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Gene Review

TPT1  -  tumor protein, translationally-controlled 1

Homo sapiens

Synonyms: Fortilin, HRF, Histamine-releasing factor, TCTP, Translationally-controlled tumor protein, ...
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Disease relevance of TPT1


Psychiatry related information on TPT1


High impact information on TPT1


Chemical compound and disease context of TPT1


Biological context of TPT1

  • Recombinant placental TPT1 bound calcium in vitro, while downregulation of the protein levels by siRNA in HTR-8/SVneo cells was associated with a reduced cellular calcium-uptake activity and buffering capacity [13].
  • The present study aimed to evaluate the expression of TPT1 in the human placenta and to examine the functional role of the protein in the calcium binding and homeostasis of trophoblast cells [13].
  • TPT1 expression significantly increased during gestation, with the higher protein and mRNA levels reached at term [13].
  • TPT1 protein and mRNA were detected in first-trimester and term placenta [13].
  • Inhibition of TCTP expression by anti-sense cDNA or small interfering RNA molecules results in suppression of the malignant phenotype and in cellular reorganization, similar to the effect of SIAH-1 [14].

Anatomical context of TPT1


Associations of TPT1 with chemical compounds

  • Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A [18].
  • TCTP (also called histamine-releasing factor) has been described previously as a secreted protein that participates in inflammatory responses by promoting the release of histamine [15].
  • Antiapoptotic protein partners fortilin and MCL1 independently protect cells from 5-fluorouracil-induced cytotoxicity [19].
  • Secondary structure predictions and gel electrophoretic mobility investigations on P23/TCTP transcripts confirmed the potential of this mRNA to form extensive secondary structure [20].
  • Plk phosphorylates TCTP on two serine residues in vitro and cofractionates with the majority of kinase activity toward TCTP in mitotic cell lysates [21].
  • A crystal structure of the E12V mutant hTCTP, which lacks the guanine nucleotide exchange factor activity, shows that the deficiency appears to be caused by loss of a salt-bridging interaction with Lys-45 of hRheb [22].

Physical interactions of TPT1

  • In vitro and in vivo studies confirmed that TCTP bound specifically eEF1Bbeta and eEF1A [18].
  • Fortilin specifically interacted with MCL1 both in vitro and in vivo [16].
  • We screened a rat skeletal muscle cDNA library using yeast two-hybrid system and found that TCTP interacts with the third large cytoplasmic domain of alpha1 as well as alpha2 isoforms of Na,K-ATPase, believed involved in the regulation of Na,K-ATPase activity [2].

Regulatory relationships of TPT1


Other interactions of TPT1


Analytical, diagnostic and therapeutic context of TPT1

  • Additionally, DNA microarray data classifies TCTP (HrHRF) as co-regulated with ribosomal proteins and recent structural analysis of TCTP (HrHRF) relates it to a guanine nucleotide-free chaperone [27].
  • The intracellular localization of fortilin was predominantly nuclear and identical to that of MCL1, as shown by immunostaining and confocal microscopy analysis [16].
  • Western blot analysis using anti-fortilin antibody showed more extensive expression in cancerous cell lines (H1299, MCF-7, and A549) than in cell lines derived from normal tissue (HEK293) [1].
  • Sequence analysis of fortilin revealed it to be a 172-amino acid polypeptide highly conserved from mammals to plants [1].
  • Northern blot analysis showed the fortilin message to be ubiquitous in normal tissue but especially abundant in the liver, kidney, and small intestine [1].


  1. Characterization of fortilin, a novel antiapoptotic protein. Li, F., Zhang, D., Fujise, K. J. Biol. Chem. (2001) [Pubmed]
  2. Translationally controlled tumor protein interacts with the third cytoplasmic domain of Na,K-ATPase alpha subunit and inhibits the pump activity in HeLa cells. Jung, J., Kim, M., Kim, M.J., Kim, J., Moon, J., Lim, J.S., Kim, M., Lee, K. J. Biol. Chem. (2004) [Pubmed]
  3. Translationally controlled tumor protein: a protein identified in several nontumoral cells including erythrocytes. Sanchez, J.C., Schaller, D., Ravier, F., Golaz, O., Jaccoud, S., Belet, M., Wilkins, M.R., James, R., Deshusses, J., Hochstrasser, D. Electrophoresis (1997) [Pubmed]
  4. Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: expression, distribution, and calcium binding activity. Arcuri, F., Papa, S., Carducci, A., Romagnoli, R., Liberatori, S., Riparbelli, M.G., Sanchez, J.C., Tosi, P., del Vecchio, M.T. Prostate (2004) [Pubmed]
  5. Decreased brain histamine-releasing factor protein in patients with Down syndrome and Alzheimer's disease. Kim, S.H., Cairns, N., Fountoulakisc, M., Lubec, G. Neurosci. Lett. (2001) [Pubmed]
  6. Spontaneous release of histamine from basophils and histamine-releasing factor in patients with atopic dermatitis and food hypersensitivity. Sampson, H.A., Broadbent, K.R., Bernhisel-Broadbent, J. N. Engl. J. Med. (1989) [Pubmed]
  7. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Freeman, B.C., Toft, D.O., Morimoto, R.I. Science (1996) [Pubmed]
  8. Molecular identification of an IgE-dependent histamine-releasing factor. MacDonald, S.M., Rafnar, T., Langdon, J., Lichtenstein, L.M. Science (1995) [Pubmed]
  9. Large-cell anaplastic lymphoma-specific translocation (t[2;5] [p23;q35]) in Hodgkin's disease: indication of a common pathogenesis? Orscheschek, K., Merz, H., Hell, J., Binder, T., Bartels, H., Feller, A.C. Lancet (1995) [Pubmed]
  10. The role of the adenovirus protease on virus entry into cells. Greber, U.F., Webster, P., Weber, J., Helenius, A. EMBO J. (1996) [Pubmed]
  11. Heterologous expression and characterization of the human R-ras gene product. Lowe, D.G., Goeddel, D.V. Mol. Cell. Biol. (1987) [Pubmed]
  12. Increased expression of IgE-dependent histamine-releasing factor in endometriotic implants. Oikawa, K., Kosugi, Y., Ohbayashi, T., Kameta, A., Isaka, K., Takayama, M., Kuroda, M., Mukai, K. J. Pathol. (2003) [Pubmed]
  13. The translationally controlled tumor protein is a novel calcium binding protein of the human placenta and regulates calcium handling in trophoblast cells. Arcuri, F., Papa, S., Meini, A., Carducci, A., Romagnoli, R., Bianchi, L., Riparbelli, M.G., Sanchez, J.C., Palmi, M., Tosi, P., Cintorino, M. Biol. Reprod. (2005) [Pubmed]
  14. Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1. Tuynder, M., Susini, L., Prieur, S., Besse, S., Fiucci, G., Amson, R., Telerman, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  15. TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway. Amzallag, N., Passer, B.J., Allanic, D., Segura, E., Théry, C., Goud, B., Amson, R., Telerman, A. J. Biol. Chem. (2004) [Pubmed]
  16. Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone. Zhang, D., Li, F., Weidner, D., Mnjoyan, Z.H., Fujise, K. J. Biol. Chem. (2002) [Pubmed]
  17. Inhibition of cytokine gene transcription by the human recombinant histamine-releasing factor in human T lymphocytes. Vonakis, B.M., Sora, R., Langdon, J.M., Casolaro, V., MacDonald, S.M. J. Immunol. (2003) [Pubmed]
  18. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Cans, C., Passer, B.J., Shalak, V., Nancy-Portebois, V., Crible, V., Amzallag, N., Allanic, D., Tufino, R., Argentini, M., Moras, D., Fiucci, G., Goud, B., Mirande, M., Amson, R., Telerman, A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  19. Antiapoptotic protein partners fortilin and MCL1 independently protect cells from 5-fluorouracil-induced cytotoxicity. Graidist, P., Phongdara, A., Fujise, K. J. Biol. Chem. (2004) [Pubmed]
  20. The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR. Bommer, U.A., Borovjagin, A.V., Greagg, M.A., Jeffrey, I.W., Russell, P., Laing, K.G., Lee, M., Clemens, M.J. RNA (2002) [Pubmed]
  21. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Yarm, F.R. Mol. Cell. Biol. (2002) [Pubmed]
  22. Molecular basis of the acceleration of the GDP-GTP exchange of human ras homolog enriched in brain by human translationally controlled tumor protein. Dong, X., Yang, B., Li, Y., Zhong, C., Ding, J. J. Biol. Chem. (2009) [Pubmed]
  23. Stimulation of human bronchial epithelial cells by IgE-dependent histamine-releasing factor. Yoneda, K., Rokutan, K., Nakamura, Y., Yanagawa, H., Kondo-Teshima, S., Sone, S. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  24. Monocyte chemotactic and activating factor is a potent histamine-releasing factor for human basophils. Kuna, P., Reddigari, S.R., Rucinski, D., Oppenheim, J.J., Kaplan, A.P. J. Exp. Med. (1992) [Pubmed]
  25. An immunoglobulin E-dependent recombinant histamine-releasing factor induces interleukin-4 secretion from human basophils. Schroeder, J.T., Lichtenstein, L.M., MacDonald, S.M. J. Exp. Med. (1996) [Pubmed]
  26. Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13 secretion by human basophils. Schroeder, J.T., Lichtenstein, L.M., MacDonald, S.M. J. Immunol. (1997) [Pubmed]
  27. Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta). Langdon, J.M., Vonakis, B.M., MacDonald, S.M. Biochim. Biophys. Acta (2004) [Pubmed]
  28. Histamine-releasing activity in supernatants of mononuclear cells: contribution of monocyte chemotactic protein-1 activity compared with IgE-dependent activity. Pasmans, S.G., Aalbers, M., Daha, M.R., Knol, E.F., Jansen, H.M., Aalberse, R.C. J. Allergy Clin. Immunol. (1996) [Pubmed]
  29. Monitoring of gene expression by functional proteomics: response of human lung fibroblast cells to stimulation by endothelin-1. Predic, J., Soskic, V., Bradley, D., Godovac-Zimmermann, J. Biochemistry (2002) [Pubmed]
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