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Gene Review

TFCP2  -  transcription factor CP2

Homo sapiens

Synonyms: Alpha-globin transcription factor CP2, CP2, LBP-1C, LBP1C, LSF, ...
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Disease relevance of TFCP2

  • We report that both YY1 and LSF participate in the formation of a complex that recognizes the initiation region of the HIV-1 LTR [1].
  • YY1 and LSF may establish transcriptional and virological latency of HIV, a state that has recently been recognized in vivo and has significant implications for the long-term treatment of AIDS [2].
  • RESULTS: After exposure to any of 4 different polyamides that specifically block HDAC-1 recruitment by LSF to the HIV promoter, replication-competent HIV was recovered from cultures of resting CD4+ T cells in 6 of 8 HIV-infected patients whose viremia had been suppressed by therapy [3].
  • The transcription factor LSF, identified as a HeLa protein that binds the simian virus 40 late promoter, recognizes direct repeats with a center-to-center spacing of 10 bp [4].
  • In addition to its role in regulating SAA3 gene expression, we provide evidence that SEF could also bind in a sequence-specific manner to the promoters of the alpha(2)-macroglobulin and Aalpha-fibrinogen genes and to an intronic enhancer of the human Wilm's tumor 1 gene, suggesting a functional role in the regulation of these genes [5].

Psychiatry related information on TFCP2

  • The transcriptional factor LBP-1c/CP2/LSF gene on chromosome 12 is a genetic determinant of Alzheimer's disease [6].
  • We studied whether pretreatment levels of learned helplessness (LH) were related to outcomes for substance-dependent individuals receiving high-structure, behaviorally oriented (HSB) or low-structure, facilitative (LSF) treatment [7].

High impact information on TFCP2

  • Surprisingly, CP1, CP2, and NF-I each appear to recognize their binding site with highest affinity as a multisubunit complex composed of heterologous subunits [8].
  • Mitogenic stimulation of resting T cells causes rapid phosphorylation of the transcription factor LSF and increased DNA-binding activity [9].
  • This modulation of LSF-DNA-binding activity as T cells progress from a resting to a replicating state reveals that LSF activity is regulated during cell growth and suggests that LSF regulates growth-responsive promoters [9].
  • This serum-induced CCAAT factor also bound CCAAT sequences from other promoters, for example, those of human heat shock protein 70, human c-Ha-ras, and human histone 1, but not to the adenovirus origin of replication or the SV40 enhancer core sequence, suggesting that it was related to CP1 or CP2 [10].
  • LSF activates transcription from the SV40 late promoter in vitro from initiation site L325, via its binding to the template DNA [11].

Chemical compound and disease context of TFCP2

  • The only significant difference in toxicities occurring through the eighth dose of IL-2 was in the maximum elevation of serum creatinine (mean, 1.7 +/- 0.8 for placebo versus 1.5 +/- 0.6 mg/dl for LSF, P = 0.013) [12].
  • RESULTS: Loss of consciousness was accurately monitored by BIS, SEMG and SEF 95%, and propofol drug effect by BIS only [13].

Biological context of TFCP2


Anatomical context of TFCP2


Associations of TFCP2 with chemical compounds

  • Glutathione S-transferase pull-down and coimmunoprecipitation assays showed that two HXPR motif-containing proteins REST and YY1 indeed were able to bind CP2 [19].
  • Four guanine residues within the LSF-GC site, when methylated, strongly interfere with LSF binding [11].
  • LSF binds specifically to the 21-base-pair repeats of the SV40 promoters, forming specific protein-DNA complexes, which migrate more rapidly through nondenaturing polyacrylamide gels than that formed by the previously identified transcription factor Sp1 [21].
  • Double labeling experiments with CP1 and CP2, respectively, and a murine anti-chymase mAb demonstrated the presence of HMC-CP in the tryptase-positive, chymase-positive mast cell type (MCTC) only [22].
  • CT1501R (lisofylline; LSF) is one of several methyl xanthine congeners that inhibit the effects of TNF by the interruption of specific signal transduction pathways [12].

Physical interactions of TFCP2

  • Using an epitope-counting method, we show that LSF binds DNA as a homodimer [4].

Regulatory relationships of TFCP2


Other interactions of TFCP2


Analytical, diagnostic and therapeutic context of TFCP2


  1. Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF. Romerio, F., Gabriel, M.N., Margolis, D.M. J. Virol. (1997) [Pubmed]
  2. The human factors YY1 and LSF repress the human immunodeficiency virus type 1 long terminal repeat via recruitment of histone deacetylase 1. Coull, J.J., Romerio, F., Sun, J.M., Volker, J.L., Galvin, K.M., Davie, J.R., Shi, Y., Hansen, U., Margolis, D.M. J. Virol. (2000) [Pubmed]
  3. Polyamides reveal a role for repression in latency within resting T cells of HIV-infected donors. Ylisastigui, L., Coull, J.J., Rucker, V.C., Melander, C., Bosch, R.J., Brodie, S.J., Corey, L., Sodora, D.L., Dervan, P.B., Margolis, D.M. J. Infect. Dis. (2004) [Pubmed]
  4. One exon of the human LSF gene includes conserved regions involved in novel DNA-binding and dimerization motifs. Shirra, M.K., Zhu, Q., Huang, H.C., Pallas, D., Hansen, U. Mol. Cell. Biol. (1994) [Pubmed]
  5. Purification and characterization of the serum amyloid A3 enhancer factor. Bing, Z., Reddy, S.A., Ren, Y., Qin, J., Liao, W.S. J. Biol. Chem. (1999) [Pubmed]
  6. The transcriptional factor LBP-1c/CP2/LSF gene on chromosome 12 is a genetic determinant of Alzheimer's disease. Lambert, J.C., Goumidi, L., Vrièze, F.W., Frigard, B., Harris, J.M., Cummings, A., Coates, J., Pasquier, F., Cottel, D., Gaillac, M., St Clair, D., Mann, D.M., Hardy, J., Lendon, C.L., Amouyel, P., Chartier-Harlin, M.C. Hum. Mol. Genet. (2000) [Pubmed]
  7. High- and low-structure treatments for substance dependence: role of learned helplessness. Thornton, C.C., Patkar, A.A., Murray, H.W., Mannelli, P., Gottheil, E., Vergare, M.J., Weinstein, S.P. The American journal of drug and alcohol abuse. (2003) [Pubmed]
  8. Human CCAAT-binding proteins have heterologous subunits. Chodosh, L.A., Baldwin, A.S., Carthew, R.W., Sharp, P.A. Cell (1988) [Pubmed]
  9. Mitogenic stimulation of resting T cells causes rapid phosphorylation of the transcription factor LSF and increased DNA-binding activity. Volker, J.L., Rameh, L.E., Zhu, Q., DeCaprio, J., Hansen, U. Genes Dev. (1997) [Pubmed]
  10. Serum and v-src increase the level of a CCAAT-binding factor required for transcription from a retroviral long terminal repeat. Dutta, A., Stoeckle, M.Y., Hanafusa, H. Genes Dev. (1990) [Pubmed]
  11. Transcription factor LSF binds two variant bipartite sites within the SV40 late promoter. Huang, H.C., Sundseth, R., Hansen, U. Genes Dev. (1990) [Pubmed]
  12. Prospective randomized trial of lisofylline for the prevention of toxicities of high-dose interleukin 2 therapy in advanced renal cancer and malignant melanoma. Margolin, K., Atkins, M., Sparano, J., Sosman, J., Weiss, G., Lotze, M., Doroshow, J., Mier, J., O'Boyle, K., Fisher, R., Campbell, E., Rubin, J., Federighi, D., Bursten, S. Clin. Cancer Res. (1997) [Pubmed]
  13. Comparison of spontaneous frontal EMG, EEG power spectrum and bispectral index to monitor propofol drug effect and emergence. Struys, M., Versichelen, L., Mortier, E., Ryckaert, D., De Mey, J.C., De Deyne, C., Rolly, G. Acta anaesthesiologica Scandinavica. (1998) [Pubmed]
  14. Counterregulation of chromatin deacetylation and histone deacetylase occupancy at the integrated promoter of human immunodeficiency virus type 1 (HIV-1) by the HIV-1 repressor YY1 and HIV-1 activator Tat. He, G., Margolis, D.M. Mol. Cell. Biol. (2002) [Pubmed]
  15. CRTR-1, a developmentally regulated transcriptional repressor related to the CP2 family of transcription factors. Rodda, S., Sharma, S., Scherer, M., Chapman, G., Rathjen, P. J. Biol. Chem. (2001) [Pubmed]
  16. Mitogen-activated protein kinases regulate LSF occupancy at the human immunodeficiency virus type 1 promoter. Ylisastigui, L., Kaur, R., Johnson, H., Volker, J., He, G., Hansen, U., Margolis, D. J. Virol. (2005) [Pubmed]
  17. Hemoglobin switching in man and chicken is mediated by a heteromeric complex between the ubiquitous transcription factor CP2 and a developmentally specific protein. Jane, S.M., Nienhuis, A.W., Cunningham, J.M. EMBO J. (1995) [Pubmed]
  18. The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1. Zambrano, N., Minopoli, G., de Candia, P., Russo, T. J. Biol. Chem. (1998) [Pubmed]
  19. Identification and characterization of four novel peptide motifs that recognize distinct regions of the transcription factor CP2. Kang, H.C., Chung, B.M., Chae, J.H., Yang, S.I., Kim, C.G., Kim, C.G. FEBS J. (2005) [Pubmed]
  20. CP2 binding to the promoter is essential for the enhanced transcription of globin genes in erythroid cells. Chae, J.H., Kim, C.G. Mol. Cells (2003) [Pubmed]
  21. Specific stimulation of simian virus 40 late transcription in vitro by a cellular factor binding the simian virus 40 21-base-pair repeat promoter element. Kim, C.H., Heath, C., Bertuch, A., Hansen, U. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  22. Human mast cell carboxypeptidase. Selective localization to MCTC cells. Irani, A.M., Goldstein, S.M., Wintroub, B.U., Bradford, T., Schwartz, L.B. J. Immunol. (1991) [Pubmed]
  23. Activation of the human PAX6 gene through the exon 1 enhancer by transcription factors SEF and Sp1. Zheng, J.B., Zhou, Y.H., Maity, T., Liao, W.S., Saunders, G.F. Nucleic Acids Res. (2001) [Pubmed]
  24. A novel tricyclic pyrone compound ameliorates cell death associated with intracellular amyloid-beta oligomeric complexes. Maezawa, I., Hong, H.S., Wu, H.C., Battina, S.K., Rana, S., Iwamoto, T., Radke, G.A., Pettersson, E., Martin, G.M., Hua, D.H., Jin, L.W. J. Neurochem. (2006) [Pubmed]
  25. Molecular cloning of the alpha-globin transcription factor CP2. Lim, L.C., Swendeman, S.L., Sheffery, M. Mol. Cell. Biol. (1992) [Pubmed]
  26. Intracerebral dynamics of saccade generation in the human frontal eye field and supplementary eye field. Lachaux, J.P., Hoffmann, D., Minotti, L., Berthoz, A., Kahane, P. Neuroimage (2006) [Pubmed]
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