, J., Asmal, M., Luban, J. Genomics (2000) [Pubmed]
  8. One novel quinoxaline derivative as a potent human cyclophilin A inhibitor shows highly inhibitory activity against mouse spleen cell proliferation. Li, J., Chen, J., Zhang, L., Wang, F., Gui, C., Zhang, L., Qin, Y., Xu, Q., Liu, H., Nan, F., Shen, J., Bai, D., Chen, K., Shen, X., Jiang, H. Bioorg. Med. Chem. (2006) [Pubmed]
  9. Cyclophilin-A is a zinc-dependent DNA binding protein in macrophages. Krummrei, U., Bang, R., Schmidtchen, R., Brune, K., Bang, H. FEBS Lett. (1995) [Pubmed]
  10. Identification and characterization of Schistosoma mansoni p17.7, a cyclophilin. Kiang, D., El Ghazalie, N.E., Medhat, A.M., Abdel-Fattah, M., Karim, A.M., LoVerde, P.T. Mol. Biochem. Parasitol. (1996) [Pubmed]
  11. Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A. Ke, H., Zhao, Y., Luo, F., Weissman, I., Friedman, J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  12. Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex. Galigniana, M.D., Morishima, Y., Gallay, P.A., Pratt, W.B. J. Biol. Chem. (2004) [Pubmed]
  13. Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine. Colgan, J., Asmal, M., Yu, B., Luban, J. J. Immunol. (2005) [Pubmed]
  14. Cyclophilin A participates in the nuclear translocation of apoptosis-inducing factor in neurons after cerebral hypoxia-ischemia. Zhu, C., Wang, X., Deinum, J., Huang, Z., Gao, J., Modjtahedi, N., Neagu, M.R., Nilsson, M., Eriksson, P.S., Hagberg, H., Luban, J., Kroemer, G., Blomgren, K. J. Exp. Med. (2007) [Pubmed]
  15. Gravitational loading of a simulated launch alters mRNA expression in osteoblasts. Fitzgerald, J., Hughes-Fulford, M. Exp. Cell Res. (1996) [Pubmed]
  16. Calcineurin enhances acetylcholinesterase mRNA stability during C2-C12 muscle cell differentiation. Luo, Z.D., Wang, Y., Werlen, G., Camp, S., Chien, K.R., Taylor, P. Mol. Pharmacol. (1999) [Pubmed]
  17. Localization of cyclophilin A and cyclophilin C mRNA in murine kidney using RT-PCR. Otsuka, M., Terada, Y., Yang, T., Nonoguchi, H., Tomita, K., Marumo, F. Kidney Int. (1994) [Pubmed]
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