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Gene Review

TSTA3  -  tissue specific transplantation antigen P35B

Homo sapiens

Synonyms: FX, GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase, GDP-L-fucose synthase, P35B, Protein FX, ...
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Disease relevance of TSTA3


High impact information on TSTA3


Chemical compound and disease context of TSTA3


Biological context of TSTA3

  • The reported P35B cDNA contains an open reading frame (ORF) of 813 bp and encodes a putative protein of 271 amino acids (30 kD), whereas FX protein is 320 amino acids in length (35.81 kD, in good agreement with previous studies) [6].
  • Recently, on the basis of partial amino acid sequence, it proved to be the human homolog of the murine protein P35B, a tumor rejection antigen [1].
  • This latter finding obviously favors the conclusion that "autosomal" rather than "X-linked" genes are involved in the determination of the FX levels [7].
  • In this family, two differently affected FX genes are present, leading to double heterozygosity of the proposita and thus excluding consanguinity of parents [8].
  • Preliminary data indicated that the levels of this protein are significantly increased in hemizygotes, heterozygotes, and homozygotes for the G6PD Mediterranean mutant, thus raising the question of whether or not the individual variation in FX levels is more or less directly influenced by X-linked genes [7].

Anatomical context of TSTA3

  • It was also shown that the FX enzyme regulated important interaction parameters between these cancer cells and endothelial cells [2].
  • To address these limitations, we developed a flow cytometric assay to directly measure the binding of FX to monocytes in whole blood [9].
  • The FX enzyme is a functional component of lymphocyte activation [10].
  • From a panel of 17 reactive hybridomas to FX, 3 were selected for further characterisation [11].
  • Four Irish children with severe FX deficiency presented with umbilical cord bleeding [12].

Associations of TSTA3 with chemical compounds


Other interactions of TSTA3

  • These results suggest that metabolites generated in this pathway may participate in the transcriptional regulation of the FX protein and possibly the GMD protein [13].
  • The recombinant GFS was a homodimer with an optimum pH of 8 [15].
  • Upon activation, monocytes express the alphaMbeta2 integrin CD11b/CD18, which has a binding site for the plasma protein FX [9].

Analytical, diagnostic and therapeutic context of TSTA3

  • Mapping of the genes encoding tum- transplantation antigens P91A, P35B, and P198 [16].
  • Neonatal intramuscular injection resulted in expression of hFX at 248 ng/ml (3.1% of normal), which derived from both liver and muscle [17].
  • We conclude that neonatal gene therapy with an AAV vector with the CMV-beta-actin promoter might correct hemophilia due to hFX deficiency [17].
  • A radioimmunoassay (RIA) demonstrated a 5,100-fold increase in the levels of FX activation peptide after exposure to sarcoma extract [18].
  • The mutation causing the Glu102Lys substitution was introduced by site directed mutagenesis into a wild-type FX cDNA, and recombinant protein was expressed in HEK 293 cells [19].


  1. Synthesis of GDP-L-fucose by the human FX protein. Tonetti, M., Sturla, L., Bisso, A., Benatti, U., De Flora, A. J. Biol. Chem. (1996) [Pubmed]
  2. Tumor-microenvironment interactions: the fucose-generating FX enzyme controls adhesive properties of colorectal cancer cells. Zipin, A., Israeli-Amit, M., Meshel, T., Sagi-Assif, O., Yron, I., Lifshitz, V., Bacharach, E., Smorodinsky, N.I., Many, A., Czernilofsky, P.A., Morton, D.L., Witz, I.P. Cancer Res. (2004) [Pubmed]
  3. Relationship between elevated FX expression and increased production of GDP-L-fucose, a common donor substrate for fucosylation in human hepatocellular carcinoma and hepatoma cell lines. Noda, K., Miyoshi, E., Gu, J., Gao, C.X., Nakahara, S., Kitada, T., Honke, K., Suzuki, K., Yoshihara, H., Yoshikawa, K., Kawano, K., Tonetti, M., Kasahara, A., Hori, M., Hayashi, N., Taniguchi, N. Cancer Res. (2003) [Pubmed]
  4. Factor XSanto Domingo. Evidence that the severe clinical phenotype arises from a mutation blocking secretion. Watzke, H.H., Wallmark, A., Hamaguchi, N., Giardina, P., Stafford, D.W., High, K.A. J. Clin. Invest. (1991) [Pubmed]
  5. Therapeutic levels of functional human factor X in rats after retroviral-mediated hepatic gene therapy. Le, M., Okuyama, T., Cai, S.R., Kennedy, S.C., Bowling, W.M., Flye, M.W., Ponder, K.P. Blood (1997) [Pubmed]
  6. Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B. Camardella, L., Carratore, V., Ciardiello, M.A., Damonte, G., Benatti, U., De Flora, A. Blood (1995) [Pubmed]
  7. Genetic variation in the quantitative levels of an NADP (H)-binding protein (FX) in human erythrocytes. Lenzerini, L., Benatti, U., Morelli, A., Pontremoli, S., De Flora, A., Piazza, A., Rinaldi, A., Filippi, G., Siniscalco, M. Blood (1981) [Pubmed]
  8. Partial gene deletion in a family with factor X deficiency. Bernardi, F., Marchetti, G., Patracchini, P., Volinia, S., Gemmati, D., Simioni, P., Girolami, A. Blood (1989) [Pubmed]
  9. A flow cytometric method for determining the binding of coagulation factor X to monocytes in whole human blood. Le Guyader, A., Davis-Gorman, G., Copeland, J.G., McDonagh, P.F. J. Immunol. Methods (2004) [Pubmed]
  10. The FX enzyme is a functional component of lymphocyte activation. Eshel, R., Besser, M., Zanin, A., Sagi-Assif, O., Witz, I.P. Cell. Immunol. (2001) [Pubmed]
  11. Characterisation of monoclonal antibodies to human factor X/Xa. Initial observations with a quantitative ELISA procedure. Hoad, R.B., Geczy, C.L. J. Immunol. Methods (1991) [Pubmed]
  12. The role of primary prophylactic factor replacement therapy in children with severe factor X deficiency. McMahon, C., Smith, J., Goonan, C., Byrne, M., Smith, O.P. Br. J. Haematol. (2002) [Pubmed]
  13. Molecular cloning and expression of GDP-D-mannose-4,6-dehydratase, a key enzyme for fucose metabolism defective in Lec13 cells. Ohyama, C., Smith, P.L., Angata, K., Fukuda, M.N., Lowe, J.B., Fukuda, M. J. Biol. Chem. (1998) [Pubmed]
  14. Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution of GDP-fucose biosynthesis in vitro. Sullivan, F.X., Kumar, R., Kriz, R., Stahl, M., Xu, G.Y., Rouse, J., Chang, X.J., Boodhoo, A., Potvin, B., Cumming, D.A. J. Biol. Chem. (1998) [Pubmed]
  15. Identification and characterization of GDP-d-mannose 4,6-dehydratase and GDP-l-fucose snthetase in a GDP-l-fucose biosynthetic gene cluster from Helicobacter pylori. Wu, B., Zhang, Y., Wang, P.G. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  16. Mapping of the genes encoding tum- transplantation antigens P91A, P35B, and P198. Dyson, P.J., de Smet, C., Knight, A.M., Simon-Chazottes, D., Guénet, J.L., Boon, T. Immunogenetics (1992) [Pubmed]
  17. CMV-beta-actin promoter directs higher expression from an adeno-associated viral vector in the liver than the cytomegalovirus or elongation factor 1 alpha promoter and results in therapeutic levels of human factor X in mice. Xu, L., Daly, T., Gao, C., Flotte, T.R., Song, S., Byrne, B.J., Sands, M.S., Parker Ponder, K. Hum. Gene Ther. (2001) [Pubmed]
  18. The production of a factor X activator by a methylcholanthrene-induced rat fibrosarcoma. Pangasnan, R.S., Devereux, D., DeCunzo, L.P., Karp, G.I. Thromb. Haemost. (1992) [Pubmed]
  19. The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). Forberg, E., Huhmann, I., Jimenez-Boj, E., Watzke, H.H. Thromb. Haemost. (2000) [Pubmed]
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