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F9  -  coagulation factor IX

Mus musculus

Synonyms: AW111646, Cf-9, Cf9, Christmas factor, Coagulation factor IX
 
 
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Disease relevance of F9

 

High impact information on F9

 

Chemical compound and disease context of F9

 

Biological context of F9

 

Anatomical context of F9

 

Associations of F9 with chemical compounds

  • We demonstrated that coagulation factor IX and complement component C4-binding protein can bind the Ad fiber knob domain and provide a bridge for virus uptake through cell surface heparan sulfate proteoglycans and low-density lipoprotein receptor-related protein [20].
  • The REX-1 mRNA decrease did not result from the reduction in cell growth rate associated with the differentiation process, since the REX-1 mRNA level did not decline in F9 cells that were partially growth arrested after 48 h of isoleucine deprivation [2].
  • A full-length cDNA clone for mouse N-acetylglucosamine (beta 1-4)galactosyltransferase (beta 1-4GT) [EC 2.4.1.90] and several clones diverged from the beta 1-4GT cDNA were isolated from a mouse F9 cDNA library and then sequenced [21].
 

Other interactions of F9

  • Despite this short distance we were able to order Mcf-2 and Cf-9 relative to one another and other genes in this region [15].
  • An additional 128 progeny have been screened for recombination events between Cf-9 and Dmd [22].
  • In contrast to results in F9 cells, we have been unable thus far to detect REX-1 mRNA in day 7.5 to 12.5 mouse embryo RNA samples or in the P19 teratocarcinoma stem cell line [2].
  • Transcripts for both IGF-I and IGF-II ligands were also detectable in the embryo and F9 RNA samples, but transcripts for insulin ligand were undetectable in either set of material [23].
  • Comparison of the cDNA and genomic sequences indicates that the youngest subgroup of A-type L1 elements is preferentially transcribed in F9 cells [24].
 

Analytical, diagnostic and therapeutic context of F9

References

  1. Targeted inactivation of the coagulation factor IX gene causes hemophilia B in mice. Kundu, R.K., Sangiorgi, F., Wu, L.Y., Kurachi, K., Anderson, W.F., Maxson, R., Gordon, E.M. Blood (1998) [Pubmed]
  2. Expression of REX-1, a gene containing zinc finger motifs, is rapidly reduced by retinoic acid in F9 teratocarcinoma cells. Hosler, B.A., LaRosa, G.J., Grippo, J.F., Gudas, L.J. Mol. Cell. Biol. (1989) [Pubmed]
  3. Effect of silencer on polyomavirus DNA replication. Ariizumi, K., Takahashi, H., Nakamura, M., Ariga, H. Mol. Cell. Biol. (1989) [Pubmed]
  4. Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity. Häkli, M., Lorick, K.L., Weissman, A.M., Jänne, O.A., Palvimo, J.J. FEBS Lett. (2004) [Pubmed]
  5. Cloning, sequencing, and expression of the gene encoding the Clostridium stercorarium xylanase C in Escherichia coli. Ali, M.K., Fukumura, M., Sakano, K., Karita, S., Kimura, T., Sakka, K., Ohmiya, K. Biosci. Biotechnol. Biochem. (1999) [Pubmed]
  6. Evidence for gene transfer and expression of factor IX in haemophilia B patients treated with an AAV vector. Kay, M.A., Manno, C.S., Ragni, M.V., Larson, P.J., Couto, L.B., McClelland, A., Glader, B., Chew, A.J., Tai, S.J., Herzog, R.W., Arruda, V., Johnson, F., Scallan, C., Skarsgard, E., Flake, A.W., High, K.A. Nat. Genet. (2000) [Pubmed]
  7. Induction of immune tolerance to coagulation factor IX antigen by in vivo hepatic gene transfer. Mingozzi, F., Liu, Y.L., Dobrzynski, E., Kaufhold, A., Liu, J.H., Wang, Y., Arruda, V.R., High, K.A., Herzog, R.W. J. Clin. Invest. (2003) [Pubmed]
  8. Prevention of cytotoxic T lymphocyte responses to factor IX-expressing hepatocytes by gene transfer-induced regulatory T cells. Dobrzynski, E., Fitzgerald, J.C., Cao, O., Mingozzi, F., Wang, L., Herzog, R.W. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  9. The Malmö polymorphism of coagulation factor IX, an immunologic polymorphism due to dimorphism of residue 148 that is in linkage disequilibrium with two other F.IX polymorphisms. Graham, J.B., Lubahn, D.B., Lord, S.T., Kirshtein, J., Nilsson, I.M., Wallmark, A., Ljung, R., Frazier, L.D., Ware, J.L., Lin, S.W. Am. J. Hum. Genet. (1988) [Pubmed]
  10. The effects of intrinsic pathway protease deficiencies on plasminogen-deficient mice. Cheng, Q., Zhao, Y., Lawson, W.E., Polosukhin, V.V., Johnson, J.E., Blackwell, T.S., Gailani, D. Blood (2005) [Pubmed]
  11. Mouse cellular retinoic acid binding protein: cloning, complementary DNA sequence, and messenger RNA expression during the retinoic acid-induced differentiation of F9 wild type and RA-3-10 mutant teratocarcinoma cells. Stoner, C.M., Gudas, L.J. Cancer Res. (1989) [Pubmed]
  12. Risk and prevention of anti-factor IX formation in AAV-mediated gene transfer in the context of a large deletion of F9. Fields, P.A., Arruda, V.R., Armstrong, E., Chu, K., Mingozzi, F., Hagstrom, J.N., Herzog, R.W., High, K.A. Mol. Ther. (2001) [Pubmed]
  13. Mapping of FMR1, the gene implicated in fragile X-linked mental retardation, on the mouse X chromosome. Laval, S.H., Blair, H.J., Hirst, M.C., Davies, K.E., Boyd, Y. Genomics (1992) [Pubmed]
  14. The properdin structural locus (Pfc) lies close to the locus for tissue inhibitor of metallothionine proteases (Timp) on the mouse X chromosome. Laval, S.H., Chen, Z.Y., Boyd, Y. Genomics (1991) [Pubmed]
  15. Localization of the mouse Mcf-2 (Dbl) protooncogene within a conserved linkage group on the mouse X chromosome. Grant, S.G., Mattei, M.G., Galland, F., Stephenson, D.A., Keitz, B.T., Birnbaum, D., Chapman, V.M. Cytogenet. Cell Genet. (1990) [Pubmed]
  16. Creation of a mouse expressing defective human factor IX. Jin, D.Y., Zhang, T.P., Gui, T., Stafford, D.W., Monahan, P.E. Blood (2004) [Pubmed]
  17. Overexpression of uvomorulin in a compaction-negative F9 mutant cell line. Calogero, A., Samuels, M., Darland, T., Edwards, S.A., Kemler, R., Adamson, E.D. Dev. Biol. (1991) [Pubmed]
  18. Factors influencing in vivo transduction by recombinant adeno-associated viral vectors expressing the human factor IX cDNA. Nathwani, A.C., Davidoff, A., Hanawa, H., Zhou, J.F., Vanin, E.F., Nienhuis, A.W. Blood (2001) [Pubmed]
  19. Capture and expansion of bone marrow-derived mesenchymal progenitor cells with a transforming growth factor-beta1-von Willebrand's factor fusion protein for retrovirus-mediated delivery of coagulation factor IX. Gordon, E.M., Skotzko, M., Kundu, R.K., Han, B., Andrades, J., Nimni, M., Anderson, W.F., Hall, F.L. Hum. Gene Ther. (1997) [Pubmed]
  20. Adenovirus binding to blood factors results in liver cell infection and hepatotoxicity. Shayakhmetov, D.M., Gaggar, A., Ni, S., Li, Z.Y., Lieber, A. J. Virol. (2005) [Pubmed]
  21. Cloning and sequencing of a full-length cDNA of mouse N-acetylglucosamine (beta 1-4)galactosyltransferase. Nakazawa, K., Ando, T., Kimura, T., Narimatsu, H. J. Biochem. (1988) [Pubmed]
  22. Genetic mapping of the mouse X chromosome in the region homologous to human Xq27-Xq28. Herman, G.E., Faust, C.J., Darlison, M.G., Barnard, E.A. Genomics (1991) [Pubmed]
  23. Expression of genes for insulin and insulin-like growth factors and receptors in early postimplantation mouse embryos and embryonal carcinoma cells. Telford, N.A., Hogan, A., Franz, C.R., Schultz, G.A. Mol. Reprod. Dev. (1990) [Pubmed]
  24. Strand-specific LINE-1 transcription in mouse F9 cells originates from the youngest phylogenetic subgroup of LINE-1 elements. Schichman, S.A., Severynse, D.M., Edgell, M.H., Hutchison, C.A. J. Mol. Biol. (1992) [Pubmed]
  25. A coagulation factor IX-deficient mouse model for human hemophilia B. Lin, H.F., Maeda, N., Smithies, O., Straight, D.L., Stafford, D.W. Blood (1997) [Pubmed]
  26. Improved muscle-derived expression of human coagulation factor IX from a skeletal actin/CMV hybrid enhancer/promoter. Hagstrom, J.N., Couto, L.B., Scallan, C., Burton, M., McCleland, M.L., Fields, P.A., Arruda, V.R., Herzog, R.W., High, K.A. Blood (2000) [Pubmed]
  27. Therapeutic levels of factor IX expression using a muscle-specific promoter and adeno-associated virus serotype 1 vector. Liu, Y.L., Mingozzi, F., Rodriguéz-Colôn, S.M., Joseph, S., Dobrzynski, E., Suzuki, T., High, K.A., Herzog, R.W. Hum. Gene Ther. (2004) [Pubmed]
 
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